Result

Untitled Document

  Tissue-type plasminogen activator

SourceMus musculus (house mouse)
Taxonomy Mus musculus Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
KeywordsCleavage on pair of basic residues; Direct protein sequencing; Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Kringle; Plasminogen activation; Protease; Repeat; Secreted; Serine protease; Signal; Zymogen.
Details
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.

Post-translational modification: 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. Contains 1 EGF-like domain. Contains 1 fibronectin type-I domain. Contains 2 kringle domains. Contains 1 peptidase S1 domain.

Subcellular location: Secreted, extracellular space.

Subunit structure: 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 (By similarity).

Sequence length: 559 AA.

Sequence
MKRELLCVLLLCGLAFPLPDQGIHGRFRRGARSYRATCRDEPTQTTYQQHQSWLRPMLRS
SRVEYCRCNSGLVQCHSVPVRSCSEPRCFNGGTCQQALYFSDFVCQCPDGFVGKRCDIDT
RATCFEEQGITYRGTWSTAESGAECINWNSSVLSLKPYNARRPNAIKLGLGNHNYCRNPD
RDLKPWCYVFKAGKYTTEFCSTPACPKGKSEDCYVGKGVTYRGTHSLTTSQASCLPWNSI
VLMGKSYTAWRTNSQALGLGRHNYCRNPDGDARPWCHVMKDRKLTWEYCDMSPCSTCGLR
QYKRPQFRIKGGLYTDITSHPWQAAIFVKNKRSPGERFLCGGVLISSCWVLSAAHCFLER
FPPNHLKVVLGRTYRVVPGEEEQTFEIEKYIVHEEFDDDTYDNDIALLQLRSQSKQCAQE
SSSVGTACLPDPNLQLPDWTECELSGYGKHEASSPFFSDRLKEAHVRLYPSSRCTSQHLF
NKTVTNNMLCAGDTRSGGNQDLHDACQGDSGGPLVCMINKQMTLTGIISWGLGCGQKDVP
GVYTKVTNYLDWIHDNMKQ
Accession NumberP11214 
PubMed ID2826484, 16141072, 15489334, 7523120 
CEX DBMM_PLAT
CTD DB18791
eggNOG DBroNOG14617
Ensembl DBENSMUST00000033941
CATHG3DSA:2.10.70.10, G3DSA:2.40.20.10
GeneID DB18791
GermOnline DBENSMUSG00000031538
GO DB0045177, 0005615, 0030141, 0004252, 0048008, 0006508, 0001666, 0014909
HOGENOM DBHBG755338
InterPro DBIPR016060, IPR006209, IPR006210, IPR013032, IPR000742, IPR000083, IPR000001, IPR013806, IPR018056, IPR018059, IPR018114, IPR001254, IPR001314, IPR009003
IPI DBIPI00319513
KEGGmmu:18791
NCBIJ03520, AAA40470, AK135857, BAE22698, AK135965, BAE22749, BC011256, AAH11256, BC057967, AAH57967, BC061508, AAH61508, NP_032898.2
OMATCGLRQY
OMIM105200, 134820, 202400, 134830, 202400, 134850, 202400, 176930, 601367, 134390, 188055, 227400, 600880, 601367, 612309, 227500, 134500, 306700, 300746, 306900, 227600, 176860, 188050, 612283, 612304, 176880, 612336, 264900, 612416, 234000, 610618, 610619, 229000, 612423, 107300, 188050, 134570, 134580, 193400, 277480
OrthoDBEOG9TQPVK
PfamPF00008, PF00039, PF00051, PF00089
PROSITE DBPS00022, PS01186, PS50026, PS01253, PS51091, PS00021, PS50070, PS50240, PS00134, PS00135
SMART DBSM00181, SM00058, SM00130, SM00020
UniGeneMm.154660, Mm.477132



Useful Links

©Biomedical Informatics Centre, NIRRH, Mumbai