[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1093/nar/10.24.8113; PubMed=6298709 [NCBI, ExPASy, EBI, Israel, Japan] Bock S.C., Wion K.L., Vehar G.A., Lawn R.M.; "Cloning and expression of the cDNA for human antithrombin III."; Nucleic Acids Res. 10:8113-8125(1982).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1073/pnas.80.7.1845; PubMed=6572945 [NCBI, ExPASy, EBI, Israel, Japan] Chandra T., Stackhouse R., Kidd V.J., Woo S.L.C.; "Isolation and sequence characterization of a cDNA clone of human antithrombin III."; Proc. Natl. Acad. Sci. U.S.A. 80:1845-1848(1983).
[3]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT AT-III DEFICIENCY MET-438. Tsuji H., Takada O., Nakagawa M., Tanaka S., Hashimoto-Gotoh T.; "Hereditary antithrombin III deficiency: identification of an arginine-406 to methionine point mutation near protease reactive site."; (In) Yoshida T.O., Wilson J.M. (eds.); Molecular approaches to the study and treatment of Human diseases, pp.51-55, Elsevier, Amsterdam (1992).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1021/bi00067a008; PubMed=8476848 [NCBI, ExPASy, EBI, Israel, Japan] Olds R.J., Lane D.A., Chowdhury V., de Stefano V., Leone G., Thein S.L.; "Complete nucleotide sequence of the antithrombin gene: evidence for homologous recombination causing thrombophilia."; Biochemistry 32:4216-4224(1993).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Fetal liver; Zhang C., Yu Y., Zhang S., Wei H., Bi J., Zhou G., Dong C., Zai Y., Xu W., Gao F., Liu M., He F.; "Functional prediction of the coding sequences of 75 new genes deduced by analysis of cDNA clones from human fetal liver."; Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Liver; 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).
[7]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-30 AND ALA-147. SeattleSNPs variation discovery resource; Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[8]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan] Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; "The DNA sequence and biological annotation of human chromosome 1."; Nature 441:315-321(2006).
[9]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.; Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]	PROTEIN SEQUENCE OF 33-464, GLYCOSYLATION AT ASN-128; ASN-167; ASN-187 AND ASN-224, AND DISULFIDE BONDS. Petersen T.E., Dudek-Wojciechowska G., Sottrup-Jensen L., Magnusson S.; "Primary structure of antithrombin-III (heparin cofactor). Partial homology between alpha-1-antitrypsin and antithrombin-III."; (In) Collen D., Wiman B., Verstraete M. (eds.); The physiological inhibitors of blood coagulation and fibrinolysis, pp.43-54, Elsevier, Amsterdam (1979).
[11]	NUCLEOTIDE SEQUENCE [MRNA] OF 42-464. PubMed=6305982 [NCBI, ExPASy, EBI, Israel, Japan] Prochownik E.V., Markham A.F., Orkin S.H.; "Isolation of a cDNA clone for human antithrombin III."; J. Biol. Chem. 258:8389-8394(1983).
[12]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 137-208, AND VARIANT AT3D LEU-439. DOI=10.1021/bi00416a052; PubMed=3191114 [NCBI, ExPASy, EBI, Israel, Japan] Bock S.C., Marrinan J.A., Radziejewska E.; "Antithrombin III Utah: proline-407 to leucine mutation in a highly conserved region near the inhibitor reactive site."; Biochemistry 27:6171-6178(1988).
[13]	PROTEIN SEQUENCE OF 371-425, MASS SPECTROMETRY, AND VARIANT AT-III DEFICIENCY THR-414. TISSUE=Plasma; DOI=10.1111/j.1365-2141.1995.tb08368.x; PubMed=7734359 [NCBI, ExPASy, EBI, Israel, Japan] Lindo V.S., Kakkar V.V., Learmonth M., Melissari E., Zappacosta F., Panico M., Morris H.R.; "Antithrombin-TRI (Ala382 to Thr) causing severe thromboembolic tendency undergoes the S-to-R transition and is associated with a plasma-inactive high-molecular-weight complex of aggregated antithrombin."; Br. J. Haematol. 89:589-601(1995).
[14]	ACTIVE SITE. DOI=10.1016/0014-5793(81)80255-4; PubMed=7238875 [NCBI, ExPASy, EBI, Israel, Japan] Bjoerk I., Danielsson A., Fenton J.W. II, Joernvall H.; "The site in human antithrombin for functional proteolytic cleavage by human thrombin."; FEBS Lett. 126:257-260(1981).
[15]	HEPARIN-BINDING SITE. PubMed=6693405 [NCBI, ExPASy, EBI, Israel, Japan] Blackburn M.N., Smith R.L., Carson J., Sibley C.C.; "The heparin-binding site of antithrombin III. Identification of a critical tryptophan in the amino acid sequence."; J. Biol. Chem. 259:939-941(1984).
[16]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187, AND MASS SPECTROMETRY. TISSUE=Bile; DOI=10.1074/mcp.M400015-MCP200; PubMed=15084671 [NCBI, ExPASy, EBI, Israel, Japan] Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.; "A proteomic analysis of human bile."; Mol. Cell. Proteomics 3:715-728(2004).
[17]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128 AND ASN-187, 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).
[18]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128; ASN-187 AND ASN-224, 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).
[19]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-224, AND MASS SPECTROMETRY. TISSUE=Platelet; DOI=10.1074/mcp.M500324-MCP200; PubMed=16263699 [NCBI, ExPASy, EBI, Israel, Japan] Lewandrowski U., Moebius J., Walter U., Sickmann A.; "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."; Mol. Cell. Proteomics 5:226-233(2006).
[20]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128 AND ASN-187, 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).
[21]	X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). DOI=10.1016/S0969-2126(00)00028-9; PubMed=8087553 [NCBI, ExPASy, EBI, Israel, Japan] Carrell R.W., Stein P.E., Fermi G., Wardell M.R.; "Biological implications of a 3 A structure of dimeric antithrombin."; Structure 2:257-270(1994).
[22]	X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS). DOI=10.1038/nsb0194-48; PubMed=7656006 [NCBI, ExPASy, EBI, Israel, Japan] Schreuder H.A., de Boer B., Dijkema R., Mulders J., Theunissen H.J.M., Grootenhuis P.D.J., Hol W.G.J.; "The intact and cleaved human antithrombin III complex as a model for serpin-proteinase interactions."; Nat. Struct. Biol. 1:48-54(1994).
[23]	X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). DOI=10.1006/jmbi.1996.0798; PubMed=9067613 [NCBI, ExPASy, EBI, Israel, Japan] Skinner R., Abrahams J.P., Whisstock J.C., Lesk A.M., Carrel R.W., Wardell M.R.; "The 2.6 A structure of antithrombin indicates a conformational change at the heparin binding site."; J. Mol. Biol. 266:601-609(1997).
[24]	X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS). DOI=10.1006/jmbi.1998.2083; PubMed=9761669 [NCBI, ExPASy, EBI, Israel, Japan] Skinner R., Chang W.-S.W., Jin L., Pei X.Y., Huntington J.A., Abrahams J.P., Carrell R.W., Lomas D.A.; "Implications for function and therapy of a 2.9 A structure of binary-complexed antithrombin."; J. Mol. Biol. 283:9-14(1998).
[25]	REVIEW. DOI=10.1016/0300-9084(90)90123-X; PubMed=2126464 [NCBI, ExPASy, EBI, Israel, Japan] Mourey L., Samama J.-P., Delarue M., Choay J., Lormeau J.C., Petitou M., Moras D.; "Antithrombin III: structural and functional aspects."; Biochimie 72:599-608(1990).
[26]	REVIEW ON VARIANTS. PubMed=8236149 [NCBI, ExPASy, EBI, Israel, Japan] Lane D.A., Olds R.J., Boisclair M., Chowdhury V., Thein S.L., Cooper D.N., Blajchman M., Perry D., Emmerich J., Aiach M.; "Antithrombin III mutation database: first update. For the Thrombin and its Inhibitors Subcommittee of the Scientific and Standardization Committee of the International Society on Thrombosis and Haemostasis."; Thromb. Haemost. 70:361-369(1993).
[27]	REVIEW ON VARIANTS. DOI=10.1038/nsb0295-96; PubMed=7749926 [NCBI, ExPASy, EBI, Israel, Japan] Stein P.E., Carrell R.W.; "What do dysfunctional serpins tell us about molecular mobility and disease?"; Nat. Struct. Biol. 2:96-113(1995).
[28]	REVIEW ON VARIANTS. DOI=10.1002/(SICI)1098-1004(1996)7:1<7::AID-HUMU2>3.3.CO;2-A; PubMed=8664906 [NCBI, ExPASy, EBI, Israel, Japan] Perry D.J., Carrell R.W.; "Molecular genetics of human antithrombin deficiency."; Hum. Mutat. 7:7-22(1996).
[29]	VARIANTS AT3D SER-17; PRO-23; ASN-39; CYS-56; LEU-73; CYS-79; HIS-79; SER-79; ASN-87 DEL; CYS-89; LEU-90; CYS-95; SER-95; PRO-98; THR-112; PHE-131; VAL-131; LYS-133; PHE-138-139-LYS DEL; PRO-148; PRO-150; PRO-158; TYR-160; GLN-161; CYS-198; HIS-198; ILE-218 DEL; ASP-219; LYS-219; ARG-257; LYS-269; ILE-283; ASN-316; LYS-334; ARG-412; THR-414; PRO-416; SER-416; VAL-419; ASP-424; CYS-425; HIS-425; PRO-425; LEU-426; CYS-434; LEU-434; SER-434; THR-436; LYS-437; GLY-438; MET-438; LEU-439; THR-439; THR-453; ARG-456; THR-457; ASP-459; LEU-461 AND PHE-462, AND VARIANTS GLU-30; THR-52 AND CYS-190. PubMed=9031473 [NCBI, ExPASy, EBI, Israel, Japan] The plasma coagulation inhibitors subcommittee of the scientific and standardization committee of the international society on thrombosis and haemostasis; Lane D.A., Bayston T., Olds R.J., Fitches A.C., Cooper D.N., Millar D.S., Jochmans K., Perry D.J., Okajima K., Thein S.L., Emmerich J.; "Antithrombin mutation database: 2nd (1997) update."; Thromb. Haemost. 77:197-211(1997).
[30]	VARIANT AT3D CYS-79. DOI=10.1073/pnas.81.2.289; PubMed=6582486 [NCBI, ExPASy, EBI, Israel, Japan] Koide T., Odani S., Takahashi K., Ono T., Sakuragawa N.; "Antithrombin III Toyama: replacement of arginine-47 by cysteine in hereditary abnormal antithrombin III that lacks heparin-binding ability."; Proc. Natl. Acad. Sci. U.S.A. 81:289-293(1984).
[31]	VARIANT AT3D LEU-73. PubMed=3080419 [NCBI, ExPASy, EBI, Israel, Japan] Chang J.Y., Tran T.H.; "Antithrombin III Basel. Identification of a Pro-Leu substitution in a hereditary abnormal antithrombin with impaired heparin cofactor activity."; J. Biol. Chem. 261:1174-1176(1986).
[32]	VARIANT AT3D LEU-426. PubMed=3805013 [NCBI, ExPASy, EBI, Israel, Japan] Stephens A.W., Thalley B.S., Hirs C.H.W.; "Antithrombin-III Denver, a reactive site variant."; J. Biol. Chem. 262:1044-1048(1987).
[33]	VARIANT AT3D THR-414. PubMed=3179438 [NCBI, ExPASy, EBI, Israel, Japan] Devrak-Kizuk R., Chui D.H.K., Prochownik E.V., Carter C.J., Ofosu F.A., Blajchman M.A.; "Antithrombin-III-Hamilton: a gene with a point mutation (guanine to adenine) in codon 382 causing impaired serine protease reactivity."; Blood 72:1518-1523(1988).
[34]	VARIANTS AT3D CYS-425 AND HIS-425. PubMed=3162733 [NCBI, ExPASy, EBI, Israel, Japan] Erdjument H., Laned D.A., Panico M., di Marzo V., Morris H.R.; "Single amino acid substitutions in the reactive site of antithrombin leading to thrombosis. Congenital substitution of arginine 393 to cysteine in antithrombin Northwick Park and to histidine in antithrombin Glasgow."; J. Biol. Chem. 263:5589-5593(1988).
[35]	VARIANT AT3D HIS-425. DOI=10.1016/0049-3848(89)90127-8; PubMed=2781509 [NCBI, ExPASy, EBI, Israel, Japan] Erdjument H., Lane D.A., Panico M., di Marzo V., Morris H.R., Bauer K., Rosenberg R.D.; "Antithrombin Chicago, amino acid substitution of arginine 393 to histidine."; Thromb. Res. 54:613-619(1989).
[36]	VARIANT AT3D CYS-56. DOI=10.1016/0014-5793(90)81530-2; PubMed=2365065 [NCBI, ExPASy, EBI, Israel, Japan] Borg J.Y., Brennan S.O., Carrell R.W., George P., Perry D.J., Shaw J.; "Antithrombin Rouen-IV 24 Arg-->Cys. The amino-terminal contribution to heparin binding."; FEBS Lett. 266:163-166(1990).
[37]	VARIANT GLU-30. DOI=10.1016/0014-5793(90)81057-U; PubMed=1977621 [NCBI, ExPASy, EBI, Israel, Japan] Daly M., Bruce D., Perry D.J., Price J., Harper P.L., O'Meara A., Carrell R.W.; "Antithrombin Dublin (-3 Val-->Glu): an N-terminal variant which has an aberrant signal peptidase cleavage site."; FEBS Lett. 273:87-90(1990).
[38]	VARIANT AT3D GLN-161. PubMed=2229057 [NCBI, ExPASy, EBI, Israel, Japan] Gandrille S., Aiach M., Lane D.A., Vidaud D., Molho-Sabatier P., Caso R., de Moerloose P., Fiessinger J.-N., Clauser E.; "Important role of arginine 129 in heparin-binding site of antithrombin III. Identification of a novel mutation arginine 129 to glutamine."; J. Biol. Chem. 265:18997-19001(1990).
[39]	CHARACTERIZATION OF VARIANT AT3D THR-414, AND MUTAGENESIS OF ALA-414. DOI=10.1016/0014-5793(91)80305-M; PubMed=2013320 [NCBI, ExPASy, EBI, Israel, Japan] Austin R.C., Rachubinski R.A., Blachjman M.A.; "Site-directed mutagenesis of alanine-382 of human antithrombin III."; FEBS Lett. 280:254-258(1991).
[40]	VARIANT AT3D SER-416. DOI=10.1016/0014-5793(91)80809-H; PubMed=1906811 [NCBI, ExPASy, EBI, Israel, Japan] Perry D.J., Daly M., Harper P.L., Tait R.C., Price J., Walker I.D., Carrell R.W.; "Antithrombin Cambridge II, 384 Ala to Ser. Further evidence of the role of the reactive centre loop in the inhibitory function of the serpins."; FEBS Lett. 285:248-250(1991).
[41]	VARIANT AT3D PHE-131. DOI=10.1016/0014-5793(92)80854-A; PubMed=1555650 [NCBI, ExPASy, EBI, Israel, Japan] Olds R.J., Lane D.A., Boisclair M., Sas G., Bock S.C., Thein S.L.; "Antithrombin Budapest 3. An antithrombin variant with reduced heparin affinity resulting from the substitution L99F."; FEBS Lett. 300:241-246(1992).
[42]	VARIANT AT3D ASP-424. PubMed=1547341 [NCBI, ExPASy, EBI, Israel, Japan] Blajchman M.A., Fernandez-Rachubinski F., Sheffield W.P., Austin R.C., Schulman S.; "Antithrombin-III Stockholm: a codon 392 (Gly-->Asp) mutation with normal heparin binding and impaired serine protease reactivity."; Blood 79:1428-1434(1992).
[43]	VARIANT AT3D PRO-148. PubMed=8443391 [NCBI, ExPASy, EBI, Israel, Japan] Okajima K., Abe H., Maeda S., Motomura M., Tsujihata M., Nagataki S., Okabe H., Takatsuki K.; "Antithrombin III Nagasaki (Ser116-Pro): a heterozygous variant with defective heparin binding associated with thrombosis."; Blood 81:1300-1305(1993).
[44]	VARIANT AT3D 138-PHE-LYS-139 DEL. DOI=10.1006/geno.1993.1184; PubMed=8486379 [NCBI, ExPASy, EBI, Israel, Japan] Olds R.J., Lane D.A., Beresford C.H., Abildgaard U., Hughes P.M., Thein S.L.; "A recurrent deletion in the antithrombin gene, AT106-108(-6 bp), identified by DNA heteroduplex detection."; Genomics 16:298-299(1993).
[45]	VARIANTS AT3D HIS-79 AND TYR-160. PubMed=7981186 [NCBI, ExPASy, EBI, Israel, Japan] Emmerich J., Vidaud D., Alhenc-Gelas M., Chadeuf G., Gouault-Heilmann M., Aillaud M.-F., Aiach M.; "Three novel mutations of antithrombin inducing high-molecular-mass compounds."; Arterioscler. Thromb. 14:1958-1965(1994).
[46]	VARIANTS AT3D THR-112; TYR-152 AND ILE-283, AND VARIANT CYS-190. DOI=10.1007/BF00211016; PubMed=7959685 [NCBI, ExPASy, EBI, Israel, Japan] Millar D.S., Wacey A.I., Ribando J., Melissari E., Laursen B., Woods P., Kakkar V.V., Cooper D.N.; "Three novel missense mutations in the antithrombin III (AT3) gene causing recurrent venous thrombosis."; Hum. Genet. 94:509-512(1994).
[47]	VARIANT AT3D ARG-456. PubMed=8274732 [NCBI, ExPASy, EBI, Israel, Japan] Jochmans K., Lissens W., Vervoort R., Peeters S., de Waelwe M., Liebaers I.; "Antithrombin-Gly 424 Arg: a novel point mutation responsible for type 1 antithrombin deficiency and neonatal thrombosis."; Blood 83:146-151(1994).
[48]	VARIANTS AT3D SER-95; THR-453 AND PHE-462. PubMed=7994035 [NCBI, ExPASy, EBI, Israel, Japan] van Boven H.H., Olds R.J., Thein S.L., Reitsma P.H., Lane D.A., Briet E., Vandenbroucke J.P., Rosendaal F.R.; "Hereditary antithrombin deficiency: heterogeneity of the molecular basis and mortality in Dutch families."; Blood 84:4209-4213(1994).
[49]	VARIANT AT3D ASP-219. PubMed=7989582 [NCBI, ExPASy, EBI, Israel, Japan] Bruce D., Perry D.J., Borg J.-Y., Carrell R.W., Wardell M.R.; "Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen-VI (187 Asn-->Asp)."; J. Clin. Invest. 94:2265-2274(1994).
[50]	VARIANTS AT3D VAL-131 AND PRO-150. Chowdhury V., Olds R.J., Lane D.A., Mille B., Pabinger I., Thein S.L.; "Two novel antithrombin variants (L99V and Q118P) which alter the heparin binding domain."; Nouv. Rev. Fr. Hematol. 86:268-268(1994).
[51]	VARIANT AT3D 273-LYS--LYS-307 DEL. PubMed=7878627 [NCBI, ExPASy, EBI, Israel, Japan] Emmerich J., Chadeuf G., Alhenc-Gelas M., Gouault-Heilman M., Toulon P., Fiessinger J.-N., Aiach M.; "Molecular basis of antithrombin type I deficiency: the first large in-frame deletion and two novel mutations in exon 6."; Thromb. Haemost. 72:534-539(1994).
[52]	VARIANT AT3D HIS-425. DOI=10.1002/ajh.2830480104; PubMed=7832187 [NCBI, ExPASy, EBI, Israel, Japan] Okajima K., Abe H., Wagatsuma M., Okabe H., Takatsuki K.; "Antithrombin III Kumamoto II; a single mutation at Arg393-His increased the affinity of antithrombin III for heparin."; Am. J. Hematol. 48:12-18(1995).
[53]	VARIANT AT3D ARG-127. PubMed=9157604 [NCBI, ExPASy, EBI, Israel, Japan] Ozawa T., Takikawa Y., Niiya K., Fujiwara T., Suzuki K., Sato S., Sakuragawa N.; "Antithrombin Morioka (Cys 95-Arg): a novel missense mutation causing type I antithrombin deficiency."; Thromb. Haemost. 77:403-403(1997).
[54]	VARIANT AT3D PRO-23. PubMed=9845533 [NCBI, ExPASy, EBI, Israel, Japan] Fitches A.C., Appleby R., Lane D.A., De Stefano V., Leone G., Olds R.J.; "Impaired cotranslational processing as a mechanism for type I antithrombin deficiency."; Blood 92:4671-4676(1998).
[55]	VARIANTS AT3D ARG-32; LEU-73; CYS-79; HIS-198; ARG-257 AND ARG-412. PubMed=9759613 [NCBI, ExPASy, EBI, Israel, Japan] Jochmans K., Lissens W., Seneca S., Capel P., Chatelain B., Meeus P., Osselaer J.C., Peerlinck K., Seghers J., Slacmeulder M., Stibbe J., van de Loo J., Vermylen J., Liebaers I., De Waele M.; "The molecular basis of antithrombin deficiency in Belgian and Dutch families."; Thromb. Haemost. 80:376-381(1998).
[56]	VARIANT THR-167. PubMed=10361121 [NCBI, ExPASy, EBI, Israel, Japan] Bayston T.A., Tripodi A., Mannucci P.M., Thompson E., Ireland H., Fitches A.C., Hananeia L., Olds R.J., Lane D.A.; "Familial overexpression of beta-antithrombin caused by an Asn135-to-Thr substitution."; Blood 93:4242-4247(1999).
[57]	VARIANTS AT3D PHE-214; PRO-223; ILE-243; THR-251; VAL-283 AND PRO-397. DOI=10.1046/j.1365-2141.2000.02245.x; PubMed=10997988 [NCBI, ExPASy, EBI, Israel, Japan] Picard V., Bura A., Emmerich J., Alhenc-Gelas M., Biron C., Houbouyan-Reveillard L.L., Molho P., Labatide-Alanore A., Sie P., Toulon P., Verdy E., Aiach M.; "Molecular bases of antithrombin deficiency in French families: identification of seven novel mutations in the antithrombin gene."; Br. J. Haematol. 110:731-734(2000).
[58]	VARIANT AT3D 152-HIS--PHE-154 DEL. DOI=10.1007/BF02982095; PubMed=11794707 [NCBI, ExPASy, EBI, Israel, Japan] Niiya K., Kiguchi T., Dansako H., Fujimura K., Fujimoto T., Iijima K., Tanimoto M., Harada M.; "Two novel gene mutations in type I antithrombin deficiency."; Int. J. Hematol. 74:469-472(2001).
[59]	VARIANT AT3D PRO-223. DOI=10.1067/mpd.2001.118191; PubMed=11713457 [NCBI, ExPASy, EBI, Israel, Japan] Baud O., Picard V., Durand P., Duchemin J., Proulle V., Alhenc-Gelas M., Devictor D., Dreyfus M.; "Intracerebral hemorrhage associated with a novel antithrombin gene mutation in a neonate."; J. Pediatr. 139:741-743(2001).
[60]	VARIANT AT3D GLU-146. DOI=10.1267/THRO88030436; PubMed=12353073 [NCBI, ExPASy, EBI, Israel, Japan] Mushunje A., Zhou A., Huntington J.A., Conard J., Carrell R.W.; "Antithrombin 'DREUX' (Lys 114Glu): a variant with complete loss of heparin affinity."; Thromb. Haemost. 88:436-443(2002).
[61]	VARIANT AT3D LEU-261. DOI=10.1182/blood-2002-11-3391; PubMed=12595305 [NCBI, ExPASy, EBI, Israel, Japan] Picard V., Dautzenberg M.-D., Villoutreix B.O., Orliaguet G., Alhenc-Gelas M., Aiach M.; "Antithrombin Phe229Leu: a new homozygous variant leading to spontaneous antithrombin polymerization in vivo associated with severe childhood thrombosis."; Blood 102:919-925(2003).
[62]	VARIANTS AT3D LYS-121; HIS-178; CYS-425; HIS-425 AND PRO-441. DOI=10.1007/BF02983246; PubMed=12894857 [NCBI, ExPASy, EBI, Israel, Japan] Nagaizumi K., Inaba H., Amano K., Suzuki M., Arai M., Fukutake K.; "Five novel and four recurrent point mutations in the antithrombin gene causing venous thrombosis."; Int. J. Hematol. 78:79-83(2003).
[63]	VARIANTS AT3D LEU-179; CYS-425 AND LEU-426. DOI=10.1002/ajh.20067; PubMed=15164384 [NCBI, ExPASy, EBI, Israel, Japan] David D., Ribeiro S., Ferrao L., Gago T., Crespo F.; "Molecular basis of inherited antithrombin deficiency in Portuguese families: identification of genetic alterations and screening for additional thrombotic risk factors."; Am. J. Hematol. 76:163-171(2004).
[64]	VARIANT AT3D HIS-398. DOI=10.1001/archopht.124.8.1165; PubMed=16908819 [NCBI, ExPASy, EBI, Israel, Japan] Kuhli C., Jochmans K., Scharrer I., Luechtenberg M., Hattenbach L.-O.; "Retinal vein occlusion associated with antithrombin deficiency secondary to a novel G9840C missense mutation."; Arch. Ophthalmol. 124:1165-1169(2006).

Comments

FUNCTION: Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin.
INTERACTION:
P19174:PLCG1; NbExp=1; IntAct=EBI-1039832, EBI-79387;
SUBCELLULAR LOCATION: Secreted, extracellular space.
TISSUE SPECIFICITY: Found in plasma.
MASS SPECTROMETRY: Mass=57863; Method=Electrospray; Range=33-464; Source=PubMed:7734359;.
MASS SPECTROMETRY: Mass=57911; Method=Electrospray; Range=33-464; Note=Variant Thr-414; Source=PubMed:7734359;.
DISEASE: Defects in SERPINC1 are the cause of antithrombin-III deficiency (AT3D) [MIM:107300]. AT3D is an important risk factor for hereditary thrombophilia, a hemostatic disorder characterized by a tendency to recurrent thrombosis. AT3D is classified into 4 types. Type I: characterized by a 50% decrease in antigenic and functional levels. Type II: has defects affecting the thrombin-binding domain. Type III: alteration of the heparin-binding domain. Plasma AT-III antigen levels are normal in type II and III. Type IV: consists of miscellaneous group of unclassifiable mutations.
SIMILARITY: Belongs to the serpin family.
WEB RESOURCE: Name=Wikipedia; Note=Antithrombin entry; URL="http://en.wikipedia.org/wiki/Antithrombin";.
WEB RESOURCE: Name=Antithrombin mutation database; URL="http://www1.imperial.ac.uk/medicine/about/divisions/is/haemo/coag/antithrombin/";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=SERPINC1";.
WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/serpinc1/";.
WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and polymorphism database; URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=SERPINC1";.

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

L00185; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
L00186; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
L00190; AAB40025.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D29832; BAA06212.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X68793; CAA48690.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF130100; AAG35525.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK312654; BAG35537.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF386078; AAK60337.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136170; CAI19423.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471067; EAW90969.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M21643; AAA51793.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M21644; AAA51794.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M21643; AAA51794.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M21642; AAA51796.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M21636; AAA51796.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M21637; AAA51796.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M21638; AAA51796.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M21640; AAA51796.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M21641; AAA51796.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00032179; -.

A49494; XHHU3.

NP_000479.1; -.

3D structure databases

PDB

1ANT; X-ray; 3.00 A; I/L=33-464.	[ExPASy / RCSB / EBI]
1ATH; X-ray; 3.20 A; A/B=33-464.	[ExPASy / RCSB / EBI]
1AZX; X-ray; 2.90 A; I/L=33-464.	[ExPASy / RCSB / EBI]
1BR8; X-ray; 2.90 A; I/L=33-464.	[ExPASy / RCSB / EBI]
1DZG; X-ray; 2.80 A; I=33-464, L=33-464.	[ExPASy / RCSB / EBI]
1DZH; X-ray; 2.85 A; I=33-464, L=33-464.	[ExPASy / RCSB / EBI]
1E03; X-ray; 2.90 A; I/L=33-464.	[ExPASy / RCSB / EBI]
1E04; X-ray; 2.60 A; I/L=33-464.	[ExPASy / RCSB / EBI]
1E05; X-ray; 2.62 A; I/L=33-464.	[ExPASy / RCSB / EBI]
1JVQ; X-ray; 2.60 A; I/L=33-464.	[ExPASy / RCSB / EBI]
1LK6; X-ray; 2.80 A; I/L=33-464.	[ExPASy / RCSB / EBI]
1NQ9; X-ray; 2.60 A; I/L=33-464.	[ExPASy / RCSB / EBI]
1OYH; X-ray; 2.62 A; I=33-464, L=33-464.	[ExPASy / RCSB / EBI]
1R1L; X-ray; 2.70 A; I/L=33-464.	[ExPASy / RCSB / EBI]
1SR5; X-ray; 3.10 A; A=33-464.	[ExPASy / RCSB / EBI]
1T1F; X-ray; 2.75 A; A/B/C=33-464.	[ExPASy / RCSB / EBI]
1TB6; X-ray; 2.50 A; I=33-464.	[ExPASy / RCSB / EBI]
2ANT; X-ray; 2.60 A; I/L=33-464.	[ExPASy / RCSB / EBI]
2B4X; X-ray; 2.80 A; I=37-463, L=37-463.	[ExPASy / RCSB / EBI]
2B5T; X-ray; 2.10 A; I=33-464.	[ExPASy / RCSB / EBI]
2BEH; X-ray; 2.70 A; I=33-464, L=33-464.	[ExPASy / RCSB / EBI]
2GD4; X-ray; 3.30 A; C/I=22-464.	[ExPASy / RCSB / EBI]
2HIJ; X-ray; 2.90 A; I=33-464, L=33-464.	[ExPASy / RCSB / EBI]
2ZNH; X-ray; 2.80 A; A/B=33-464.	[ExPASy / RCSB / EBI]
3EVJ; X-ray; 3.00 A; I/L=33-464.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1ANT; -.
1ATH; -.
1AZX; -.
1BR8; -.
1DZG; -.
1DZH; -.
1E03; -.
1E04; -.
1E05; -.
1JVQ; -.
1LK6; -.
1NQ9; -.
1OYH; -.
1R1L; -.
1SR5; -.
1T1F; -.
1TB6; -.
2ANT; -.
2B4X; -.
2B5T; -.
2BEH; -.
2GD4; -.
2HIJ; -.
2ZNH; -.
3EVJ; -.

ModBase

P01008.

Protein-protein interaction databases

IntAct

P01008; 2.

Protein family/group databases

MEROPS

I04.018; -.

Enzyme and pathway databases

Pathway_Interaction_DB

glypican_1pathway; Glypican 1 network.

Reactome

REACT_604; Hemostasis.

2D gel databases

P01008; -.

P01008; -.

P01008; -.

P01008; -.

Organism-specific databases

GC01M172139; -.

HIX0001345; -.

HGNC:775; SERPINC1.

CAB016790; -.
HPA001816; -.

MIM

107300; gene+phenotype. [NCBI / EBI]
188050; phenotype. [NCBI / EBI]

Orphanet

82; Antithrombin deficiency, congenital.

PharmGKB

PA35026; -.

Gene expression databases

P01008; -.

P01008; -.

HS_SERPINC1; -.

ENSG00000117601; Homo sapiens.

Ontologies

GO:0005615;	Cellular component: extracellular space (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005886;	Cellular component: plasma membrane (inferred from experiment from Reactome).
GO:0008201;	Molecular function: heparin binding (inferred from electronic annotation from UniProtKB-KW).
GO:0002020;	Molecular function: protease binding (inferred from physical interaction from UniProtKB).
GO:0004867;	Molecular function: serine-type endopeptidase inhibitor activity (non-traceable author statement from UniProtKB).
GO:0007596;	Biological process: blood coagulation (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000215; Protease_inhib_I4_serpin.
IPR015555; Protease_inhib_serpin_AT-III.
Graphical view of domain structure.

PANTHER

PTHR11461; Prot_inh_serpin; 1.
PTHR11461:SF53; Serpin_ATIII; 1.

Pfam

PF00079; Serpin; 1.
Pfam graphical view of domain structure.

SMART

SM00093; SERPIN; 1.
SMART graphical view of domain structure.

PROSITE

PS00284; SERPIN; 1.

Proteomic databases

PRIDE

P01008; -.

Genome annotation databases

Ensembl

ENSG00000117601; Homo sapiens. [Contig view]

GeneID

462; -.

KEGG

hsa:462; -.

Phylogenomic databases

HOVERGEN

P01008; -.

OMA

P01008; FRYRRVA.

Other

DrugBank

DB01225; Enoxaparin.
DB00569; Fondaparinux sodium.
DB01109; Heparin.

NextBio

1911; -.

PMAP-CutDB

P01008; -.

SOURCE

SERPINC1; Homo sapiens.

ProtoNet

P01008.

UniRef

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

Keywords

3D-structure; Blood coagulation; Direct protein sequencing; Disease mutation; Disulfide bond; Glycoprotein; Heparin-binding; Polymorphism; Protease inhibitor; Secreted; Serine protease inhibitor; Signal; Thrombophilia.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 32`	`32`
`CHAIN`	`33 464`	`432`	`Antithrombin-III.`	`PRO_0000032489`
`BINDING`	`81 81`		`Heparin.`
`BINDING`	`161 161`		`Heparin.`
`BINDING`	`177 177`		`Heparin.`
`SITE`	`425 426`	`2`	`Reactive bond.`
`CARBOHYD`	`128 128`		`N-linked (GlcNAc...).`
`CARBOHYD`	`167 167`		`N-linked (GlcNAc...).`
`CARBOHYD`	`187 187`		`N-linked (GlcNAc...).`
`CARBOHYD`	`224 224`		`N-linked (GlcNAc...).`
`DISULFID`	`40 160`
`DISULFID`	`53 127`
`DISULFID`	`279 462`
`VARIANT`	`17 17`	`1`	`Y -> S (in AT3D; type-I).`	`VAR_027450`
`VARIANT`	`23 23`	`1`	`L -> P (in AT3D; type-I; impairs cotranslational processing).`	`VAR_012748`
`VARIANT`	`30 30`	`1`	`V -> E (in Dublin; dbSNP:rs2227624 [NCBI]).`	`VAR_007032`
`VARIANT`	`32 32`	`1`	`C -> R (in AT3D; type-I).`	`VAR_027451`
`VARIANT`	`39 39`	`1`	`I -> N (in AT3D; type-II; Rouen-3; lack of heparin-binding properties).`	`VAR_007033`
`VARIANT`	`52 52`	`1`	`M -> T (previously Whitechapel).`	`VAR_007034`
`VARIANT`	`56 56`	`1`	`R -> C (in AT3D; type-II; Rouen-4; lack of heparin-binding properties).`	`VAR_007035`
`VARIANT`	`73 73`	`1`	`P -> L (in AT3D; type-II; Basel/Franconville/Clichy-1/Clichy-2/` `Dublin-2; lacks heparin-binding ability).`	`VAR_007036`
`VARIANT`	`79 79`	`1`	`R -> C (in AT3D; Tours/Alger/Amiens/Toyama/Paris-1/Paris-2/` `Padua-2/Barcelona-2/Kumamoto/Omura/Sasebo; lacks heparin-binding ability).`	`VAR_007037`
`VARIANT`	`79 79`	`1`	`R -> H (in AT3D; type-II; Rouen-1/Padua-1/Bligny/Budapest-2; lack of heparin-binding properties).`	`VAR_007038`
`VARIANT`	`79 79`	`1`	`R -> S (in AT3D; type-II; Rouen-2; lack of heparin-binding properties).`	`VAR_007039`
`VARIANT`	`87 87`	`1`	`Missing (in AT3D; type-I).`	`VAR_007040`
`VARIANT`	`89 89`	`1`	`R -> C (in AT3D; type-I).`	`VAR_007041`
`VARIANT`	`90 90`	`1`	`F -> L (in AT3D; type-I; Budapest-6).`	`VAR_007042`
`VARIANT`	`95 95`	`1`	`Y -> C (in AT3D; type-I).`	`VAR_027452`
`VARIANT`	`95 95`	`1`	`Y -> S (in AT3D; type-I).`	`VAR_012316`
`VARIANT`	`98 98`	`1`	`L -> P (in AT3D; type-I).`	`VAR_027453`
`VARIANT`	`108 109`	`2`	`Missing (in AT3D; type-I).`	`VAR_007043`
`VARIANT`	`112 112`	`1`	`P -> T (in AT3D; type-I).`	`VAR_007044`
`VARIANT`	`121 121`	`1`	`M -> K (in AT3D; type-I).`	`VAR_027454`
`VARIANT`	`127 127`	`1`	`C -> R (in AT3D; type-I).`	`VAR_027455`
`VARIANT`	`131 131`	`1`	`L -> F (in AT3D; type-II; Budapest-3/Budapest-7).`	`VAR_007045`
`VARIANT`	`131 131`	`1`	`L -> V (in AT3D; type-II; Southport).`	`VAR_007046`
`VARIANT`	`133 133`	`1`	`Q -> K (in AT3D; type I).`	`VAR_007047`
`VARIANT`	`138 139`	`2`	`Missing (in AT3D; type-I).`	`VAR_007048`
`VARIANT`	`146 146`	`1`	`K -> E (in AT3D; Dreux; complete loss af heparin binding).`	`VAR_027456`
`VARIANT`	`147 147`	`1`	`T -> A (in dbSNP:rs2227606 [NCBI]).`	`VAR_013085`
`VARIANT`	`148 148`	`1`	`S -> P (in AT3D; type-II; Nagasaki; defective heparin binding associated with thrombosis).`	`VAR_007049`
`VARIANT`	`150 150`	`1`	`Q -> P (in AT3D; type-II; Vienna).`	`VAR_007050`
`VARIANT`	`152 154`	`3`	`Missing (in AT3D; type-I).`	`VAR_012749`
`VARIANT`	`152 152`	`1`	`H -> Y (in AT3D; type-I).`	`VAR_007051`
`VARIANT`	`153 153`	`1`	`Missing (in AT3D; type-I).`	`VAR_007052`
`VARIANT`	`158 158`	`1`	`L -> P (in AT3D; type-I).`	`VAR_007053`
`VARIANT`	`160 160`	`1`	`C -> Y (in AT3D; type-I).`	`VAR_027457`
`VARIANT`	`161 161`	`1`	`R -> Q (in AT3D; type-II; Geneva).`	`VAR_007054`
`VARIANT`	`167 167`	`1`	`N -> T.`	`VAR_012750`
`VARIANT`	`178 178`	`1`	`L -> H (in AT3D; type-I).`	`VAR_027458`
`VARIANT`	`179 179`	`1`	`F -> L (in AT3D; type-I).`	`VAR_027459`
`VARIANT`	`190 190`	`1`	`Y -> C (polymorphism in population of Scandinavian origin).`	`VAR_007055`
`VARIANT`	`198 198`	`1`	`Y -> C (in AT3D; type-I and -II; Whitechapel).`	`VAR_007056`
`VARIANT`	`198 198`	`1`	`Y -> H (in AT3D; type-I).`	`VAR_027460`
`VARIANT`	`214 214`	`1`	`S -> F (in AT3D; type-I).`	`VAR_027461`
`VARIANT`	`214 214`	`1`	`S -> Y (in AT3D; type-I).`	`VAR_007057`
`VARIANT`	`218 218`	`1`	`Missing (in AT3D; type-I).`	`VAR_027462`
`VARIANT`	`219 219`	`1`	`N -> D (in AT3D; type-II; Rouen-6; increases affinity for heparin).`	`VAR_007059`
`VARIANT`	`219 219`	`1`	`N -> K (in AT3D; type-II; Glasgow-3).`	`VAR_007058`
`VARIANT`	`223 223`	`1`	`S -> P (in AT3D; type-I).`	`VAR_027463`
`VARIANT`	`243 243`	`1`	`T -> I (in AT3D; type-I).`	`VAR_027464`
`VARIANT`	`251 251`	`1`	`I -> T (in AT3D; type-I).`	`VAR_027465`
`VARIANT`	`257 257`	`1`	`W -> R (in AT3D; type-I).`	`VAR_027466`
`VARIANT`	`261 261`	`1`	`F -> L (in AT3D).`	`VAR_027467`
`VARIANT`	`269 269`	`1`	`E -> K (in AT3D; type-II; Truro, increases affinity for heparin).`	`VAR_007060`
`VARIANT`	`273 307`	`35`	`Missing (in AT3D; type-I).`	`VAR_007061`
`VARIANT`	`283 283`	`1`	`M -> I (in AT3D; type-II).`	`VAR_007062`
`VARIANT`	`283 283`	`1`	`M -> V (in AT3D; type-II).`	`VAR_027468`
`VARIANT`	`302 302`	`1`	`L -> P (in AT3D; type-I).`	`VAR_007063`
`VARIANT`	`316 316`	`1`	`I -> N (in AT3D; type-II; Haslar/Whitechapel).`	`VAR_007064`
`VARIANT`	`323 323`	`1`	`S -> P (in AT3D).`	`VAR_027469`
`VARIANT`	`334 334`	`1`	`E -> K (in AT3D; type-II).`	`VAR_007065`
`VARIANT`	`344 344`	`1`	`Missing (in AT3D; type-I).`	`VAR_007066`
`VARIANT`	`381 381`	`1`	`S -> P (in AT3D; type-I).`	`VAR_007067`
`VARIANT`	`391 391`	`1`	`R -> Q.`	`VAR_007068`
`VARIANT`	`397 397`	`1`	`S -> P (in AT3D; type-I).`	`VAR_027470`
`VARIANT`	`398 398`	`1`	`D -> H (in AT3D; type-I).`	`VAR_027471`
`VARIANT`	`412 412`	`1`	`S -> R (in AT3D; type-I).`	`VAR_027472`
`VARIANT`	`414 414`	`1`	`A -> T (in AT3D; type-II; Hamilton/Glasgow-2; reduces interaction with thrombin by 90%).`	`VAR_007069`
`VARIANT`	`416 416`	`1`	`A -> P (in AT3D; type-II; Charleville/Sudbury/Vicenza/Cambridge-1).`	`VAR_007070`
`VARIANT`	`416 416`	`1`	`A -> S (in AT3D; type-II; Cambridge-2).`	`VAR_007071`
`VARIANT`	`419 419`	`1`	`A -> V (in AT3D; type-I).`	`VAR_007072`
`VARIANT`	`424 424`	`1`	`G -> D (in AT3D; type-II; Stockholm).`	`VAR_007073`
`VARIANT`	`425 425`	`1`	`R -> C (in AT3D; type-II; Northwick-Park/Milano-1/Frankfurt-1; deprived of inhibitory activity).`	`VAR_007075`
`VARIANT`	`425 425`	`1`	`R -> H (in AT3D; type-II; Glasgow/Sheffield/Chicago/Avranches/` `Kumamoto-2; increases affinity for heparin; deprived of inhibitory activity).`	`VAR_007074`
`VARIANT`	`425 425`	`1`	`R -> P (in AT3D; type-II; Pescara; deprived of inhibitory of activity).`	`VAR_007076`
`VARIANT`	`426 426`	`1`	`S -> L (in AT3D; type-II; Denver/Milano-2; deprived of inhibitory activity).`	`VAR_007077`
`VARIANT`	`434 434`	`1`	`F -> C (in AT3D; type-II; Rosny).`	`VAR_007078`
`VARIANT`	`434 434`	`1`	`F -> L (in AT3D; type-II; Maisons-Laffite).`	`VAR_007080`
`VARIANT`	`434 434`	`1`	`F -> S (in AT3D; type-II; Torino).`	`VAR_007079`
`VARIANT`	`436 436`	`1`	`A -> T (in AT3D; type-II; Oslo/Paris-3).`	`VAR_007081`
`VARIANT`	`437 437`	`1`	`N -> K (in AT3D; type-II; La Rochelle).`	`VAR_007082`
`VARIANT`	`438 438`	`1`	`R -> G (in AT3D; type-II).`	`VAR_009258`
`VARIANT`	`438 438`	`1`	`R -> M (in AT3D; type-II; Kyoto).`	`VAR_007083`
`VARIANT`	`439 439`	`1`	`P -> L (in AT3D; type-II; Utah; deprived of inhibitory activity).`	`VAR_007084`
`VARIANT`	`439 439`	`1`	`P -> T (in AT3D; type-II; Budapest-5).`	`VAR_007085`
`VARIANT`	`441 441`	`1`	`L -> P (in AT3D; type-II).`	`VAR_027473`
`VARIANT`	`453 453`	`1`	`I -> T (in AT3D; type-I).`	`VAR_007086`
`VARIANT`	`456 456`	`1`	`G -> R (in AT3D; type-I).`	`VAR_007087`
`VARIANT`	`457 457`	`1`	`R -> T (in AT3D; type-II).`	`VAR_007088`
`VARIANT`	`459 461`	`3`	`Missing (in AT3D; type-I).`	`VAR_007089`
`VARIANT`	`459 459`	`1`	`A -> D (in AT3D; type-I).`	`VAR_007090`
`VARIANT`	`461 461`	`1`	`P -> L (in AT3D; type-II; Budapest).`	`VAR_007091`
`VARIANT`	`462 462`	`1`	`C -> F (in AT3D; type-I).`	`VAR_007092`
`MUTAGEN`	`414 414`		`A->K: Reduces interaction with thrombin by 99%.`
`MUTAGEN`	`414 414`		`A->Q: Reduces interaction with thrombin by 80%.`
`CONFLICT`	`69 70`		`EQ -> QE (in Ref. 10; AA sequence).`
`CONFLICT`	`77 77`		`N -> NN (in Ref. 3; BAA06212).`
`CONFLICT`	`97 97`		`H -> R (in Ref. 5; AAG35525).`
`CONFLICT`	`120 120`		`A -> T (in Ref. 6; BAG35537).`
`CONFLICT`	`226 226`		`T -> A (in Ref. 6; BAG35537).`
`CONFLICT`	`247 249`		`Missing (in Ref. 10; AA sequence).`
`CONFLICT`	`388 388`		`Missing (in Ref. 13; AA sequence).`
`CONFLICT`	`395 395`		`Y -> YA (in Ref. 13; AA sequence).`
`TURN`	`39 41`	`3`
`TURN`	`44 46`	`3`
`HELIX`	`78 100`	`23`
`STRAND`	`108 110`	`3`
`HELIX`	`112 123`	`12`
`HELIX`	`128 137`	`10`
`HELIX`	`140 142`	`3`
`HELIX`	`145 149`	`5`
`HELIX`	`151 162`	`12`
`STRAND`	`168 181`	`14`
`HELIX`	`188 198`	`11`
`STRAND`	`203 205`	`3`
`TURN`	`207 209`	`3`
`HELIX`	`211 225`	`15`
`TURN`	`226 228`	`3`
`STRAND`	`245 259`	`15`
`HELIX`	`263 265`	`3`
`STRAND`	`267 271`	`5`
`STRAND`	`274 276`	`3`
`STRAND`	`279 294`	`16`
`HELIX`	`296 298`	`3`
`STRAND`	`300 306`	`7`
`STRAND`	`309 317`	`9`
`STRAND`	`320 322`	`3`
`HELIX`	`324 330`	`7`
`HELIX`	`333 342`	`10`
`STRAND`	`344 353`	`10`
`STRAND`	`355 358`	`4`
`HELIX`	`363 368`	`6`
`TURN`	`369 371`	`3`
`HELIX`	`374 376`	`3`
`TURN`	`378 380`	`3`
`TURN`	`384 386`	`3`
`STRAND`	`389 392`	`4`
`STRAND`	`398 407`	`10`
`STRAND`	`409 413`	`5`
`STRAND`	`440 446`	`7`
`TURN`	`447 449`	`3`
`STRAND`	`452 459`	`8`

Sequence information

Length: 464 AA [This is the length of the unprocessed precursor]

Molecular weight: 52602 Da [This is the MW of the unprocessed precursor]

CRC64: 9A4E324F00683D9D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MYSNVIGTVT SGKRKVYLLS LLLIGFWDCV TCHGSPVDIC TAKPRDIPMN PMCIYRSPEK 

        70         80         90        100        110        120 
KATEDEGSEQ KIPEATNRRV WELSKANSRF ATTFYQHLAD SKNDNDNIFL SPLSISTAFA 

       130        140        150        160        170        180 
MTKLGACNDT LQQLMEVFKF DTISEKTSDQ IHFFFAKLNC RLYRKANKSS KLVSANRLFG 

       190        200        210        220        230        240 
DKSLTFNETY QDISELVYGA KLQPLDFKEN AEQSRAAINK WVSNKTEGRI TDVIPSEAIN 

       250        260        270        280        290        300 
ELTVLVLVNT IYFKGLWKSK FSPENTRKEL FYKADGESCS ASMMYQEGKF RYRRVAEGTQ 

       310        320        330        340        350        360 
VLELPFKGDD ITMVLILPKP EKSLAKVEKE LTPEVLQEWL DELEEMMLVV HMPRFRIEDG 

       370        380        390        400        410        420 
FSLKEQLQDM GLVDLFSPEK SKLPGIVAEG RDDLYVSDAF HKAFLEVNEE GSEAAASTAV 

       430        440        450        460 
VIAGRSLNPN RVTFKANRPF LVFIREVPLN TIIFMGRVAN PCVK

P01008 in FASTA format

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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