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   Plasminogen

SourceErinaceus europaeus (western European hedgehog)
Taxonomy Erinaceus europaeus Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Insectivora; Erinaceidae; Erinaceinae; Erinaceus.
KeywordsBlood coagulation; Cleavage on pair of basic residues; Disulfide bond; Fibrinolysis; Glycoprotein; Hydrolase; Kringle; Protease; Repeat; Secreted; Serine protease; Signal; Tissue remodeling; Zymogen.
Details
Function: Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation; in ovulation it weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. It cleaves fibrin, fibronectin, thrombospondin, laminin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4.

Post-translational modification: In the presence of the inhibitor, the activation involves only cleavage after Arg-582, yielding two chains held together by two disulfide bonds. In the absence of the inhibitor, the activation involves additionally the removal of the activation peptide (By similarity).

Similarity: Belongs to the peptidase S1 family. Plasminogen subfamily. Contains 5 kringle domains. Contains 1 PAN domain. Contains 1 peptidase S1 domain.

Subcellular location: Secreted.

Subunit structure: Interacts with CSPG4 (By similarity).

Sequence length: 810 AA.

Sequence
MQRKELVLLFLLFLQPGHGIPLDDYVTTQGASLCSSTKKQLSVGSTEECAVKCEKETSFI
CRSFQYHSKEQQCVIMAENSKSTPVLRMRDVILFEKKMYLSECKVGNGKYYRGTVSKTKT
GLTCQKWSAETPHKPRFSPDENPSEGLDQNYCRNPDNDPKGPWCYTMDPEVRYEYCEIIQ
CEDECMHCSGQNYVGKISRTMSGLECQPWDSQIPHPHGFIPSKFPSKNLKMNYCRNPDGE
PRPWCFTMDRNKRWEYCDIPRCTTPPPPSGPTYQCLMGNGEHYQGNVAVTVSGLTCQRWG
EQSPHRHDRTPENYPCKNLDENYCRNPDGEPAPWCFTTNSSVRWEFCKIPDCVSSASETE
HSDAPVIVPPEQTPVVQECYQGNGQTYRGTSSTTITGKKCQPWTSMRPHRHSKTPENYPD
ADLTMNYCRNPDGDKGPWCYTTDPSVRWEFCNLKKCSGTEMSATNSSPVQVSSASESSEQ
DCIIDNGKGYRGTKATTGAGTPCQAWAAQEPHRHSIFTPETNPRADLQENYCRNPDGDAN
GPWCYTTNPRKLFDYCDIPHCVSPSSADCGKPKVEPKKCPGRVGGCVAHPHSWPWQVSLR
RFGQHFCGGTLISPEWVVTAAHCLEKFSNPAIYKVVLGAHQETRLERDVQIKGVTKMFLE
PYRADIALLKLSSPAIITDKDHPACLPNSNYMVADRSLCYITGWGETKGTYGAGLLKEAQ
LPVIENKVCNRQSFLNGRVRSTELCAGHLAGGVDSCQGDSGGPLVCFEKDRYILQGVTSW
GLGCARLTRPGVYVRVSRYVSWLQDVMRNN
Accession NumberQ29485 
PubMed ID7592597 
CATHG3DSA:2.40.20.10
GO DB0005576, 0005509, 0004252, 0007596, 0042730, 0006508, 0048771
InterPro DBIPR000001, IPR013806, IPR018056, IPR018059, IPR003014, IPR003609, IPR011358, IPR018114, IPR001254, IPR001314, IPR003966, IPR009003
NCBIU33171, AAC48717
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, 228960, 612358, 176895, 173350, 188050, 217090
PfamPF00051, PF00024, PF00089
PROSITE DBPS00021, PS50070, PS50948, PS50240, PS00134, PS00135
SMART DBSM00130, SM00473, SM00020



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