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

 TPA_MOUSE               Reviewed;         559 AA.
P11214; Q6P7U0; Q91VP2;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
02-OCT-2007, sequence version 3.
07-JUN-2017, entry version 174.
RecName: Full=Tissue-type plasminogen activator;
Short=t-PA;
Short=t-plasminogen activator;
Short=tPA;
EC=3.4.21.68;
Contains:
RecName: Full=Tissue-type plasminogen activator chain A;
Contains:
RecName: Full=Tissue-type plasminogen activator chain B;
Flags: Precursor;
Name=Plat;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2826484;
Rickles R.J., Darrow A.L., Strickland S.;
"Molecular cloning of complementary DNA to mouse tissue plasminogen
activator mRNA and its expression during F9 teratocarcinoma cell
differentiation.";
J. Biol. Chem. 263:1563-1569(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N, and NMRI; TISSUE=Mammary gland, and Mammary tumor;
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).
[4]
PROTEIN SEQUENCE OF 33-40 AND 309-316.
PubMed=7523120; DOI=10.1111/j.1432-1033.1994.00863.x;
Lijnen H.R., van Hoef B., Beelen V., Collen D.;
"Characterization of the murine plasma fibrinolytic system.";
Eur. J. Biochem. 224:863-871(1994).
-!- 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.
-!- CATALYTIC ACTIVITY: Specific cleavage of Arg-|-Val bond in
plasminogen to form plasmin.
-!- ENZYME REGULATION: Inhibited by SERPINA5. {ECO:0000250}.
-!- 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 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. Binds LRP1B;
binding is followed by internalization and degradation. Forms
heterodimer with SERPINA5 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space.
-!- DOMAIN: Both FN1 and one of the kringle domains are required for
binding to fibrin. {ECO:0000250}.
-!- DOMAIN: Both FN1 and EGF-like domains are important for binding to
LRP1. {ECO:0000250}.
-!- DOMAIN: The FN1 domain mediates binding to annexin A2.
{ECO:0000250}.
-!- DOMAIN: The second kringle domain is implicated in binding to
cytokeratin-8 and to the endothelial cell surface binding site.
{ECO:0000250}.
-!- PTM: The single chain, almost fully active enzyme, can be further
processed into a two-chain fully active form by a cleavage after
Arg-308 catalyzed by plasmin, tissue kallikrein or factor Xa.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
-----------------------------------------------------------------------
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EMBL; J03520; AAA40470.1; -; mRNA.
EMBL; AK135857; BAE22698.1; -; mRNA.
EMBL; AK135965; BAE22749.1; -; mRNA.
EMBL; BC011256; AAH11256.1; -; mRNA.
EMBL; BC057967; AAH57967.1; -; mRNA.
EMBL; BC061508; AAH61508.1; -; mRNA.
CCDS; CCDS22183.1; -.
PIR; A29941; A29941.
RefSeq; NP_032898.2; NM_008872.3.
UniGene; Mm.154660; -.
ProteinModelPortal; P11214; -.
SMR; P11214; -.
IntAct; P11214; 2.
MINT; MINT-8178492; -.
STRING; 10090.ENSMUSP00000033941; -.
ChEMBL; CHEMBL3259492; -.
MEROPS; S01.232; -.
PhosphoSitePlus; P11214; -.
MaxQB; P11214; -.
PaxDb; P11214; -.
PeptideAtlas; P11214; -.
PRIDE; P11214; -.
Ensembl; ENSMUST00000033941; ENSMUSP00000033941; ENSMUSG00000031538.
GeneID; 18791; -.
KEGG; mmu:18791; -.
UCSC; uc009ldx.2; mouse.
CTD; 5327; -.
MGI; MGI:97610; Plat.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000119133; -.
HOGENOM; HOG000237314; -.
HOVERGEN; HBG008633; -.
InParanoid; P11214; -.
KO; K01343; -.
OMA; AHVRLYP; -.
OrthoDB; EOG091G0AH5; -.
PhylomeDB; P11214; -.
TreeFam; TF329901; -.
BRENDA; 3.4.21.68; 3474.
Reactome; R-MMU-186797; Signaling by PDGF.
Reactome; R-MMU-75205; Dissolution of Fibrin Clot.
PRO; PR:P11214; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000031538; -.
CleanEx; MM_PLAT; -.
Genevisible; P11214; MM.
GO; GO:0045177; C:apical part of cell; IDA:MGI.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0030141; C:secretory granule; IDA:MGI.
GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
GO; GO:0005102; F:receptor binding; ISO:MGI.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:MGI.
GO; GO:0045861; P:negative regulation of proteolysis; ISO:MGI.
GO; GO:0031639; P:plasminogen activation; ISO:MGI.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IDA:MGI.
GO; GO:0006508; P:proteolysis; IDA:MGI.
GO; GO:0001666; P:response to hypoxia; IMP:MGI.
GO; GO:0014909; P:smooth muscle cell migration; IMP:MGI.
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; PTHR24256:SF341; PTHR24256:SF341; 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; SM00181; EGF; 1.
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;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disulfide bond; EGF-like domain;
Glycoprotein; Hydrolase; Kringle; Plasminogen activation; Protease;
Reference proteome; Repeat; Secreted; Serine protease; Signal;
Zymogen.
SIGNAL 1 17 {ECO:0000255}.
PROPEP 18 29 {ECO:0000250}.
/FTId=PRO_0000028353.
PROPEP 30 32 Removed by plasmin.
{ECO:0000269|PubMed:7523120}.
/FTId=PRO_0000285906.
CHAIN 33 559 Tissue-type plasminogen activator.
/FTId=PRO_0000028354.
CHAIN 33 308 Tissue-type plasminogen activator chain
A.
/FTId=PRO_0000028355.
CHAIN 309 559 Tissue-type plasminogen activator chain
B.
/FTId=PRO_0000028356.
DOMAIN 36 78 Fibronectin type-I. {ECO:0000255|PROSITE-
ProRule:PRU00478}.
DOMAIN 79 117 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 124 205 Kringle 1. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 213 294 Kringle 2. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 309 558 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
REGION 39 49 Important for binding to annexin A2.
{ECO:0000250}.
ACT_SITE 355 355 Charge relay system.
ACT_SITE 404 404 Charge relay system.
ACT_SITE 510 510 Charge relay system.
SITE 99 99 Important for binding to LRP1.
{ECO:0000250}.
SITE 462 462 Important for single-chain activity.
{ECO:0000250}.
SITE 509 509 Important for single-chain activity.
{ECO:0000250}.
CARBOHYD 149 149 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 481 481 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 38 68 {ECO:0000250}.
DISULFID 66 75 {ECO:0000250}.
DISULFID 83 94 {ECO:0000250}.
DISULFID 88 105 {ECO:0000250}.
DISULFID 107 116 {ECO:0000250}.
DISULFID 124 205 {ECO:0000250}.
DISULFID 145 187 {ECO:0000250}.
DISULFID 176 200 {ECO:0000250}.
DISULFID 213 294 {ECO:0000250}.
DISULFID 234 276 {ECO:0000250}.
DISULFID 265 289 {ECO:0000250}.
DISULFID 297 428 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}.
DISULFID 340 356 {ECO:0000250}.
DISULFID 348 417 {ECO:0000250}.
DISULFID 442 516 {ECO:0000250}.
DISULFID 474 490 {ECO:0000250}.
DISULFID 506 534 {ECO:0000250}.
CONFLICT 260 260 G -> A (in Ref. 1; AAA40470).
{ECO:0000305}.
CONFLICT 325 325 A -> P (in Ref. 3; AAH11256).
{ECO:0000305}.
SEQUENCE 559 AA; 63097 MW; 0A158A5A273CFAA0 CRC64;
MKRELLCVLL LCGLAFPLPD QGIHGRFRRG ARSYRATCRD EPTQTTYQQH QSWLRPMLRS
SRVEYCRCNS GLVQCHSVPV RSCSEPRCFN GGTCQQALYF SDFVCQCPDG FVGKRCDIDT
RATCFEEQGI TYRGTWSTAE SGAECINWNS SVLSLKPYNA RRPNAIKLGL GNHNYCRNPD
RDLKPWCYVF KAGKYTTEFC STPACPKGKS EDCYVGKGVT YRGTHSLTTS QASCLPWNSI
VLMGKSYTAW RTNSQALGLG RHNYCRNPDG DARPWCHVMK DRKLTWEYCD MSPCSTCGLR
QYKRPQFRIK GGLYTDITSH PWQAAIFVKN KRSPGERFLC GGVLISSCWV LSAAHCFLER
FPPNHLKVVL GRTYRVVPGE EEQTFEIEKY IVHEEFDDDT YDNDIALLQL RSQSKQCAQE
SSSVGTACLP DPNLQLPDWT ECELSGYGKH EASSPFFSDR LKEAHVRLYP SSRCTSQHLF
NKTVTNNMLC AGDTRSGGNQ DLHDACQGDS GGPLVCMINK QMTLTGIISW GLGCGQKDVP
GVYTKVTNYL DWIHDNMKQ


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