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Tissue-type plasminogen activator (t-PA) (t-plasminogen activator) (tPA) (EC 3.4.21.68) (Alteplase) (Reteplase) [Cleaved into: Tissue-type plasminogen activator chain A; Tissue-type plasminogen activator chain B]

 TPA_HUMAN               Reviewed;         562 AA.
P00750; A8K022; B2R8E8; Q15103; Q503B0; Q6PJA5; Q7Z7N2; Q86YK8;
Q9BU99; Q9BZW1;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
25-OCT-2017, entry version 233.
RecName: Full=Tissue-type plasminogen activator;
Short=t-PA;
Short=t-plasminogen activator;
Short=tPA;
EC=3.4.21.68;
AltName: INN=Alteplase;
AltName: INN=Reteplase;
Contains:
RecName: Full=Tissue-type plasminogen activator chain A;
Contains:
RecName: Full=Tissue-type plasminogen activator chain B;
Flags: Precursor;
Name=PLAT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Melanoma;
PubMed=6337343; DOI=10.1038/301214a0;
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; DOI=10.1073/pnas.81.17.5355;
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;
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;
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; DOI=10.1089/dna.1987.6.461;
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;
PubMed=3133640; DOI=10.1093/nar/16.12.5695;
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;
PubMed=2107528; DOI=10.1093/nar/18.4.1086;
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] (ISOFORMS 1 AND 3).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
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 variation discovery resource;
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;
PubMed=15489334; DOI=10.1101/gr.2596504;
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;
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; DOI=10.1271/bbb1961.55.1225;
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; DOI=10.1111/j.1432-1033.1983.tb07418.x;
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;
PubMed=6433976; DOI=10.1021/bi00311a020;
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; DOI=10.1073/pnas.80.2.349;
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]
GLYCOSYLATION AT ASN-152; ASN-219 AND ASN-483, AND STRUCTURE OF
CARBOHYDRATES.
PubMed=2513186; DOI=10.1111/j.1432-1033.1989.tb15206.x;
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.
PubMed=1900431; DOI=10.1021/bi00223a004;
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 DOMAIN.
PubMed=1645336;
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]
ENZYME REGULATION, AND HETERODIMER WITH SERPINA5.
PubMed=10340997; DOI=10.1093/molehr/5.6.513;
He S., Lin Y.L., Liu Y.X.;
"Functionally inactive protein C inhibitor in seminal plasma may be
associated with infertility.";
Mol. Hum. Reprod. 5:513-519(1999).
[25]
INTERACTION WITH LRP1B.
PubMed=11384978; DOI=10.1074/jbc.M102727200;
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).
[26]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[27]
STRUCTURE BY NMR OF KRINGLE 2.
PubMed=2558718; DOI=10.1021/bi00450a016;
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).
[28]
STRUCTURE BY NMR OF KRINGLE 2.
PubMed=1901789; DOI=10.1111/j.1432-1033.1991.tb15894.x;
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).
[29]
STRUCTURE BY NMR OF KRINGLE 2.
PubMed=1762144; DOI=10.1016/0022-2836(91)90592-T;
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).
[30]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF KRINGLE 2.
PubMed=1310033; DOI=10.1021/bi00116a037;
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).
[31]
STRUCTURE BY NMR OF 38-85.
PubMed=1602484; DOI=10.1016/0022-2836(92)90403-7;
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).
[32]
STRUCTURE BY NMR OF 36-126.
PubMed=7582899; DOI=10.1016/S0969-2126(01)00217-9;
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).
[33]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF CATALYTIC DOMAIN.
PubMed=8613982; DOI=10.1006/jmbi.1996.0238;
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).
[34]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF CATALYTIC DOMAIN.
PubMed=9305622; DOI=10.1093/emboj/16.16.4797;
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).
-!- 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. Plays a direct role in
facilitating neuronal migration.
-!- CATALYTIC ACTIVITY: Specific cleavage of Arg-|-Val bond in
plasminogen to form plasmin.
-!- ENZYME REGULATION: Inhibited by SERPINA5.
{ECO:0000269|PubMed:10340997}.
-!- SUBUNIT: Heterodimer of chain A and chain B held by a disulfide
bond. Forms a heterodimer with SERPINA5. 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:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=Long;
IsoId=P00750-1; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=P00750-2; Sequence=VSP_005411, VSP_005412;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=3;
IsoId=P00750-3; Sequence=VSP_015957;
Note=No experimental confirmation available.;
Name=4; Synonyms=Neonatal;
IsoId=P00750-4; Sequence=VSP_028029, VSP_028030;
Note=No experimental confirmation available.;
-!- 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.
{ECO:0000269|PubMed:1900431}.
-!- PTM: N-glycosylation of Asn-152; the bound oligomannosidic glycan
is involved in the interaction with the mannose receptor.
{ECO:0000269|PubMed:1900431}.
-!- PTM: Characterization of O-linked glycan was studied in Bowes
melanoma cell line. {ECO:0000269|PubMed:1900431}.
-!- DISEASE: Note=Increased activity of TPA results in increased
fibrinolysis of fibrin blood clots that is associated with
excessive bleeding. Defective release of TPA results in
hypofibrinolysis that can lead to thrombosis or embolism.
{ECO:0000269|PubMed:1762144}.
-!- 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.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Tissue plasminogen activator
entry;
URL="https://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";
-!- WEB RESOURCE: Name=Chiesi; Note=Clinical information on Retavase;
URL="https://chiesiusa.com/products/retavase-2/";
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EMBL; L00153; AAB59510.1; -; Genomic_DNA.
EMBL; L00141; AAB59510.1; JOINED; Genomic_DNA.
EMBL; L00142; AAB59510.1; JOINED; Genomic_DNA.
EMBL; L00143; AAB59510.1; JOINED; Genomic_DNA.
EMBL; L00144; AAB59510.1; JOINED; Genomic_DNA.
EMBL; L00145; AAB59510.1; JOINED; Genomic_DNA.
EMBL; L00146; AAB59510.1; JOINED; Genomic_DNA.
EMBL; L00147; AAB59510.1; JOINED; Genomic_DNA.
EMBL; L00148; AAB59510.1; JOINED; Genomic_DNA.
EMBL; L00149; AAB59510.1; JOINED; Genomic_DNA.
EMBL; L00150; AAB59510.1; JOINED; Genomic_DNA.
EMBL; L00151; AAB59510.1; JOINED; Genomic_DNA.
EMBL; K03021; AAA98809.1; -; Genomic_DNA.
EMBL; M15518; AAA60111.1; -; mRNA.
EMBL; M18182; AAA36800.1; -; mRNA.
EMBL; X07393; CAA30302.1; -; mRNA.
EMBL; X13097; CAA31489.1; -; mRNA.
EMBL; AF260825; AAK11956.1; -; mRNA.
EMBL; AY221101; AAO34406.1; -; mRNA.
EMBL; AK289387; BAF82076.1; -; mRNA.
EMBL; AK290575; BAF83264.1; -; mRNA.
EMBL; AK313342; BAG36145.1; -; mRNA.
EMBL; BT007060; AAP35709.1; -; mRNA.
EMBL; AY291060; AAP34246.1; -; Genomic_DNA.
EMBL; CH471080; EAW63235.1; -; Genomic_DNA.
EMBL; CH471080; EAW63233.1; -; Genomic_DNA.
EMBL; BC002795; AAH02795.3; -; mRNA.
EMBL; BC007231; AAH07231.1; -; mRNA.
EMBL; BC013968; AAH13968.3; -; mRNA.
EMBL; BC018636; AAH18636.3; -; mRNA.
EMBL; BC095403; AAH95403.1; -; mRNA.
EMBL; M11890; AAA61213.1; -; Genomic_DNA.
EMBL; M11889; AAA61213.1; JOINED; Genomic_DNA.
EMBL; D01096; BAA00881.1; -; mRNA.
EMBL; V00570; CAA23833.1; -; mRNA.
CCDS; CCDS6126.1; -. [P00750-1]
CCDS; CCDS6127.1; -. [P00750-3]
PIR; A94004; UKHUT.
PIR; I38098; I38098.
RefSeq; NP_000921.1; NM_000930.4. [P00750-1]
RefSeq; NP_001306118.1; NM_001319189.1.
RefSeq; NP_127509.1; NM_033011.3. [P00750-3]
UniGene; Hs.491582; -.
PDB; 1A5H; X-ray; 2.90 A; A/B=311-562, C/D=298-304.
PDB; 1BDA; X-ray; 3.35 A; A/B=298-562.
PDB; 1PK2; NMR; -; A=209-298.
PDB; 1PML; X-ray; 2.38 A; A/B/C=213-298.
PDB; 1RTF; X-ray; 2.30 A; B=311-562.
PDB; 1TPG; NMR; -; A=36-126.
PDB; 1TPK; X-ray; 2.40 A; A/B/C=211-298.
PDB; 1TPM; NMR; -; A=36-85.
PDB; 1TPN; NMR; -; A=36-85.
PDB; 5BRR; X-ray; 3.16 A; E=311-562.
PDBsum; 1A5H; -.
PDBsum; 1BDA; -.
PDBsum; 1PK2; -.
PDBsum; 1PML; -.
PDBsum; 1RTF; -.
PDBsum; 1TPG; -.
PDBsum; 1TPK; -.
PDBsum; 1TPM; -.
PDBsum; 1TPN; -.
PDBsum; 5BRR; -.
ProteinModelPortal; P00750; -.
SMR; P00750; -.
BioGrid; 111343; 40.
ELM; P00750; -.
IntAct; P00750; 2.
MINT; MINT-8309345; -.
STRING; 9606.ENSP00000220809; -.
BindingDB; P00750; -.
ChEMBL; CHEMBL1873; -.
DrugBank; DB07684; 5-(DIMETHYLAMINO)-2-NAPHTHALENESULFONIC ACID.
DrugBank; DB00513; Aminocaproic Acid.
DrugBank; DB06404; C1 Esterase Inhibitor (Human).
DrugBank; DB09228; C1 Esterase Inhibitor (Recombinant).
DrugBank; DB01050; Ibuprofen.
DrugBank; DB01088; Iloprost.
DrugBank; DB00013; Urokinase.
GuidetoPHARMACOLOGY; 2392; -.
MEROPS; S01.232; -.
iPTMnet; P00750; -.
PhosphoSitePlus; P00750; -.
UniCarbKB; P00750; -.
BioMuta; PLAT; -.
DMDM; 137119; -.
EPD; P00750; -.
MaxQB; P00750; -.
PaxDb; P00750; -.
PeptideAtlas; P00750; -.
PRIDE; P00750; -.
DNASU; 5327; -.
Ensembl; ENST00000220809; ENSP00000220809; ENSG00000104368. [P00750-1]
Ensembl; ENST00000352041; ENSP00000270188; ENSG00000104368. [P00750-3]
Ensembl; ENST00000429089; ENSP00000392045; ENSG00000104368. [P00750-1]
GeneID; 5327; -.
KEGG; hsa:5327; -.
UCSC; uc003xos.3; human. [P00750-1]
CTD; 5327; -.
DisGeNET; 5327; -.
EuPathDB; HostDB:ENSG00000104368.17; -.
GeneCards; PLAT; -.
HGNC; HGNC:9051; PLAT.
HPA; CAB009335; -.
HPA; HPA003412; -.
MalaCards; PLAT; -.
MIM; 173370; gene.
neXtProt; NX_P00750; -.
OpenTargets; ENSG00000104368; -.
PharmGKB; PA33381; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000119133; -.
HOVERGEN; HBG008633; -.
InParanoid; P00750; -.
KO; K01343; -.
OMA; AHVRLYP; -.
OrthoDB; EOG091G0AH5; -.
PhylomeDB; P00750; -.
TreeFam; TF329901; -.
BRENDA; 3.4.21.68; 2681.
Reactome; R-HSA-186797; Signaling by PDGF.
Reactome; R-HSA-75205; Dissolution of Fibrin Clot.
SIGNOR; P00750; -.
ChiTaRS; PLAT; human.
EvolutionaryTrace; P00750; -.
GeneWiki; Tissue_plasminogen_activator; -.
GenomeRNAi; 5327; -.
PMAP-CutDB; B2R8E8; -.
PRO; PR:P00750; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000104368; -.
ExpressionAtlas; P00750; baseline and differential.
Genevisible; P00750; HS.
GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0030141; C:secretory granule; IEA:Ensembl.
GO; GO:0051219; F:phosphoprotein binding; IPI:AgBase.
GO; GO:0005102; F:receptor binding; IPI:AgBase.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:BHF-UCL.
GO; GO:0007596; P:blood coagulation; TAS:ProtInc.
GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc.
GO; GO:0042730; P:fibrinolysis; TAS:Reactome.
GO; GO:0045861; P:negative regulation of proteolysis; IDA:BHF-UCL.
GO; GO:0031639; P:plasminogen activation; IDA:UniProtKB.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0006508; P:proteolysis; TAS:ProtInc.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0014909; P:smooth muscle cell migration; IEA:Ensembl.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000083; Fibronectin_type1.
InterPro; IPR000001; Kringle.
InterPro; IPR013806; Kringle-like.
InterPro; IPR018056; Kringle_CS.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR026280; Tissue_plasm_act.
InterPro; IPR034811; tPA.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
PANTHER; PTHR44617; PTHR44617; 1.
Pfam; PF00008; EGF; 1.
Pfam; PF00039; fn1; 1.
Pfam; PF00051; Kringle; 2.
Pfam; PF00089; Trypsin; 1.
PIRSF; PIRSF001145; Tissue_plasm_act; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00058; FN1; 1.
SMART; SM00130; KR; 2.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57440; SSF57440; 2.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS01253; FN1_1; 1.
PROSITE; PS51091; FN1_2; 1.
PROSITE; PS00021; KRINGLE_1; 2.
PROSITE; PS50070; KRINGLE_2; 2.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disulfide bond; EGF-like domain;
Glycoprotein; Hydrolase; Kringle; Pharmaceutical;
Plasminogen activation; Polymorphism; Protease; Reference proteome;
Repeat; Secreted; Serine protease; Signal; Zymogen.
SIGNAL 1 22 {ECO:0000269|Ref.20}.
PROPEP 23 32 {ECO:0000269|PubMed:6682760}.
/FTId=PRO_0000028348.
PROPEP 33 35 Removed by plasmin.
{ECO:0000269|PubMed:6433976}.
/FTId=PRO_0000028349.
CHAIN 36 562 Tissue-type plasminogen activator.
/FTId=PRO_0000028350.
CHAIN 36 310 Tissue-type plasminogen activator chain
A.
/FTId=PRO_0000028351.
CHAIN 311 562 Tissue-type plasminogen activator chain
B.
/FTId=PRO_0000028352.
DOMAIN 39 81 Fibronectin type-I. {ECO:0000255|PROSITE-
ProRule:PRU00478}.
DOMAIN 82 120 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 127 208 Kringle 1. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 215 296 Kringle 2. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 311 561 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
REGION 42 52 Important for binding to annexin A2.
ACT_SITE 357 357 Charge relay system.
ACT_SITE 406 406 Charge relay system.
ACT_SITE 513 513 Charge relay system.
SITE 102 102 Important for binding to LRP1.
SITE 253 253 Not glycosylated.
SITE 464 464 Important for single-chain activity.
SITE 512 512 Important for single-chain activity.
CARBOHYD 96 96 O-linked (Fuc) threonine.
{ECO:0000269|PubMed:1900431}.
/FTId=CAR_000029.
CARBOHYD 152 152 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:2513186}.
CARBOHYD 219 219 N-linked (GlcNAc...) asparagine; partial.
{ECO:0000269|PubMed:2513186}.
/FTId=CAR_000030.
CARBOHYD 483 483 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:2513186}.
/FTId=CAR_000031.
DISULFID 41 71 {ECO:0000269|PubMed:1645336}.
DISULFID 69 78 {ECO:0000269|PubMed:1645336}.
DISULFID 86 97 {ECO:0000269|PubMed:1645336}.
DISULFID 91 108 {ECO:0000269|PubMed:1645336}.
DISULFID 110 119 {ECO:0000269|PubMed:1645336}.
DISULFID 127 208 {ECO:0000250}.
DISULFID 148 190 {ECO:0000250}.
DISULFID 179 203 {ECO:0000250}.
DISULFID 215 296 {ECO:0000269|PubMed:1645336}.
DISULFID 236 278 {ECO:0000269|PubMed:1645336}.
DISULFID 267 291 {ECO:0000269|PubMed:1645336}.
DISULFID 299 430 Interchain (between A and B chains).
{ECO:0000255|PROSITE-ProRule:PRU00076,
ECO:0000255|PROSITE-ProRule:PRU00121,
ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000255|PROSITE-ProRule:PRU00478,
ECO:0000269|PubMed:1645336}.
DISULFID 342 358 {ECO:0000250}.
DISULFID 350 419 {ECO:0000250}.
DISULFID 444 519 {ECO:0000250}.
DISULFID 476 492 {ECO:0000250}.
DISULFID 509 537 {ECO:0000250}.
VAR_SEQ 1 40 MDAMKRGLCCVLLLCGAVFVSPSQEIHARFRRGARSYQVI
-> MAS (in isoform 4).
{ECO:0000303|Ref.8}.
/FTId=VSP_028029.
VAR_SEQ 39 85 VICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCH
SVPVKS -> G (in isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_015957.
VAR_SEQ 79 208 Missing (in isoform 4).
{ECO:0000303|Ref.8}.
/FTId=VSP_028030.
VAR_SEQ 269 291 NPDGDAKPWCHVLKNRRLTWEYC -> TGRSVSSPATASMR
PCPLSIRSG (in isoform 2).
{ECO:0000303|PubMed:2107528}.
/FTId=VSP_005411.
VAR_SEQ 292 562 Missing (in isoform 2).
{ECO:0000303|PubMed:2107528}.
/FTId=VSP_005412.
VARIANT 34 34 A -> D (in dbSNP:rs8178733).
{ECO:0000269|Ref.12}.
/FTId=VAR_020181.
VARIANT 136 136 R -> S (in dbSNP:rs8178747).
{ECO:0000269|Ref.12}.
/FTId=VAR_038732.
VARIANT 146 146 A -> T (in dbSNP:rs8178748).
{ECO:0000269|Ref.12}.
/FTId=VAR_038733.
VARIANT 164 164 R -> W (in dbSNP:rs2020921).
{ECO:0000269|Ref.12}.
/FTId=VAR_011783.
CONFLICT 93 93 N -> T (in Ref. 2; AAB59510).
{ECO:0000305}.
CONFLICT 159 160 KP -> NA (in Ref. 7; CAA31489).
{ECO:0000305}.
CONFLICT 247 247 K -> N (in Ref. 9; AAO34406).
{ECO:0000305}.
CONFLICT 283 283 N -> S (in Ref. 14; AAH95403).
{ECO:0000305}.
CONFLICT 333 334 RR -> EE (in Ref. 8; AAK11956).
{ECO:0000305}.
CONFLICT 389 389 V -> C (in Ref. 8; AAK11956).
{ECO:0000305}.
STRAND 41 43 {ECO:0000244|PDB:1TPM}.
STRAND 44 46 {ECO:0000244|PDB:1TPG}.
STRAND 48 50 {ECO:0000244|PDB:1TPM}.
STRAND 55 59 {ECO:0000244|PDB:1TPG}.
STRAND 61 64 {ECO:0000244|PDB:1TPG}.
STRAND 66 70 {ECO:0000244|PDB:1TPG}.
STRAND 72 74 {ECO:0000244|PDB:1TPG}.
STRAND 77 81 {ECO:0000244|PDB:1TPM}.
STRAND 83 85 {ECO:0000244|PDB:1TPG}.
STRAND 96 104 {ECO:0000244|PDB:1TPG}.
STRAND 106 109 {ECO:0000244|PDB:1TPG}.
STRAND 115 118 {ECO:0000244|PDB:1TPG}.
STRAND 221 223 {ECO:0000244|PDB:1PK2}.
STRAND 229 233 {ECO:0000244|PDB:1PK2}.
HELIX 242 244 {ECO:0000244|PDB:1PML}.
STRAND 248 250 {ECO:0000244|PDB:1PML}.
STRAND 251 253 {ECO:0000244|PDB:1PK2}.
HELIX 256 259 {ECO:0000244|PDB:1PML}.
STRAND 262 264 {ECO:0000244|PDB:1PML}.
STRAND 277 282 {ECO:0000244|PDB:1PML}.
STRAND 285 291 {ECO:0000244|PDB:1PML}.
STRAND 309 311 {ECO:0000244|PDB:1BDA}.
STRAND 312 316 {ECO:0000244|PDB:1RTF}.
HELIX 319 321 {ECO:0000244|PDB:1RTF}.
STRAND 325 331 {ECO:0000244|PDB:1RTF}.
STRAND 338 346 {ECO:0000244|PDB:1RTF}.
STRAND 348 354 {ECO:0000244|PDB:1RTF}.
HELIX 356 359 {ECO:0000244|PDB:1RTF}.
HELIX 365 367 {ECO:0000244|PDB:1RTF}.
STRAND 368 373 {ECO:0000244|PDB:1RTF}.
STRAND 375 379 {ECO:0000244|PDB:1RTF}.
STRAND 385 394 {ECO:0000244|PDB:1RTF}.
TURN 400 402 {ECO:0000244|PDB:1RTF}.
STRAND 408 412 {ECO:0000244|PDB:1RTF}.
STRAND 415 417 {ECO:0000244|PDB:1RTF}.
STRAND 423 425 {ECO:0000244|PDB:5BRR}.
STRAND 443 449 {ECO:0000244|PDB:1RTF}.
STRAND 451 453 {ECO:0000244|PDB:1BDA}.
STRAND 464 470 {ECO:0000244|PDB:1RTF}.
HELIX 473 475 {ECO:0000244|PDB:1RTF}.
TURN 478 483 {ECO:0000244|PDB:1RTF}.
STRAND 490 494 {ECO:0000244|PDB:1RTF}.
STRAND 499 501 {ECO:0000244|PDB:1A5H}.
STRAND 516 521 {ECO:0000244|PDB:1RTF}.
STRAND 524 533 {ECO:0000244|PDB:1RTF}.
STRAND 535 538 {ECO:0000244|PDB:1RTF}.
STRAND 544 548 {ECO:0000244|PDB:1RTF}.
HELIX 549 552 {ECO:0000244|PDB:1RTF}.
HELIX 553 559 {ECO:0000244|PDB:1RTF}.
SEQUENCE 562 AA; 62917 MW; B7EC9B1A5E3FDC4D CRC64;
MDAMKRGLCC VLLLCGAVFV SPSQEIHARF RRGARSYQVI CRDEKTQMIY QQHQSWLRPV
LRSNRVEYCW CNSGRAQCHS VPVKSCSEPR CFNGGTCQQA LYFSDFVCQC PEGFAGKCCE
IDTRATCYED QGISYRGTWS TAESGAECTN WNSSALAQKP YSGRRPDAIR LGLGNHNYCR
NPDRDSKPWC YVFKAGKYSS EFCSTPACSE GNSDCYFGNG SAYRGTHSLT ESGASCLPWN
SMILIGKVYT AQNPSAQALG LGKHNYCRNP DGDAKPWCHV LKNRRLTWEY CDVPSCSTCG
LRQYSQPQFR IKGGLFADIA SHPWQAAIFA KHRRSPGERF LCGGILISSC WILSAAHCFQ
ERFPPHHLTV ILGRTYRVVP GEEEQKFEVE KYIVHKEFDD DTYDNDIALL QLKSDSSRCA
QESSVVRTVC LPPADLQLPD WTECELSGYG KHEALSPFYS ERLKEAHVRL YPSSRCTSQH
LLNRTVTDNM LCAGDTRSGG PQANLHDACQ GDSGGPLVCL NDGRMTLVGI ISWGLGCGQK
DVPGVYTKVT NYLDWIRDNM RP


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