[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1021/bi00393a033; PubMed=2825773 [NCBI, ExPASy, EBI, Israel, Japan] Degen S.J.F., Davie E.W.; "Nucleotide sequence of the gene for human prothrombin."; Biochemistry 26:6165-6177(1987).
[2]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT DYSPROTHROMBINEMIA GLY-72. TISSUE=Blood; DOI=10.1046/j.1365-2516.2003.00838.x; PubMed=14962227 [NCBI, ExPASy, EBI, Israel, Japan] Wang W., Fu Q., Zhou R., Wu W., Ding Q., Hu Y., Wang X., Wang H., Wang Z.; "Prothrombin Shanghai: hypoprothrombinaemia caused by substitution of Gla29 by Gly."; Haemophilia 10:94-97(2004).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-165. TISSUE=Liver, and Mammary gland; DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan] Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; "Complete sequencing and characterization of 21,243 full-length human cDNAs."; Nat. Genet. 36:40-45(2004).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Liver; Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.; Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-165. SeattleSNPs variation discovery resource; Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Liver; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[7]	NUCLEOTIDE SEQUENCE [MRNA] OF 8-622. DOI=10.1021/bi00278a008; PubMed=6305407 [NCBI, ExPASy, EBI, Israel, Japan] Degen S.J.F., McGillivray R.T.A., Davie E.W.; "Characterization of the complementary deoxyribonucleic acid and gene coding for human prothrombin."; Biochemistry 22:2087-2097(1983).
[8]	PROTEIN SEQUENCE OF 44-64. TISSUE=Urine; DOI=10.1007/BF00431548; PubMed=8073540 [NCBI, ExPASy, EBI, Israel, Japan] Suzuki K., Moriyama M., Nakajima C., Kawamura K., Miyazawa K., Tsugawa R., Kikuchi N., Nagata K.; "Isolation and partial characterization of crystal matrix protein as a potent inhibitor of calcium oxalate crystal aggregation: evidence of activation peptide of human prothrombin."; Urol. Res. 22:45-50(1994).
[9]	PROTEIN SEQUENCE OF 44-314. DOI=10.1073/pnas.74.5.1969; PubMed=266717 [NCBI, ExPASy, EBI, Israel, Japan] Walz D.A., Hewett-Emmett D., Seegers W.H.; "Amino acid sequence of human prothrombin fragments 1 and 2."; Proc. Natl. Acad. Sci. U.S.A. 74:1969-1972(1977).
[10]	PROTEIN SEQUENCE OF 315-622. PubMed=873923 [NCBI, ExPASy, EBI, Israel, Japan] Butkowski R.J., Elion J., Downing M.R., Mann K.G.; "Primary structure of human prethrombin 2 and alpha-thrombin."; J. Biol. Chem. 252:4942-4957(1977).
[11]	PROTEOLYTIC PROCESSING. PubMed=3759958 [NCBI, ExPASy, EBI, Israel, Japan] Rabiet M.J., Blashill A., Furie B., Furie B.C.; "Prothrombin fragment 1 X 2 X 3, a major product of prothrombin activation in human plasma."; J. Biol. Chem. 261:13210-13215(1986).
[12]	FUNCTION, AND CHARACTERIZATION. PubMed=2856554 [NCBI, ExPASy, EBI, Israel, Japan] Glenn K.C., Frost G.H., Bergmann J.S., Carney D.H.; "Synthetic peptides bind to high-affinity thrombin receptors and modulate thrombin mitogenesis."; Pept. Res. 1:65-73(1988).
[13]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-121 AND ASN-143, AND MASS SPECTROMETRY. TISSUE=Plasma; DOI=10.1002/pmic.200300556; PubMed=14760718 [NCBI, ExPASy, EBI, Israel, Japan] Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."; Proteomics 4:454-465(2004).
[14]	CHARACTERIZATION OF THE TP508 PEPTIDE. DOI=10.1016/j.orthres.2004.12.005; PubMed=15885491 [NCBI, ExPASy, EBI, Israel, Japan] Li G., Cui Y., McIlmurray L., Allen W.E., Wang H.; "rhBMP-2, rhVEGF(165), rhPTN and thrombin-related peptide, TP508 induce chemotaxis of human osteoblasts and microvascular endothelial cells."; J. Orthop. Res. 23:680-685(2005).
[15]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-121; ASN-143 AND ASN-416, AND MASS SPECTROMETRY. TISSUE=Plasma; DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan] Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.; "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."; J. Proteome Res. 4:2070-2080(2005).
[16]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-416, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1021/pr8008012; PubMed=19159218 [NCBI, ExPASy, EBI, Israel, Japan] Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."; J. Proteome Res. 8:651-661(2009).
[17]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). PubMed=2583108 [NCBI, ExPASy, EBI, Israel, Japan] Bode W., Mayr I., Baumann U., Huber R., Stone S.R., Hofsteenge J.; "The refined 1.9 A crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment."; EMBO J. 8:3467-3475(1989).
[18]	X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH HIRUDIN. PubMed=2369893 [NCBI, ExPASy, EBI, Israel, Japan] Gruetter M.G., Priestle J.P., Rahuel J., Grossenbacher H., Bode W., Hofsteenge J., Stone S.R.; "Crystal structure of the thrombin-hirudin complex: a novel mode of serine protease inhibition."; EMBO J. 9:2361-2365(1990).
[19]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH HIRUDIN. DOI=10.1126/science.2374926; PubMed=2374926 [NCBI, ExPASy, EBI, Israel, Japan] Rydel T.J., Ravichandran K.G., Tulinsky A., Bode W., Huber R., Roitsch C., Fenton J.W. II; "The structure of a complex of recombinant hirudin and human alpha-thrombin."; Science 249:277-280(1990).
[20]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 328-622 IN COMPLEXES WITH HIRUDIN AND SYNTHETIC INHIBITOR. PubMed=8251938 [NCBI, ExPASy, EBI, Israel, Japan] Priestle J.P., Rahuel J., Rink H., Tones M., Gruetter M.G.; "Changes in interactions in complexes of hirudin derivatives and human alpha-thrombin due to different crystal forms."; Protein Sci. 2:1630-1642(1993).
[21]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). PubMed=8071320 [NCBI, ExPASy, EBI, Israel, Japan] Rydel T.J., Yin M., Padmanabhan K.P., Blankenship D.T., Cardin A.D., Correa P.E., Fenton J.W. II, Tulinsky A.; "Crystallographic structure of human gamma-thrombin."; J. Biol. Chem. 269:22000-22006(1994).
[22]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). DOI=10.1093/emboj/16.11.2977; PubMed=9214615 [NCBI, ExPASy, EBI, Israel, Japan] van de Locht A., Bode W., Huber R., le Bonniec B.F., Stone S.R., Esmon C.T., Stubbs M.T.; "The thrombin E192Q-BPTI complex reveals gross structural rearrangements: implications for the interaction with antithrombin and thrombomodulin."; EMBO J. 16:2977-2984(1997).
[23]	X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 328-601. DOI=10.1073/pnas.96.5.1852; PubMed=10051558 [NCBI, ExPASy, EBI, Israel, Japan] Guinto E.R., Caccia S., Rose T., Fuetterer K., Waksman G., di Cera E.; "Unexpected crucial role of residue 225 in serine proteases."; Proc. Natl. Acad. Sci. U.S.A. 96:1852-1857(1999).
[24]	X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 333-621 IN COMPLEX WITH SYNTHETIC INHIBITOR. DOI=10.1006/jmbi.2001.4872; PubMed=11493008 [NCBI, ExPASy, EBI, Israel, Japan] Skordalakes E., Dodson G.G., Green D.S., Goodwin C.A., Scully M.F., Hudson H.R., Kakkar V.V., Deadman J.J.; "Inhibition of human alpha-thrombin by a phosphonate tripeptide proceeds via a metastable pentacoordinated phosphorus intermediate."; J. Mol. Biol. 311:549-555(2001).
[25]	X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 334-620 IN COMPLEX WITH HIRUDIN AND SYNTHETIC INHIBITOR. DOI=10.1039/b602585d; PubMed=16763681 [NCBI, ExPASy, EBI, Israel, Japan] Schweizer E., Hoffmann-Roeder A., Olsen J.A., Seiler P., Obst-Sander U., Wagner B., Kansy M., Banner D.W., Diederich F.; "Multipolar interactions in the D pocket of thrombin: large differences between tricyclic imide and lactam inhibitors."; Org. Biomol. Chem. 4:2364-2375(2006).
[26]	X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 334-621 IN COMPLEX WITH HIRUDIN. DOI=10.1021/ja0735002; PubMed=17685615 [NCBI, ExPASy, EBI, Israel, Japan] Liu C.C., Brustad E., Liu W., Schultz P.G.; "Crystal structure of a biosynthetic sulfo-hirudin complexed to thrombin."; J. Am. Chem. Soc. 129:10648-10649(2007).
[27]	X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 335-621 IN COMPLEX WITH SYNTHETIC INHIBITOR. DOI=10.1016/j.bmcl.2008.01.098; PubMed=18291642 [NCBI, ExPASy, EBI, Israel, Japan] Isaacs R.C.A., Solinsky M.G., Cutrona K.J., Newton C.L., Naylor-Olsen A.M., McMasters D.R., Krueger J.A., Lewis S.D., Lucas B.J., Kuo L.C., Yan Y., Lynch J.J., Lyle E.A.; "Structure-based design of novel groups for use in the P1 position of thrombin inhibitor scaffolds. Part 2: N-acetamidoimidazoles."; Bioorg. Med. Chem. Lett. 18:2062-2066(2008).
[28]	X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 315-622 IN COMPLEX WITH SERPINA5 AND HEPARIN. DOI=10.1073/pnas.0711055105; PubMed=18362344 [NCBI, ExPASy, EBI, Israel, Japan] Li W., Adams T.E., Nangalia J., Esmon C.T., Huntington J.A.; "Molecular basis of thrombin recognition by protein C inhibitor revealed by the 1.6-A structure of the heparin-bridged complex."; Proc. Natl. Acad. Sci. U.S.A. 105:4661-4666(2008).
[29]	VARIANT DYSPROTHROMBINEMIA CYS-314. PubMed=3771562 [NCBI, ExPASy, EBI, Israel, Japan] Rabiet M.-J., Furie B.C., Furie B.; "Molecular defect of prothrombin Barcelona. Substitution of cysteine for arginine at residue 273."; J. Biol. Chem. 261:15045-15048(1986).
[30]	VARIANT DYSPROTHROMBINEMIA ALA-509. PubMed=7792730 [NCBI, ExPASy, EBI, Israel, Japan] Degen S.J.F., McDowell S.A., Sparks L.M., Scharrer I.; "Prothrombin Frankfurt: a dysfunctional prothrombin characterized by substitution of Glu-466 by Ala."; Thromb. Haemost. 73:203-209(1995).
[31]	VARIANTS DYSPROTHROMBINEMIA THR-380 AND HIS-431. PubMed=1421398 [NCBI, ExPASy, EBI, Israel, Japan] Morishita E., Saito M., Kumabashiri I., Asakura H., Matsuda T., Yamaguchi K.; "Prothrombin Himi: a compound heterozygote for two dysfunctional prothrombin molecules (Met-337-->Thr and Arg-388-->His)."; Blood 80:2275-2280(1992).
[32]	VARIANT DYSPROTHROMBINEMIA HIS-314. PubMed=7865694 [NCBI, ExPASy, EBI, Israel, Japan] James H.L., Kim D.J., Zheng D.-Q., Girolami A.; "Prothrombin Padua I: incomplete activation due to an amino acid substitution at a factor Xa cleavage site."; Blood Coagul. Fibrinolysis 5:841-844(1994).
[33]	VARIANT DYSPROTHROMBINEMIA CYS-425. DOI=10.1021/bi00426a013; PubMed=3242619 [NCBI, ExPASy, EBI, Israel, Japan] Henriksen R.A., Mann K.G.; "Identification of the primary structural defect in the dysthrombin thrombin Quick I: substitution of cysteine for arginine-382."; Biochemistry 27:9160-9165(1988).
[34]	VARIANT DYSPROTHROMBINEMIA VAL-601. DOI=10.1021/bi00431a017; PubMed=2719946 [NCBI, ExPASy, EBI, Israel, Japan] Henriksen R.A., Mann K.G.; "Substitution of valine for glycine-558 in the congenital dysthrombin thrombin Quick II alters primary substrate specificity."; Biochemistry 28:2078-2082(1989).
[35]	VARIANT DYSPROTHROMBINEMIA ALA-509. DOI=10.1021/bi00148a005; PubMed=1354985 [NCBI, ExPASy, EBI, Israel, Japan] Miyata T., Aruga R., Umeyama H., Bezeaud A., Guillin M.-C., Iwanaga S.; "Prothrombin Salakta: substitution of glutamic acid-466 by alanine reduces the fibrinogen clotting activity and the esterase activity."; Biochemistry 31:7457-7462(1992).
[36]	VARIANT DYSPROTHROMBINEMIA TRP-461. DOI=10.1021/bi00378a020; PubMed=3567158 [NCBI, ExPASy, EBI, Israel, Japan] Miyata T., Morita T., Inomoto T., Kawauchi S., Shirakami A., Iwanaga S.; "Prothrombin Tokushima, a replacement of arginine-418 by tryptophan that impairs the fibrinogen clotting activity of derived thrombin Tokushima."; Biochemistry 26:1117-1122(1987).
[37]	VARIANT DYSPROTHROMBINEMIA TRP-461. PubMed=3801671 [NCBI, ExPASy, EBI, Israel, Japan] Inomoto T., Shirakami A., Kawauchi S., Shigekiyo T., Saito S., Miyoshi K., Morita T., Iwanaga S.; "Prothrombin Tokushima: characterization of dysfunctional thrombin derived from a variant of human prothrombin."; Blood 69:565-569(1987).
[38]	VARIANT DYSPROTHROMBINEMIA TRP-461. PubMed=1349838 [NCBI, ExPASy, EBI, Israel, Japan] Iwahana H., Yoshimoto K., Shigekiyo T., Shirakami A., Saito S., Itakura M.; "Detection of a single base substitution of the gene for prothrombin Tokushima. The application of PCR-SSCP for the genetic and molecular analysis of dysprothrombinemia."; Int. J. Hematol. 55:93-100(1992).
[39]	VARIANT DYSPROTHROMBINEMIA LYS-200. DOI=10.1111/j.1365-2141.1983.tb02092.x; PubMed=6405779 [NCBI, ExPASy, EBI, Israel, Japan] Board P.G., Shaw D.C.; "Determination of the amino acid substitution in human prothrombin type 3 (157 Glu leads to Lys) and the localization of a third thrombin cleavage site."; Br. J. Haematol. 54:245-254(1983).
[40]	VARIANTS MET-165 AND THR-386. DOI=10.1038/10290; PubMed=10391209 [NCBI, ExPASy, EBI, Israel, Japan] Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.; "Characterization of single-nucleotide polymorphisms in coding regions of human genes."; Nat. Genet. 22:231-238(1999).
[41]	ERRATUM. Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.; Nat. Genet. 23:373-373(1999).
[42]	INVOLVEMENT IN SUSCEPTIBILITY TO ISCHEMIC STROKE. DOI=10.1001/archneur.61.11.1652; PubMed=15534175 [NCBI, ExPASy, EBI, Israel, Japan] Casas J.P., Hingorani A.D., Bautista L.E., Sharma P.; "Meta-analysis of genetic studies in ischemic stroke: thirty-two genes involving approximately 18,000 cases and 58,000 controls."; Arch. Neurol. 61:1652-1661(2004).
[43]	THERAPEUTIC USAGE OF THE TP508 PEPTIDE. DOI=10.1111/j.1524-475X.2006.00181.x; PubMed=17244316 [NCBI, ExPASy, EBI, Israel, Japan] Fife C., Mader J.T., Stone J., Brill L., Satterfield K., Norfleet A., Zwernemann A., Ryaby J.T., Carney D.H.; "Thrombin peptide Chrysalin stimulates healing of diabetic foot ulcers in a placebo-controlled phase I/II study."; Wound Repair Regen. 15:23-34(2007).

Comments

FUNCTION: Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing.
CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B.
INTERACTION:
Q846V4:- (xeno); NbExp=3; IntAct=EBI-297094, EBI-989571;
P07204:THBD; NbExp=1; IntAct=EBI-297094, EBI-941422;
SUBCELLULAR LOCATION: Secreted, extracellular space.
TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
PTM: The gamma-carboxyglutamyl residues, which bind calcium ions, result from the carboxylation of glutamyl residues by a microsomal enzyme, the vitamin K-dependent carboxylase. The modified residues are necessary for the calcium-dependent interaction with a negatively charged phospholipid surface, which is essential for the conversion of prothrombin to thrombin.
DISEASE: Defects in F2 are the cause of various forms of dysprothrombinemia [MIM:176930].
DISEASE: Genetic variations in F2 may be a cause of susceptibility to ischemic stroke [MIM:601367]; also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.
PHARMACEUTICAL: The peptide TP508 also known as Chrysalin (Orthologic) could be used to accelerate repair of both soft and hard tissues.
MISCELLANEOUS: Prothrombin is activated on the surface of a phospholipid membrane that binds the amino end of prothrombin and factors Va and Xa in Ca-dependent interactions; factor Xa removes the activation peptide and cleaves the remaining part into light and heavy chains. The activation process starts slowly because factor V itself has to be activated by the initial, small amounts of thrombin.
MISCELLANEOUS: It is not known whether 1 or 2 smaller activation peptides, with additional cleavage after Arg-314, are released in natural blood clotting.
MISCELLANEOUS: Thrombin can itself cleave the N-terminal fragment (fragment 1) of the prothrombin, prior to its activation by factor Xa.
MISCELLANEOUS: The cleavage after Arg-198, observed in vitro, does not occur in plasma.
SIMILARITY: Belongs to the peptidase S1 family [view classification].
SIMILARITY: Contains 1 Gla (gamma-carboxy-glutamate) domain.
SIMILARITY: Contains 2 kringle domains.
SIMILARITY: Contains 1 peptidase S1 domain [view classification].
WEB RESOURCE: Name=Wikipedia; Note=Thrombin entry; URL="http://en.wikipedia.org/wiki/Thrombin";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=F2";.
WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/f2/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M17262; AAC63054.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ972449; CAJ01369.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK303747; BAG64719.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK312965; BAG35804.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK222775; BAD96495.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK222777; BAD96497.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF478696; AAL77436.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC051332; AAH51332.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
V00595; CAA23842.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00019568; -.

A29351; TBHU.

NP_000497.1; -.

3D structure databases

PDB

1A2C; X-ray; 2.10 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1A3B; X-ray; 1.80 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1A3E; X-ray; 1.85 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1A46; X-ray; 2.12 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1A4W; X-ray; 1.80 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1A5G; X-ray; 2.06 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1A61; X-ray; 2.20 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1ABI; X-ray; 2.30 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1ABJ; X-ray; 2.40 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1AD8; X-ray; 2.00 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1AE8; X-ray; 2.00 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1AFE; X-ray; 2.00 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1AHT; X-ray; 1.60 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1AI8; X-ray; 1.85 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1AIX; X-ray; 2.10 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1AWF; X-ray; 2.20 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1AWH; X-ray; 3.00 A; A/C=328-363, B/D=364-622.	[ExPASy / RCSB / EBI]
1AY6; X-ray; 1.80 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1B5G; X-ray; 2.07 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1B7X; X-ray; 2.10 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
1BA8; X-ray; 1.80 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
1BB0; X-ray; 2.10 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
1BCU; X-ray; 2.00 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1BHX; X-ray; 2.30 A; A=331-360, B=364-510, F=518-622.	[ExPASy / RCSB / EBI]
1BMM; X-ray; 2.60 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1BMN; X-ray; 2.80 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1BTH; X-ray; 2.30 A; H/K=364-622, J/L=328-363.	[ExPASy / RCSB / EBI]
1C1U; X-ray; 1.75 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1C1V; X-ray; 1.98 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1C1W; X-ray; 1.90 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1C4U; X-ray; 2.10 A; 1=328-363, 2=364-622.	[ExPASy / RCSB / EBI]
1C4V; X-ray; 2.10 A; 1=328-363, 2=364-622.	[ExPASy / RCSB / EBI]
1C4Y; X-ray; 2.70 A; 1=328-363, 2=364-622.	[ExPASy / RCSB / EBI]
1C5L; X-ray; 1.47 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1C5N; X-ray; 1.50 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1C5O; X-ray; 1.90 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1CA8; X-ray; 2.10 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
1D3D; X-ray; 2.04 A; A=333-360, B=364-620.	[ExPASy / RCSB / EBI]
1D3P; X-ray; 2.10 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
1D3Q; X-ray; 2.90 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
1D3T; X-ray; 3.00 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
1D4P; X-ray; 2.07 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
1D6W; X-ray; 2.00 A; A=334-620.	[ExPASy / RCSB / EBI]
1D9I; X-ray; 2.30 A; A=334-621.	[ExPASy / RCSB / EBI]
1DE7; X-ray; 2.00 A; H/K=364-622, J/L=328-363.	[ExPASy / RCSB / EBI]
1DIT; X-ray; 2.30 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1DM4; X-ray; 2.50 A; A=328-362, B=363-622.	[ExPASy / RCSB / EBI]
1DOJ; X-ray; 1.70 A; A=328-622.	[ExPASy / RCSB / EBI]
1DWB; X-ray; 3.16 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1DWC; X-ray; 3.00 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1DWD; X-ray; 3.00 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1DWE; X-ray; 3.00 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1DX5; X-ray; 2.30 A; A/B/C/D=328-363, M/N/O/P=364-622.	[ExPASy / RCSB / EBI]
1E0F; X-ray; 3.10 A; A/B/C=328-363, D/E/F=364-622.	[ExPASy / RCSB / EBI]
1EB1; X-ray; 1.80 A; H=364-620, L=335-360.	[ExPASy / RCSB / EBI]
1EOJ; X-ray; 2.10 A; A=332-620.	[ExPASy / RCSB / EBI]
1EOL; X-ray; 2.10 A; A=332-620.	[ExPASy / RCSB / EBI]
1FPC; X-ray; 2.30 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1FPH; X-ray; 2.50 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1G30; X-ray; 2.00 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
1G32; X-ray; 1.90 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
1G37; X-ray; 2.00 A; A=334-620.	[ExPASy / RCSB / EBI]
1GHV; X-ray; 1.85 A; H=364-620, L=328-363.	[ExPASy / RCSB / EBI]
1GHW; X-ray; 1.75 A; H=364-620, L=328-363.	[ExPASy / RCSB / EBI]
1GHX; X-ray; 1.65 A; H=364-620, L=328-363.	[ExPASy / RCSB / EBI]
1GHY; X-ray; 1.85 A; H=364-620, L=328-363.	[ExPASy / RCSB / EBI]
1GJ4; X-ray; 1.81 A; H=364-621, L=328-363.	[ExPASy / RCSB / EBI]
1GJ5; X-ray; 1.73 A; H=364-621, L=328-363.	[ExPASy / RCSB / EBI]
1H8D; X-ray; 1.40 A; H=364-621, L=333-360.	[ExPASy / RCSB / EBI]
1H8I; X-ray; 1.75 A; H=364-622, L=334-360.	[ExPASy / RCSB / EBI]
1HAG; X-ray; 2.00 A; E=328-622.	[ExPASy / RCSB / EBI]
1HAH; X-ray; 2.30 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1HAI; X-ray; 2.40 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1HAO; X-ray; 2.80 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1HAP; X-ray; 2.80 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1HBT; X-ray; 2.00 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1HDT; X-ray; 2.60 A; H=364-622, L=331-363.	[ExPASy / RCSB / EBI]
1HGT; X-ray; 2.20 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1HLT; X-ray; 3.00 A; H/K=364-622, J/L=334-360.	[ExPASy / RCSB / EBI]
1HUT; X-ray; 2.90 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1HXE; X-ray; 2.10 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1HXF; X-ray; 2.10 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1IHS; X-ray; 2.00 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1IHT; X-ray; 2.10 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1JMO; X-ray; 2.20 A; H=363-622, L=315-362.	[ExPASy / RCSB / EBI]
1JOU; X-ray; 1.80 A; A/C/E=315-363, B/D/F=364-622.	[ExPASy / RCSB / EBI]
1JWT; X-ray; 2.50 A; A=328-622.	[ExPASy / RCSB / EBI]
1K21; X-ray; 1.86 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1K22; X-ray; 1.93 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1KTS; X-ray; 2.40 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
1KTT; X-ray; 2.10 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
1LHC; X-ray; 1.95 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1LHD; X-ray; 2.35 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1LHE; X-ray; 2.25 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1LHF; X-ray; 2.40 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1LHG; X-ray; 2.25 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1MH0; X-ray; 2.80 A; A/B=334-620.	[ExPASy / RCSB / EBI]
1MU6; X-ray; 1.99 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
1MU8; X-ray; 2.00 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
1MUE; X-ray; 2.00 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
1NM6; X-ray; 1.80 A; A=335-621.	[ExPASy / RCSB / EBI]
1NO9; X-ray; 1.90 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1NRN; X-ray; 3.10 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1NRO; X-ray; 3.10 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1NRP; X-ray; 3.00 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1NRQ; X-ray; 3.50 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1NRR; X-ray; 2.40 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1NRS; X-ray; 2.40 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1NT1; X-ray; 2.00 A; A=335-621.	[ExPASy / RCSB / EBI]
1NU7; X-ray; 2.20 A; A/E=332-359, B/F=364-622.	[ExPASy / RCSB / EBI]
1NU9; X-ray; 2.20 A; A/D=332-622.	[ExPASy / RCSB / EBI]
1NY2; X-ray; 2.30 A; 1=328-363, 2=364-622.	[ExPASy / RCSB / EBI]
1NZQ; X-ray; 2.18 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1O0D; X-ray; 2.44 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1O2G; X-ray; 1.58 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1O5G; X-ray; 1.75 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1OOK; X-ray; 2.30 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
1OYT; X-ray; 1.67 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1P8V; X-ray; 2.60 A; B=333-361, C=364-622.	[ExPASy / RCSB / EBI]
1PPB; X-ray; 1.92 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1QBV; X-ray; 1.80 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1QHR; X-ray; 2.20 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
1QJ1; X-ray; 2.00 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
1QJ6; X-ray; 2.20 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
1QJ7; X-ray; 2.20 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
1QUR; X-ray; 2.00 A; H=364-620, L=334-360.	[ExPASy / RCSB / EBI]
1RD3; X-ray; 2.50 A; A/C=328-363, B/D=364-622.	[ExPASy / RCSB / EBI]
1RIW; X-ray; 2.04 A; A=328-363, B=364-510, C=518-622.	[ExPASy / RCSB / EBI]
1SB1; X-ray; 1.90 A; H=364-621, L=333-361.	[ExPASy / RCSB / EBI]
1SFQ; X-ray; 1.91 A; A/D=328-363, B/E=364-622.	[ExPASy / RCSB / EBI]
1SG8; X-ray; 2.30 A; A/D=328-363, B/E=364-622.	[ExPASy / RCSB / EBI]
1SGI; X-ray; 2.30 A; A/D=328-363, B/E=364-622.	[ExPASy / RCSB / EBI]
1SHH; X-ray; 1.55 A; A/D=328-363, B/E=364-622.	[ExPASy / RCSB / EBI]
1SL3; X-ray; 1.81 A; A=335-621.	[ExPASy / RCSB / EBI]
1SR5; X-ray; 3.10 A; B=328-363, C=364-622.	[ExPASy / RCSB / EBI]
1T4U; X-ray; 2.00 A; H=364-622, L=334-359.	[ExPASy / RCSB / EBI]
1T4V; X-ray; 2.00 A; H=364-622, L=334-359.	[ExPASy / RCSB / EBI]
1TA2; X-ray; 2.30 A; A=335-621.	[ExPASy / RCSB / EBI]
1TA6; X-ray; 1.90 A; A=335-621.	[ExPASy / RCSB / EBI]
1TB6; X-ray; 2.50 A; H=364-622, L=315-363.	[ExPASy / RCSB / EBI]
1TBZ; X-ray; 2.30 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1THP; X-ray; 2.10 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
1THR; X-ray; 2.30 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1THS; X-ray; 2.20 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1TMB; X-ray; 2.30 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1TMT; X-ray; 2.20 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1TMU; X-ray; 2.50 A; H=364-622, L=333-360.	[ExPASy / RCSB / EBI]
1TOM; X-ray; 1.80 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1TQ0; X-ray; 2.80 A; A/C=333-363, B/D=364-620.	[ExPASy / RCSB / EBI]
1TQ7; X-ray; 2.40 A; A=320-363, B=364-620.	[ExPASy / RCSB / EBI]
1TWX; X-ray; 2.40 A; A=334-361, B=364-622.	[ExPASy / RCSB / EBI]
1UMA; X-ray; 2.00 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1UVS; X-ray; 2.80 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1VR1; X-ray; 1.90 A; H=364-620, L=334-360.	[ExPASy / RCSB / EBI]
1VZQ; X-ray; 1.54 A; H=364-620, L=334-360.	[ExPASy / RCSB / EBI]
1W7G; X-ray; 1.65 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
1WAY; X-ray; 2.02 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
1WBG; X-ray; 2.20 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
1XM1; X-ray; 2.30 A; A=328-622.	[ExPASy / RCSB / EBI]
1XMN; X-ray; 1.85 A; A/C/E/G=328-363, B/D/F/H=364-622.	[ExPASy / RCSB / EBI]
1YPE; X-ray; 1.81 A; H=364-620, L=334-360.	[ExPASy / RCSB / EBI]
1YPG; X-ray; 1.80 A; H=364-620, L=334-360.	[ExPASy / RCSB / EBI]
1YPJ; X-ray; 1.78 A; H=364-620, L=334-360.	[ExPASy / RCSB / EBI]
1YPK; X-ray; 1.78 A; H=364-620, L=334-360.	[ExPASy / RCSB / EBI]
1YPL; X-ray; 1.85 A; H=364-620, L=334-360.	[ExPASy / RCSB / EBI]
1YPM; X-ray; 1.85 A; H=364-620, L=334-360.	[ExPASy / RCSB / EBI]
1Z71; X-ray; 1.80 A; A=335-621.	[ExPASy / RCSB / EBI]
1Z8I; X-ray; 2.00 A; A=324-361, B=364-622.	[ExPASy / RCSB / EBI]
1Z8J; X-ray; 2.00 A; A=322-361, B=364-622.	[ExPASy / RCSB / EBI]
1ZGI; X-ray; 2.20 A; A=335-621.	[ExPASy / RCSB / EBI]
1ZGV; X-ray; 2.20 A; A=335-621.	[ExPASy / RCSB / EBI]
1ZRB; X-ray; 1.90 A; A=335-621.	[ExPASy / RCSB / EBI]
2A0Q; X-ray; 1.90 A; A/C=334-363, B/D=364-620.	[ExPASy / RCSB / EBI]
2A2X; X-ray; 2.44 A; H=364-622, L=330-363.	[ExPASy / RCSB / EBI]
2A45; X-ray; 3.65 A; A/D=328-363, B/E=364-622.	[ExPASy / RCSB / EBI]
2AFQ; X-ray; 1.93 A; A/C=332-360, B/D=364-622.	[ExPASy / RCSB / EBI]
2ANK; X-ray; 2.46 A; H=364-622, L=330-363.	[ExPASy / RCSB / EBI]
2ANM; X-ray; 2.40 A; H=364-620, L=328-363.	[ExPASy / RCSB / EBI]
2B5T; X-ray; 2.10 A; A/C=315-363, B/D=364-622.	[ExPASy / RCSB / EBI]
2BDY; X-ray; 1.61 A; A=334-622.	[ExPASy / RCSB / EBI]
2BVR; X-ray; 1.25 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2BVS; X-ray; 1.40 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2BVX; X-ray; 3.20 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2BXT; X-ray; 1.83 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2BXU; X-ray; 2.80 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2C8W; X-ray; 1.96 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
2C8X; X-ray; 2.17 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
2C8Y; X-ray; 2.20 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
2C8Z; X-ray; 2.14 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
2C90; X-ray; 2.25 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
2C93; X-ray; 2.20 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
2CF8; X-ray; 1.30 A; H=364-620, L=334-361.	[ExPASy / RCSB / EBI]
2CF9; X-ray; 1.79 A; H=364-620, L=334-361.	[ExPASy / RCSB / EBI]
2CN0; X-ray; 1.30 A; H=364-620, L=334-361.	[ExPASy / RCSB / EBI]
2FEQ; X-ray; 2.44 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2FES; X-ray; 2.42 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2GDE; X-ray; 2.00 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2GP9; X-ray; 1.87 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
2H9T; X-ray; 2.40 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2HGT; X-ray; 2.20 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2HNT; X-ray; 2.50 A; C=364-433, E=437-517, F=518-622, L=328-363.	[ExPASy / RCSB / EBI]
2HPP; X-ray; 3.30 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2HPQ; X-ray; 3.30 A; H=364-622, L=328-363, P=213-291.	[ExPASy / RCSB / EBI]
2HWL; X-ray; 2.40 A; A/C=328-363, B/D=364-622.	[ExPASy / RCSB / EBI]
2JH0; X-ray; 1.70 A; C=328-363, D=364-622.	[ExPASy / RCSB / EBI]
2JH5; X-ray; 2.50 A; C=328-363, D=364-622.	[ExPASy / RCSB / EBI]
2JH6; X-ray; 2.21 A; C=328-363, D=364-622.	[ExPASy / RCSB / EBI]
2OD3; X-ray; 1.75 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
2PGB; X-ray; 1.54 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
2PGQ; X-ray; 1.80 A; A=319-363, B=364-622.	[ExPASy / RCSB / EBI]
2PKS; X-ray; 2.50 A; A=334-360, B=364-510, C=518-619.	[ExPASy / RCSB / EBI]
2PW8; X-ray; 1.84 A; H=364-621, L=334-360.	[ExPASy / RCSB / EBI]
2R2M; X-ray; 2.10 A; A=334-359, B=364-622.	[ExPASy / RCSB / EBI]
2THF; X-ray; 2.10 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
2UUF; X-ray; 1.26 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
2UUJ; X-ray; 1.32 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
2UUK; X-ray; 1.39 A; A=328-363, B=364-622.	[ExPASy / RCSB / EBI]
2V3H; X-ray; 1.79 A; H=364-620, L=334-361.	[ExPASy / RCSB / EBI]
2V3O; X-ray; 1.79 A; H=364-620, L=334-361.	[ExPASy / RCSB / EBI]
2ZC9; X-ray; 1.58 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2ZDA; X-ray; 1.73 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2ZDV; X-ray; 1.72 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2ZF0; X-ray; 2.20 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2ZFF; X-ray; 1.47 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2ZFP; X-ray; 2.25 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2ZFQ; X-ray; 1.80 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2ZFR; X-ray; 1.85 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2ZG0; X-ray; 1.75 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2ZGB; X-ray; 1.60 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2ZGX; X-ray; 1.80 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2ZHE; X-ray; 2.10 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2ZHF; X-ray; 1.98 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2ZHQ; X-ray; 1.96 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2ZHW; X-ray; 2.02 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2ZI2; X-ray; 1.65 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2ZIQ; X-ray; 1.65 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
2ZNK; X-ray; 1.80 A; L=328-363, H=364-622.	[ExPASy / RCSB / EBI]
2ZO3; X-ray; 1.70 A; L=328-363, H=364-622.	[ExPASy / RCSB / EBI]
3B9F; X-ray; 1.60 A; H=364-622, L=315-363.	[ExPASy / RCSB / EBI]
3BEF; X-ray; 2.20 A; A/D=318-363, B/E=364-622.	[ExPASy / RCSB / EBI]
3BEI; X-ray; 1.55 A; A=320-363, B=364-622.	[ExPASy / RCSB / EBI]
3BF6; X-ray; 2.50 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
3BIU; X-ray; 2.30 A; H=364-620, L=333-361.	[ExPASy / RCSB / EBI]
3BIV; X-ray; 1.80 A; H=364-620, L=333-361.	[ExPASy / RCSB / EBI]
3BV9; X-ray; 1.80 A; B=364-622.	[ExPASy / RCSB / EBI]
3C1K; X-ray; 1.84 A; A=335-621.	[ExPASy / RCSB / EBI]
3C27; X-ray; 2.18 A; A=334-359, B=364-622.	[ExPASy / RCSB / EBI]
3D49; X-ray; 1.50 A; L=328-363, H=364-622.	[ExPASy / RCSB / EBI]
3DD2; X-ray; 1.90 A; H=364-621, L=332-361.	[ExPASy / RCSB / EBI]
3E6P; X-ray; 2.10 A; H=364-622, L=206-363.	[ExPASy / RCSB / EBI]
3EGK; X-ray; 2.20 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
3HAT; X-ray; 2.50 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
3HTC; X-ray; 2.30 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
4HTC; X-ray; 2.30 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
4THN; X-ray; 2.50 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
5GDS; X-ray; 2.10 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
7KME; X-ray; 2.10 A; H=364-622, L=328-363.	[ExPASy / RCSB / EBI]
8KME; X-ray; 2.10 A; 1=328-363, 2=364-622.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1A2C; -.
1A3B; -.
1A3E; -.
1A46; -.
1A4W; -.
1A5G; -.
1A61; -.
1ABI; -.
1ABJ; -.
1AD8; -.
1AE8; -.
1AFE; -.
1AHT; -.
1AI8; -.
1AIX; -.
1AWF; -.
1AWH; -.
1AY6; -.
1B5G; -.
1B7X; -.
1BA8; -.
1BB0; -.
1BCU; -.
1BHX; -.
1BMM; -.
1BMN; -.
1BTH; -.
1C1U; -.
1C1V; -.
1C1W; -.
1C4U; -.
1C4V; -.
1C4Y; -.
1C5L; -.
1C5N; -.
1C5O; -.
1CA8; -.
1D3D; -.
1D3P; -.
1D3Q; -.
1D3T; -.
1D4P; -.
1D6W; -.
1D9I; -.
1DE7; -.
1DIT; -.
1DM4; -.
1DOJ; -.
1DWB; -.
1DWC; -.
1DWD; -.
1DWE; -.
1DX5; -.
1E0F; -.
1EB1; -.
1EOJ; -.
1EOL; -.
1FPC; -.
1FPH; -.
1G30; -.
1G32; -.
1G37; -.
1GHV; -.
1GHW; -.
1GHX; -.
1GHY; -.
1GJ4; -.
1GJ5; -.
1H8D; -.
1H8I; -.
1HAG; -.
1HAH; -.
1HAI; -.
1HAO; -.
1HAP; -.
1HBT; -.
1HDT; -.
1HGT; -.
1HLT; -.
1HUT; -.
1HXE; -.
1HXF; -.
1IHS; -.
1IHT; -.
1JMO; -.
1JOU; -.
1JWT; -.
1K21; -.
1K22; -.
1KTS; -.
1KTT; -.
1LHC; -.
1LHD; -.
1LHE; -.
1LHF; -.
1LHG; -.
1MH0; -.
1MU6; -.
1MU8; -.
1MUE; -.
1NM6; -.
1NO9; -.
1NRN; -.
1NRO; -.
1NRP; -.
1NRQ; -.
1NRR; -.
1NRS; -.
1NT1; -.
1NU7; -.
1NU9; -.
1NY2; -.
1NZQ; -.
1O0D; -.
1O2G; -.
1O5G; -.
1OOK; -.
1OYT; -.
1P8V; -.
1PPB; -.
1QBV; -.
1QHR; -.
1QJ1; -.
1QJ6; -.
1QJ7; -.
1QUR; -.
1RD3; -.
1RIW; -.
1SB1; -.
1SFQ; -.
1SG8; -.
1SGI; -.
1SHH; -.
1SL3; -.
1SR5; -.
1T4U; -.
1T4V; -.
1TA2; -.
1TA6; -.
1TB6; -.
1TBZ; -.
1THP; -.
1THR; -.
1THS; -.
1TMB; -.
1TMT; -.
1TMU; -.
1TOM; -.
1TQ0; -.
1TQ7; -.
1TWX; -.
1UMA; -.
1UVS; -.
1VR1; -.
1VZQ; -.
1W7G; -.
1WAY; -.
1WBG; -.
1XM1; -.
1XMN; -.
1YPE; -.
1YPG; -.
1YPJ; -.
1YPK; -.
1YPL; -.
1YPM; -.
1Z71; -.
1Z8I; -.
1Z8J; -.
1ZGI; -.
1ZGV; -.
1ZRB; -.
2A0Q; -.
2A2X; -.
2A45; -.
2AFQ; -.
2ANK; -.
2ANM; -.
2B5T; -.
2BDY; -.
2BVR; -.
2BVS; -.
2BVX; -.
2BXT; -.
2BXU; -.
2C8W; -.
2C8X; -.
2C8Y; -.
2C8Z; -.
2C90; -.
2C93; -.
2CF8; -.
2CF9; -.
2CN0; -.
2FEQ; -.
2FES; -.
2GDE; -.
2GP9; -.
2H9T; -.
2HGT; -.
2HNT; -.
2HPP; -.
2HPQ; -.
2HWL; -.
2JH0; -.
2JH5; -.
2JH6; -.
2OD3; -.
2PGB; -.
2PGQ; -.
2PKS; -.
2PW8; -.
2R2M; -.
2THF; -.
2UUF; -.
2UUJ; -.
2UUK; -.
2V3H; -.
2V3O; -.
2ZC9; -.
2ZDA; -.
2ZDV; -.
2ZF0; -.
2ZFF; -.
2ZFP; -.
2ZFQ; -.
2ZFR; -.
2ZG0; -.
2ZGB; -.
2ZGX; -.
2ZHE; -.
2ZHF; -.
2ZHQ; -.
2ZHW; -.
2ZI2; -.
2ZIQ; -.
2ZNK; -.
2ZO3; -.
3B9F; -.
3BEF; -.
3BEI; -.
3BF6; -.
3BIU; -.
3BIV; -.
3BV9; -.
3C1K; -.
3C27; -.
3D49; -.
3DD2; -.
3E6P; -.
3EGK; -.
3HAT; -.
3HTC; -.
4HTC; -.
4THN; -.
5GDS; -.
7KME; -.
8KME; -.

SMR

P00734; 207-363.

ModBase

P00734.

Protein-protein interaction databases

DIP

DIP:6115N; -.

IntAct

P00734; 6.

Protein family/group databases

MEROPS

S01.217; -.

PTM databases

GlycoSuiteDB

P00734; -.

Enzyme and pathway databases

BRENDA

3.4.21.5; 247.

Pathway_Interaction_DB

angiopoietinreceptor_pathway; Angiopoietin receptor Tie2-mediated signaling.
hnf3bpathway; FOXA2 and FOXA3 transcription factor networks.
syndecan_4_pathway; Syndecan-4-mediated signaling events.

Reactome

REACT_1069; Post-translational protein modification.
REACT_604; Hemostasis.
REACT_6900; Signaling in Immune system.

2D gel databases

SWISS-2DPAGE

P00734; -.

Organism-specific databases

GC11P046697; -.

HIX0026188; -.

HGNC:3535; F2.

F2.

CAB016780; -.
CAB018650; -.

MIM

176930; gene+phenotype. [NCBI / EBI]
601367; phenotype. [NCBI / EBI]

Orphanet

325; Congenital factor II deficiency.

PharmGKB

PA24406; -.

Gene expression databases

P00734; -.

P00734; -.

HS_F2; -.

ENSG00000180210; Homo sapiens.

Ontologies

GO:0005615;	Cellular component: extracellular space (inferred from direct assay from UniProtKB).
GO:0005886;	Cellular component: plasma membrane (inferred from experiment from Reactome).
GO:0005625;	Cellular component: soluble fraction (traceable author statement from ProtInc).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005102;	Molecular function: receptor binding (inferred from physical interaction from UniProtKB).
GO:0004252;	Molecular function: serine-type endopeptidase activity (inferred from direct assay from UniProtKB).
GO:0003809;	Molecular function: thrombin activity (inferred from direct assay from UniProtKB).
GO:0070053;	Molecular function: thrombospondin receptor activity (inferred from direct assay from UniProtKB).
GO:0006919;	Biological process: activation of caspase activity (traceable author statement from ProtInc).
GO:0006953;	Biological process: acute-phase response (inferred from electronic annotation from UniProtKB-KW).
GO:0007166;	Biological process: cell surface receptor linked signal transduction (inferred from direct assay from UniProtKB).
GO:0042730;	Biological process: fibrinolysis (inferred from direct assay from UniProtKB).
GO:0007275;	Biological process: multicellular organismal development (traceable author statement from ProtInc).
GO:0030168;	Biological process: platelet activation (traceable author statement from UniProtKB).
GO:0030194;	Biological process: positive regulation of blood coagulation (inferred from direct assay from UniProtKB).
GO:0032967;	Biological process: positive regulation of collagen biosynthetic process (inferred from direct assay from UniProtKB).
GO:0001934;	Biological process: positive regulation of protein amino acid phosphorylation (inferred from direct assay from UniProtKB).
GO:0051281;	Biological process: positive regulation of release of sequestered calcium ion into cytosol (inferred from direct assay from UniProtKB).
GO:0006508;	Biological process: proteolysis (traceable author statement from ProtInc).
GO:0051209;	Biological process: release of sequestered calcium ion into cytosol (inferred from direct assay from UniProtKB).
GO:0007262;	Biological process: STAT protein nuclear translocation (traceable author statement from ProtInc).
GO:0007260;	Biological process: tyrosine phosphorylation of STAT protein (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR002383; Coagulation_factor_Gla.
IPR000294; GLA_domain.
IPR000001; Kringle.
IPR018056; Kringle_CS.
IPR018059; Kringle_sub.
IPR018114; Peptidase_S1/S6_AS.
IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
IPR012051; Peptidase_S1A_pr.
IPR003966; Peptidase_S1A_prothrombin.
IPR018992; Thrombin_light_chain.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.20.10; Kringle; 2.
G3DSA:4.10.140.10; Thrombin_light_chain; 1.

PANTHER

PTHR19355:SF61; Peptidase_S1A_pr; 1.

Pfam

PF00594; Gla; 1.
PF00051; Kringle; 2.
PF09396; Thrombin_light; 1.
PF00089; Trypsin; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001149; Thrombin; 1.

PRINTS

PR00722; CHYMOTRYPSIN.
PR00001; GLABLOOD.
PR00018; KRINGLE.
PR01505; PROTHROMBIN.

ProDom

PD000395; Kringle; 2.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00069; GLA; 1.
SM00130; KR; 2.
SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.

PROSITE

PS00011; GLA_1; 1.
PS50998; GLA_2; 1.
PS00021; KRINGLE_1; 2.
PS50070; KRINGLE_2; 2.
PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PeptideAtlas

P00734; -.

PRIDE

P00734; -.

Genome annotation databases

Ensembl

ENSG00000180210; Homo sapiens. [Contig view]

GeneID

2147; -.

KEGG

hsa:2147; -.

Phylogenomic databases

HOGENOM

P00734; -.

HOVERGEN

P00734; -.

OMA

P00734; EGNCAEG.

Other

BindingDB

P00734; -.

DrugBank

DB00025; Antihemophilic Factor.
DB00278; Argatroban.
DB00006; Bivalirudin.
DB00100; Coagulation Factor IX.
DB00055; Drotrecogin alfa.
DB01225; Enoxaparin.
DB01109; Heparin.
DB00001; Lepirudin.
DB00170; Menadione.
DB01123; Proflavine.
DB00641; Simvastatin.
DB04786; Suramin.
DB00682; Warfarin.
DB04898; Ximelagatran.

8681; -.

P00734; -.

F2; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acute phase; Blood coagulation; Calcium; Cleavage on pair of basic residues; Direct protein sequencing; Disease mutation; Disulfide bond; Gamma-carboxyglutamic acid; Glycoprotein; Hydrolase; Kringle; Pharmaceutical; Polymorphism; Protease; Repeat; Secreted; Serine protease; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 24`	`24`	`Potential.`
`PROPEP`	`25 43`	`19`		`PRO_0000028159`
`CHAIN`	`44 622`	`579`	`Prothrombin.`	`PRO_0000028160`
`PEPTIDE`	`44 198`	`155`	`Activation peptide fragment 1.`	`PRO_0000028161`
`PEPTIDE`	`199 327`	`129`	`Activation peptide fragment 2.`	`PRO_0000028162`
`CHAIN`	`328 363`	`36`	`Thrombin light chain.`	`PRO_0000028163`
`CHAIN`	`364 622`	`259`	`Thrombin heavy chain.`	`PRO_0000028164`
`DOMAIN`	`44 89`	`46`	`Gla.`
`DOMAIN`	`108 186`	`79`	`Kringle 1.`
`DOMAIN`	`213 291`	`79`	`Kringle 2.`
`DOMAIN`	`364 618`	`255`	`Peptidase S1.`
`REGION`	`551 573`	`23`	`High affinity receptor-binding region which is also known as the TP508 peptide.`
`ACT_SITE`	`406 406`		`Charge relay system.`
`ACT_SITE`	`462 462`		`Charge relay system.`
`ACT_SITE`	`568 568`		`Charge relay system.`
`SITE`	`198 199`	`2`	`Cleavage; by thrombin.`
`SITE`	`327 328`	`2`	`Cleavage; by factor Xa.`
`SITE`	`363 364`	`2`	`Cleavage; by factor Xa.`
`MOD_RES`	`49 49`		`4-carboxyglutamate.`
`MOD_RES`	`50 50`		`4-carboxyglutamate.`
`MOD_RES`	`57 57`		`4-carboxyglutamate.`
`MOD_RES`	`59 59`		`4-carboxyglutamate.`
`MOD_RES`	`62 62`		`4-carboxyglutamate.`
`MOD_RES`	`63 63`		`4-carboxyglutamate.`
`MOD_RES`	`68 68`		`4-carboxyglutamate.`
`MOD_RES`	`69 69`		`4-carboxyglutamate.`
`MOD_RES`	`72 72`		`4-carboxyglutamate.`
`MOD_RES`	`75 75`		`4-carboxyglutamate.`
`CARBOHYD`	`121 121`		`N-linked (GlcNAc...).`
`CARBOHYD`	`143 143`		`N-linked (GlcNAc...).`
`CARBOHYD`	`416 416`		`N-linked (GlcNAc...).`
`DISULFID`	`60 65`
`DISULFID`	`90 103`
`DISULFID`	`108 186`
`DISULFID`	`129 169`
`DISULFID`	`157 181`
`DISULFID`	`213 291`
`DISULFID`	`234 274`
`DISULFID`	`262 286`
`DISULFID`	`336 482`		`Interchain (between light and heavy chains).`
`DISULFID`	`391 407`
`DISULFID`	`536 550`		`By similarity.`
`DISULFID`	`564 594`		`By similarity.`
`VARIANT`	`72 72`	`1`	`E -> G (in dysprothrombinemia; Shanghai).`	`VAR_055232`
`VARIANT`	`165 165`	`1`	`T -> M (in dbSNP:rs5896 [NCBI]).`	`VAR_011781`
`VARIANT`	`200 200`	`1`	`E -> K (in dysprothrombinemia; prothrombin type 3).`	`VAR_006711`
`VARIANT`	`314 314`	`1`	`R -> C (in dysprothrombinemia; Barcelona/Madrid).`	`VAR_006712`
`VARIANT`	`314 314`	`1`	`R -> H (in dysprothrombinemia; Padua-1).`	`VAR_006713`
`VARIANT`	`380 380`	`1`	`M -> T (in dysprothrombinemia; Himi-1).`	`VAR_006714 [3D]`
`VARIANT`	`386 386`	`1`	`P -> T (in dbSNP:rs5897 [NCBI]).`	`VAR_011782 [3D]`
`VARIANT`	`425 425`	`1`	`R -> C (in dysprothrombinemia; Quick-1).`	`VAR_006715 [3D]`
`VARIANT`	`431 431`	`1`	`R -> H (in dysprothrombinemia; Himi-2).`	`VAR_006716 [3D]`
`VARIANT`	`461 461`	`1`	`R -> W (in dysprothrombinemia; Tokushima).`	`VAR_006717 [3D]`
`VARIANT`	`509 509`	`1`	`E -> A (in dysprothrombinemia; Salakta/Frankfurt).`	`VAR_006718 [3D]`
`VARIANT`	`601 601`	`1`	`G -> V (in dysprothrombinemia; Quick-2).`	`VAR_006719 [3D]`
`CONFLICT`	`9 25`		`Missing (in Ref. 3; BAG64719).`
`CONFLICT`	`66 66`		`S -> N (in Ref. 4; BAD96497).`
`CONFLICT`	`119 119`		`H -> N (in Ref. 9; AA sequence).`
`CONFLICT`	`121 121`		`N -> S (in Ref. 9; AA sequence).`
`CONFLICT`	`164 164`		`T -> I (in Ref. 9; AA sequence).`
`CONFLICT`	`164 164`		`T -> N (in Ref. 7; CAA23842).`
`CONFLICT`	`176 176`		`V -> A (in Ref. 9; AA sequence).`
`CONFLICT`	`183 183`		`I -> T (in Ref. 9; AA sequence).`
`CONFLICT`	`194 195`		`AM -> MV (in Ref. 9; AA sequence).`
`CONFLICT`	`308 308`		`D -> DEE (in Ref. 9; AA sequence).`
`CONFLICT`	`335 335`		`D -> N (in Ref. 10; AA sequence).`
`CONFLICT`	`337 337`		`G -> R (in Ref. 4; BAD96495).`
`CONFLICT`	`349 349`		`D -> N (in Ref. 10; AA sequence).`
`CONFLICT`	`369 369`		`D -> N (in Ref. 10; AA sequence).`
`CONFLICT`	`398 398`		`D -> N (in Ref. 10; AA sequence).`
`CONFLICT`	`414 414`		`D -> N (in Ref. 10; AA sequence).`
`CONFLICT`	`485 485`		`D -> N (in Ref. 10; AA sequence).`
`CONFLICT`	`494 494`		`Q -> G (in Ref. 10; AA sequence).`
`CONFLICT`	`504 504`		`W -> Y (in Ref. 10; AA sequence).`
`CONFLICT`	`509 509`		`E -> S (in Ref. 10; AA sequence).`
`CONFLICT`	`511 511`		`W -> V (in Ref. 10; AA sequence).`
`CONFLICT`	`514 514`		`N -> D (in Ref. 10; AA sequence).`
`CONFLICT`	`529 530`		`PI -> AL (in Ref. 10; AA sequence).`
`CONFLICT`	`532 532`		`E -> Q (in Ref. 10; AA sequence).`
`TURN`	`334 337`	`4`
`TURN`	`340 342`	`3`
`HELIX`	`343 345`	`3`
`HELIX`	`352 358`	`7`
`STRAND`	`378 383`	`6`
`TURN`	`384 387`	`4`
`STRAND`	`388 395`	`8`
`STRAND`	`397 403`	`7`
`HELIX`	`405 407`	`3`
`HELIX`	`411 413`	`3`
`HELIX`	`419 421`	`3`
`STRAND`	`422 427`	`6`
`STRAND`	`430 433`	`4`
`TURN`	`436 438`	`3`
`STRAND`	`440 442`	`3`
`STRAND`	`444 449`	`6`
`TURN`	`455 458`	`4`
`STRAND`	`464 470`	`7`
`HELIX`	`486 492`	`7`
`STRAND`	`498 504`	`7`
`STRAND`	`524 530`	`7`
`HELIX`	`533 538`	`6`
`STRAND`	`548 551`	`4`
`HELIX`	`555 557`	`3`
`STRAND`	`571 575`	`5`
`TURN`	`577 579`	`3`
`STRAND`	`582 590`	`9`
`STRAND`	`592 595`	`4`
`STRAND`	`601 605`	`5`
`HELIX`	`607 609`	`3`
`HELIX`	`610 620`	`11`

Sequence information

Length: 622 AA [This is the length of the unprocessed precursor]

Molecular weight: 70037 Da [This is the MW of the unprocessed precursor]

CRC64: 8A25E1DA88208FCF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAHVRGLQLP GCLALAALCS LVHSQHVFLA PQQARSLLQR VRRANTFLEE VRKGNLEREC 

        70         80         90        100        110        120 
VEETCSYEEA FEALESSTAT DVFWAKYTAC ETARTPRDKL AACLEGNCAE GLGTNYRGHV 

       130        140        150        160        170        180 
NITRSGIECQ LWRSRYPHKP EINSTTHPGA DLQENFCRNP DSSTTGPWCY TTDPTVRRQE 

       190        200        210        220        230        240 
CSIPVCGQDQ VTVAMTPRSE GSSVNLSPPL EQCVPDRGQQ YQGRLAVTTH GLPCLAWASA 

       250        260        270        280        290        300 
QAKALSKHQD FNSAVQLVEN FCRNPDGDEE GVWCYVAGKP GDFGYCDLNY CEEAVEEETG 

       310        320        330        340        350        360 
DGLDEDSDRA IEGRTATSEY QTFFNPRTFG SGEADCGLRP LFEKKSLEDK TERELLESYI 

       370        380        390        400        410        420 
DGRIVEGSDA EIGMSPWQVM LFRKSPQELL CGASLISDRW VLTAAHCLLY PPWDKNFTEN 

       430        440        450        460        470        480 
DLLVRIGKHS RTRYERNIEK ISMLEKIYIH PRYNWRENLD RDIALMKLKK PVAFSDYIHP 

       490        500        510        520        530        540 
VCLPDRETAA SLLQAGYKGR VTGWGNLKET WTANVGKGQP SVLQVVNLPI VERPVCKDST 

       550        560        570        580        590        600 
RIRITDNMFC AGYKPDEGKR GDACEGDSGG PFVMKSPFNN RWYQMGIVSW GEGCDRDGKY 

       610        620 
GFYTHVFRLK KWIQKVIDQF GE

P00734 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools