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UniProtKB/Swiss-Prot entry P00750


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TPA_HUMAN
Primary accession number P00750
Secondary accession numbers A8K022 Q15103 Q503B0 Q6PJA5 Q7Z7N2 Q86YK8 Q9BU99 Q9BZW1
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 134)
Name and origin of the protein
Protein name Tissue-type plasminogen activator [Precursor]
Synonyms t-plasminogen activator
t-PA
tPA
EC 3.4.21.68
Alteplase
Reteplase
Contains Tissue-type plasminogen activator chain A
Tissue-type plasminogen activator chain B
Gene name
Name: PLAT
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Melanoma;
DOI=10.1038/301214a0; PubMed=6337343 [NCBI, ExPASy, EBI, Israel, Japan]
Pennica D., Holmes W.E., Kohr W.J., Harkins R.N., Vehar G.A., Ward C.A., Bennett W.F., Yelverton E., Seeburg P.H., Heyneker H.L., Goeddel D.V., Collen D.;
"Cloning and expression of human tissue-type plasminogen activator cDNA in E. coli.";
Nature 301:214-221(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6089198 [NCBI, ExPASy, EBI, Israel, Japan]
Ny T., Elgh F., Lund B.;
"The structure of the human tissue-type plasminogen activator gene: correlation of intron and exon structures to functional and structural domains.";
Proc. Natl. Acad. Sci. U.S.A. 81:5355-5359(1984).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3009482 [NCBI, ExPASy, EBI, Israel, Japan]
Friezner Degen S.J., Rajput B., Reich E.;
"The human tissue plasminogen activator gene.";
J. Biol. Chem. 261:6972-6985(1986).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3090401 [NCBI, ExPASy, EBI, Israel, Japan]
Harris T.J., Patel T., Marston F.A., Little S., Emtage J.S., Opdenakker G., Volckaert G., Rombauts W., Billiau A., Somer P.;
"Cloning of cDNA coding for human tissue-type plasminogen activator and its expression in Escherichia coli.";
Mol. Biol. Med. 3:279-292(1986).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2824147 [NCBI, ExPASy, EBI, Israel, Japan]
Reddy V.B., Garramone A.J., Sasak H., Wei C.-M., Watkins P., Galli J., Hsiung N.;
"Expression of human uterine tissue-type plasminogen activator in mouse cells using BPV vectors.";
DNA 6:461-472(1987).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal lung;
DOI=10.1093/nar/16.12.5695; PubMed=3133640 [NCBI, ExPASy, EBI, Israel, Japan]
Sasaki H., Saito Y., Hayashi M., Otsuka K., Niwa M.;
"Nucleotide sequence of the tissue-type plasminogen activator cDNA from human fetal lung cells.";
Nucleic Acids Res. 16:5695-5695(1988).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Umbilical vein;
DOI=10.1093/nar/18.4.1086; PubMed=2107528 [NCBI, ExPASy, EBI, Israel, Japan]
Siebert P.D., Fong K.;
"Variant tissue-type plasminogen activator (PLAT) cDNA obtained from human endothelial cells.";
Nucleic Acids Res. 18:1086-1086(1990).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Dou D.;
"A brain-type plasminogen activator.";
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Liu Y., Xu L., Zeng Y., He X.;
"cDNA of tissue plasminogen activator.";
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASP-34; SER-136; THR-146 AND TRP-164.
SeattleSNPs program for genomic applications;
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[13]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Brain, Placenta, and Skin;
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).
[15]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
PubMed=3161893 [NCBI, ExPASy, EBI, Israel, Japan]
Fisher R., Waller E.K., Grossi G., Thompson D., Tizard R., Schleuning W.-D.;
"Isolation and characterization of the human tissue-type plasminogen activator structural gene including its 5' flanking region.";
J. Biol. Chem. 260:11223-11230(1985).
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 31-562.
PubMed=1368681 [NCBI, ExPASy, EBI, Israel, Japan]
Itagaki Y., Yasuda H., Morinaga T., Mitsuda S., Higashio K.;
"Purification and characterization of tissue plasminogen activator secreted by human embryonic lung diploid fibroblasts, IMR-90 cells.";
Agric. Biol. Chem. 55:1225-1232(1991).
[17]
PROTEIN SEQUENCE OF 33-52 AND 311-330.
TISSUE=Melanoma;
PubMed=6682760 [NCBI, ExPASy, EBI, Israel, Japan]
Wallen P., Pohl G., Bergsdorf N., Raanby M., Ny T., Joernvall H.;
"Purification and characterization of a melanoma cell plasminogen activator.";
Eur. J. Biochem. 132:681-686(1983).
[18]
PROTEIN SEQUENCE OF 36-562.
TISSUE=Melanoma;
DOI=10.1021/bi00311a020; PubMed=6433976 [NCBI, ExPASy, EBI, Israel, Japan]
Pohl G., Kaellstroem M., Bergsdorf N., Wallen P., Joernvall H.;
"Tissue plasminogen activator: peptide analyses confirm an indirectly derived amino acid sequence, identify the active site serine residue, establish glycosylation sites, and localize variant differences.";
Biochemistry 23:3701-3707(1984).
[19]
NUCLEOTIDE SEQUENCE [MRNA] OF 251-358.
PubMed=6572897 [NCBI, ExPASy, EBI, Israel, Japan]
Edlund T., Ny T., Raanby M., Heden L.-O., Palm G., Holmgren E., Josephson S.;
"Isolation of cDNA sequences coding for a part of human tissue plasminogen activator.";
Proc. Natl. Acad. Sci. U.S.A. 80:349-352(1983).
[20]
PARTIAL PROTEIN SEQUENCE, AND SIGNAL SEQUENCE CLEAVAGE SITE.
Jalah R., Pavlakis G.N., Felber B.J.;
Submitted (JUL-2007) to UniProtKB.
[21]
STRUCTURE OF CARBOHYDRATES.
PubMed=2513186 [NCBI, ExPASy, EBI, Israel, Japan]
Pfeiffer G., Schmidt M., Strube K.-H., Geyer R.;
"Carbohydrate structure of recombinant human uterine tissue plasminogen activator expressed in mouse epithelial cells.";
Eur. J. Biochem. 186:273-286(1989).
[22]
GLYCOSYLATION AT THR-96.
DOI=10.1021/bi00223a004; PubMed=1900431 [NCBI, ExPASy, EBI, Israel, Japan]
Harris R.J., Leonard C.K., Guzzetta A.W., Spellman M.W.;
"Tissue plasminogen activator has an O-linked fucose attached to threonine-61 in the epidermal growth factor domain.";
Biochemistry 30:2311-2314(1991).
[23]
DISULFIDE BONDS IN KRINGLE 2.
PubMed=1645336 [NCBI, ExPASy, EBI, Israel, Japan]
Vlahos C.J., Wilhelm O.G., Hassell T., Jaskunas S.R., Bang N.U.;
"Disulfide pairing of the recombinant kringle-2 domain of tissue plasminogen activator produced in Escherichia coli.";
J. Biol. Chem. 266:10070-10072(1991).
[24]
INTERACTION WITH LRP1B.
DOI=10.1074/jbc.M102727200; PubMed=11384978 [NCBI, ExPASy, EBI, Israel, Japan]
Liu C.-X., Li Y., Obermoeller-McCormick L.M., Schwartz A.L., Bu G.;
"The putative tumor suppressor LRP1B, a novel member of the low density lipoprotein (LDL) receptor family, exhibits both overlapping and distinct properties with the LDL receptor-related protein.";
J. Biol. Chem. 276:28889-28896(2001).
[25]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
DOI=10.1186/gb-2004-5-2-r8; PubMed=14759258 [NCBI, ExPASy, EBI, Israel, Japan]
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:RESEARCH008.1-RESEARCH008.16(2004).
[26]
STRUCTURE BY NMR OF KRINGLE 2.
DOI=10.1021/bi00450a016; PubMed=2558718 [NCBI, ExPASy, EBI, Israel, Japan]
Byeon I.-J.L., Kelley R.F., Llinas M.;
"1H NMR structural characterization of a recombinant kringle 2 domain from human tissue-type plasminogen activator.";
Biochemistry 28:9350-9360(1989).
[27]
STRUCTURE BY NMR OF KRINGLE 2.
PubMed=1901789 [NCBI, ExPASy, EBI, Israel, Japan]
Byeon I.-J.L., Kelley R.F., Llinas M.;
"Kringle-2 domain of the tissue-type plasminogen activator. 1H-NMR assignments and secondary structure.";
Eur. J. Biochem. 197:155-165(1991).
[28]
STRUCTURE BY NMR OF KRINGLE 2.
DOI=10.1016/0022-2836(91)90592-T; PubMed=1762144 [NCBI, ExPASy, EBI, Israel, Japan]
Byeon I.-J.L., Llinas M.;
"Solution structure of the tissue-type plasminogen activator kringle 2 domain complexed to 6-aminohexanoic acid an antifibrinolytic drug.";
J. Mol. Biol. 222:1035-1051(1991).
[29]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF KRINGLE 2.
DOI=10.1021/bi00116a037; PubMed=1310033 [NCBI, ExPASy, EBI, Israel, Japan]
de Vos A., Ultsch M.H., Kelley R.F., Padmanabhan K., Tulinskly A., Westbrook M.L., Kossiakof A.A.;
"Crystal structure of the kringle 2 domain of tissue plasminogen activator at 2.4-A resolution.";
Biochemistry 31:270-279(1992).
[30]
STRUCTURE BY NMR OF 38-85.
DOI=10.1016/0022-2836(92)90403-7; PubMed=1602484 [NCBI, ExPASy, EBI, Israel, Japan]
Downing A.K., Driscoll P.C., Harvey T.S., Dudgeon T.J., Smith B.O., Baron M., Campbell I.D.;
"Solution structure of the fibrin binding finger domain of tissue-type plasminogen activator determined by 1H nuclear magnetic resonance.";
J. Mol. Biol. 225:821-833(1992).
[31]
STRUCTURE BY NMR OF 36-126.
DOI=10.1016/S0969-2126(01)00217-9; PubMed=7582899 [NCBI, ExPASy, EBI, Israel, Japan]
Smith B.O., Downing A.K., Driscoll P.C., Dudgeon T.J., Campbell I.D.;
"The solution structure and backbone dynamics of the fibronectin type I and epidermal growth factor-like pair of modules of tissue-type plasminogen activator.";
Structure 3:823-833(1995).
[32]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF CATALYTIC DOMAIN.
DOI=10.1006/jmbi.1996.0238; PubMed=8613982 [NCBI, ExPASy, EBI, Israel, Japan]
Lamba D., Bauer M., Huber R., Fischer S., Rudolph R., Kohnert U., Bode W.;
"The 2.3 A crystal structure of the catalytic domain of recombinant two-chain human tissue-type plasminogen activator.";
J. Mol. Biol. 258:117-135(1996).
[33]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF CATALYTIC DOMAIN.
DOI=10.1093/emboj/16.16.4797; PubMed=9305622 [NCBI, ExPASy, EBI, Israel, Japan]
Renatus M., Engh R.A., Stubbs M.T., Huber R., Fischer S., Kohnert U., Bode W.;
"Lysine 156 promotes the anomalous proenzyme activity of tPA: X-ray crystal structure of single-chain human tPA.";
EMBO J. 16:4797-4805(1997).
Comments
  • FUNCTION: Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events. Play a direct role in facilitating neuronal migration.
  • CATALYTIC ACTIVITY: Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin.
  • SUBUNIT: Heterodimer of chain A and chain B held by a disulfide bond. Binds to fibrin with high affinity. This interaction leads to an increase in the catalytic efficiency of the enzyme between 100-fold and 1000-fold, due to an increase in affinity for plasminogen. Similarly, binding to heparin increases the activation of plasminogen. Binds to annexin A2, cytokeratin-8, fibronectin and laminin. Binds to mannose receptor and the low-density lipoprotein receptor-related protein (LRP1); these proteins are involved in TPA clearance. Yet unidentified interactions on endothelial cells and vascular smooth muscle cells (VSMC) lead to a 100-fold stimulation of plasminogen activation. In addition, binding to VSMC reduces TPA inhibition by PAI-1 by 30-fold. Binds LRP1B; binding is followed by internalization and degradation.
  • SUBCELLULAR LOCATION: Secreted, extracellular space.
  • ALTERNATIVE PRODUCTS: 4 named isoforms [FASTA] produced by alternative splicing.
    Name1
    SynonymsLong
    Isoform IDP00750-1
    This is the isoform sequence displayed in this entry.
    Name2
    SynonymsShort
    Isoform IDP00750-2
    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
    Features which should be applied to build the isoform sequence: VSP_005411, VSP_005412.
    Name3
    Isoform IDP00750-3
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_015957.
    Name4
    SynonymsNeonatal
    Isoform IDP00750-4
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_028029, VSP_028030.
  • TISSUE SPECIFICITY: Synthesized in numerous tissues (including tumors) and secreted into most extracellular body fluids, such as plasma, uterine fluid, saliva, gingival crevicular fluid, tears, seminal fluid, and milk.
  • DOMAIN: Both FN1 and one of the kringle domains are required for binding to fibrin.
  • DOMAIN: Both FN1 and EGF-like domains are important for binding to LRP1.
  • DOMAIN: The FN1 domain mediates binding to annexin A2.
  • DOMAIN: The second kringle domain is implicated in binding to cytokeratin-8 and to the endothelial cell surface binding site.
  • PTM: The single chain, almost fully active enzyme, can be further processed into a two-chain fully active form by a cleavage after Arg-310 catalyzed by plasmin, tissue kallikrein or factor Xa.
  • PTM: Differential cell-specific N-linked glycosylation gives rise to two glycoforms, type I (glycosylated at Asn-219) and type II (not glycosylated at Asn-219). The single chain type I glycoform is less readily converted into the two-chain form by plasmin, and the two-chain type I glycoform has a lower activity than the two-chain type II glycoform in the presence of fibrin.
  • PTM: N-glycosylation of Asn-152; the bound oligomannosidic glycan is involved in the interaction with the mannose receptor.
  • PTM: Characterization of O-linked glycan was studied in Bowes melanoma cell line.
  • DISEASE: Increased activity of TPA is the cause of hyperfibrinolysis [MIM:173370]. Hyperfibrinolysis leads to excessive bleeding. Defective release of TPA causes hypofibrinolysis, leading to thrombosis or embolism.
  • PHARMACEUTICAL: Available under the names Activase (Genentech) and Retavase (Centocor and Roche) [Retavase is a fragment of TPA that contains kringle 2 and the protease domain; it was also known as BM 06.022]. Used in Acute Myocardial Infarction (AMI), in Acute Ischemic Stroke (AIS) and Pulmonary Embolism (PE) to initiate fibrinolysis.
  • SIMILARITY: Belongs to the peptidase S1 family [view classification].
  • SIMILARITY: Contains 1 EGF-like domain.
  • SIMILARITY: Contains 1 fibronectin type-I domain.
  • SIMILARITY: Contains 2 kringle domains.
  • SIMILARITY: Contains 1 peptidase S1 domain [view classification].
  • WEB RESOURCE: Name=Wikipedia; Note=Tissue plasminogen activator entry; URL="http://en.wikipedia.org/wiki/Tissue_plasminogen_Activator";.
  • WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/plat/";.
  • 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=PLAT";.
  • WEB RESOURCE: Name=Activase; Note=Clinical information on Activase; URL="http://www.gene.com/gene/products/information/cardiovascular/activase/index.jsp";.
  • WEB RESOURCE: Name=Retavase; Note=Clinical information on Retavase; URL="http://www.retavase.com/pdf/Retavase_PI.pdf";.
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
L00153; AAB59510.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00141; AAB59510.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00142; AAB59510.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00143; AAB59510.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00144; AAB59510.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00145; AAB59510.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00146; AAB59510.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00147; AAB59510.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00148; AAB59510.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00149; AAB59510.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00150; AAB59510.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00151; AAB59510.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K03021; AAA98809.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M15518; AAA60111.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M18182; AAA36800.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X07393; CAA30302.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13097; CAA31489.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF260825; AAK11956.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY221101; AAO34406.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK289387; BAF82076.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK290575; BAF83264.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT007060; AAP35709.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY291060; AAP34246.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471080; EAW63235.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002795; AAH02795.3; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007231; AAH07231.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013968; AAH13968.3; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC018636; AAH18636.3; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC095403; AAH95403.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M11890; AAA61213.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M11889; AAA61213.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D01096; BAA00881.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
V00570; CAA23833.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
A07197; CAA00642.1; -; Unassigned_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
A01465; CAA00166.1; -; Unassigned_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A94004; UKHUT.
I38098; I38098.
RefSeq NP_000921.1; -.
NP_127509.1; -.
UniGene Hs.491582
3D structure databases
PDB
1A5H; X-ray; 2.90 A; A/B=311-562, C/D=298-304.[ExPASy / RCSB / EBI]
1BDA; X-ray; 3.35 A; A/B=298-562.[ExPASy / RCSB / EBI]
1PK2; NMR; -; A=209-298.[ExPASy / RCSB / EBI]
1PML; X-ray; 2.38 A; A/B/C=213-298.[ExPASy / RCSB / EBI]
1RTF; X-ray; 2.30 A; B=311-562.[ExPASy / RCSB / EBI]
1TPG; NMR; -; A=36-126.[ExPASy / RCSB / EBI]
1TPK; X-ray; 2.40 A; A/B/C=211-298.[ExPASy / RCSB / EBI]
1TPM; NMR; -; A=36-85.[ExPASy / RCSB / EBI]
1TPN; NMR; -; A=36-85.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1A5H; -.
1BDA; -.
1PK2; -.
1PML; -.
1RTF; -.
1TPG; -.
1TPK; -.
1TPM; -.
1TPN; -.
SMR P00750; 298-562.
ModBase P00750.
Protein family/group databases
MEROPS S01.232; -.
PTM databases
GlycoSuiteDB P00750; -.
Enzyme and pathway databases
Reactome REACT_604; Hemostasis.
Organism-specific databases
H-InvDB HIX0007476; -.
HGNC HGNC:9051; PLAT.
GenAtlas PLAT.
HPA CAB009335; -.
HPA003412; -.
MIM 173370; gene+phenotype. [NCBI / EBI]
PharmGKB PA33381; -.
GeneCards P00750.
Gene expression databases
ArrayExpress P00750; -.
CleanEx HS_PLAT; -.
GermOnline ENSG00000104368; Homo sapiens.
Ontologies
GO
GO:0005856; Cellular component: cytoskeleton (inferred from direct assay from HPA).
GO:0005576; Cellular component: extracellular region (inferred from experiment from Reactome).
GO:0007596; Biological process: blood coagulation (traceable author statement from ProtInc).
GO:0006464; Biological process: protein modification process (traceable author statement from ProtInc).
GO:0006508; Biological process: proteolysis (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR016060; Complement_control_module.
IPR006210; EGF.
IPR000742; EGF_3.
IPR006209; EGF_like.
IPR013032; EGF_like_reg_CS.
IPR000083; Fibrnctn1.
IPR000001; Kringle.
IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
Graphical view of domain structure.
Gene3D G3DSA:2.10.70.10; Complement_control_module; 1.
G3DSA:2.40.20.10; Kringle; 2.
Pfam PF00008; EGF; 1.
PF00039; fn1; 1.
PF00051; Kringle; 2.
PF00089; Trypsin; 1.
Pfam graphical view of domain structure.
PRINTS PR00722; CHYMOTRYPSIN.
PR00018; KRINGLE.
ProDom PD000395; Kringle; 2.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00181; EGF; 1.
SM00058; FN1; 1.
SM00130; KR; 2.
SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.
PROSITE PS00022; EGF_1; 1.
PS01186; EGF_2; 1.
PS50026; EGF_3; 1.
PS01253; FN1_1; 1.
PS51091; FN1_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).
BLOCKS P00750.
ProtoNet P00750.
Other
SWISS-3DIMAGE P00750.
Genome annotation databases
Ensembl ENSG00000104368; Homo sapiens. [Contig view]
GeneID 5327; -.
KEGG hsa:5327; -.
Phylogenomic databases
HOGENOM P00750; -.
HOVERGEN P00750; -.
Other
DrugBank DB00009; Alteplase.
DB00513; Aminocaproic Acid.
DB00029; Anistreplase.
DB01088; Iloprost.
DB00015; Reteplase.
DB00031; Tenecteplase.
DB00302; Tranexamic Acid.
DB00013; Urokinase.
LinkHub P00750; -.
NextBio 20622; -.
SOURCE PLAT; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Cleavage on pair of basic residues; Direct protein sequencing; EGF-like domain; Glycoprotein; Hydrolase; Kringle; Pharmaceutical; Plasminogen activation; Polymorphism; Protease; Repeat; Secreted; Serine protease; Signal; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    22  22      
PROPEP   23    32  10      PRO_0000028348
PROPEP   33    35  3     Removed by plasmin. PRO_0000028349
CHAIN   36   562  527     Tissue-type plasminogen activator. PRO_0000028350
CHAIN   36   310  275     Tissue-type plasminogen activator chain A. PRO_0000028351
CHAIN   311   562  252     Tissue-type plasminogen activator chain B. PRO_0000028352
DOMAIN   39    81  43     Fibronectin type-I. 
DOMAIN   82   120  39     EGF-like. 
DOMAIN   127   208  82     Kringle 1. 
DOMAIN   215   296  82     Kringle 2.