Result Untitled Document PlasminogenSourceRattus norvegicus (Norway rat) Taxonomy Rattus norvegicus Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.KeywordsBlood coagulation; Cleavage on pair of basic residues; Disulfide bond; Fibrinolysis; Hydrolase; Kringle; Protease; Repeat; Secreted; Serine protease; Signal; Tissue remodeling; Zymogen.DetailsFunction: 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. Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo (By similarity). Post-translational modification: In the presence of the inhibitor, the activation involves only cleavage after Arg-581, 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 and AMOT (By similarity). Sequence length: 812 AA. SequenceMDHKEIILLFLLFLKPGQGDSLDGYVSTQGASLHSLTKKQLAAGSIADCLAKCEGETDFICRSFQYHSKEQQCVIMAENSKTSSIIRMRDVILFEKRVYLSECKTGIGKGYRGTMSKTKTGVTCQKWSDTSPHVPKYSPSTHPSEGLEENYCRNPDNDEQGPWCYTTDPDQRYEYCNIPECEEECMYCSGEKYEGKISKTMSGLDCQSWDSQSPHAHGYIPAKFPSKNLKMNYCRNPDGEPRPWCFTTDPNKRWEYCDIPRCTTPPPPPGPTYQCLKGRGENYRGTVSVTASGKTCQRWSEQTPHRHNRTPENFPCKNLEENYCRNPDGETAPWCYTTDSQLRWEYCEIPSCGSSVSPDQSDSSVLPEQTPVVQECYQGNGKSYRGTSSTTNTGKKCQSWVSMTPHSHSKTPANFPDAGLEMNYCRNPDNDQRGPWCFTTDPSVRWEYCNLKRCSETGGGVAESAIVPQVPSAPGTSETDCMYGNGKEYRGKTAVTAAGTPCQEWAAQEPHSHRIFTPQTNPRAGLEKNYCRNPDGDVNGPWCYTMNPRKLYDYCNIPLCASLSSFECGKPQVEPKKCPGRVVGGCVANPHSWPWQISLRTRFSGQHFCGGTLISPEWVLTAAHCLEKSSRPEFYKVILGAHEERILGSDVQQIAVTKLVLEPNDADIALLKLSRPATITDNVIPACLPSPNYVVADRTLCYITGWGETKGTPGAGRLKEAQLPVIENKVCNRAEYLNNRVKSTELCAGHLAGGIDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRYVNWIEREMRNDAccession NumberQ01177 PubMed ID15489334, 1645711 CTD DB85253eggNOG DBroNOG14223Ensembl DBENSRNOT00000023368GeneID DB85253GermOnline DBENSRNOG00000017223GO DB0005792, 0005509, 0004252, 0007596, 0042730, 0051603, 0048771InterPro DBIPR000001, IPR013806, IPR018056, IPR018059, IPR003014, IPR003609, IPR011358, IPR018114, IPR001254, IPR001314, IPR003966, IPR009003IPI DBIPI00206780KEGGrno:85253NCBIAJ242649, CAB46014, BC091135, AAH91135, M62832, AAA41884, NP_445943NMPDR fig|10116.3.peg.463OMAENKVCNROMIM105200, 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, 217090OrthoDBEOG9C2KVWPfamPF00051, PF00024, PF00089PROSITE DBPS00021, PS50070, PS50948, PS50240, PS00134, PS00135SMART DBSM00130, SM00473, SM00020UCSCBC091135UniGeneRn.20178
Result
Plasminogen
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. Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo (By similarity). Post-translational modification: In the presence of the inhibitor, the activation involves only cleavage after Arg-581, 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 and AMOT (By similarity). Sequence length: 812 AA.
MDHKEIILLFLLFLKPGQGDSLDGYVSTQGASLHSLTKKQLAAGSIADCLAKCEGETDFICRSFQYHSKEQQCVIMAENSKTSSIIRMRDVILFEKRVYLSECKTGIGKGYRGTMSKTKTGVTCQKWSDTSPHVPKYSPSTHPSEGLEENYCRNPDNDEQGPWCYTTDPDQRYEYCNIPECEEECMYCSGEKYEGKISKTMSGLDCQSWDSQSPHAHGYIPAKFPSKNLKMNYCRNPDGEPRPWCFTTDPNKRWEYCDIPRCTTPPPPPGPTYQCLKGRGENYRGTVSVTASGKTCQRWSEQTPHRHNRTPENFPCKNLEENYCRNPDGETAPWCYTTDSQLRWEYCEIPSCGSSVSPDQSDSSVLPEQTPVVQECYQGNGKSYRGTSSTTNTGKKCQSWVSMTPHSHSKTPANFPDAGLEMNYCRNPDNDQRGPWCFTTDPSVRWEYCNLKRCSETGGGVAESAIVPQVPSAPGTSETDCMYGNGKEYRGKTAVTAAGTPCQEWAAQEPHSHRIFTPQTNPRAGLEKNYCRNPDGDVNGPWCYTMNPRKLYDYCNIPLCASLSSFECGKPQVEPKKCPGRVVGGCVANPHSWPWQISLRTRFSGQHFCGGTLISPEWVLTAAHCLEKSSRPEFYKVILGAHEERILGSDVQQIAVTKLVLEPNDADIALLKLSRPATITDNVIPACLPSPNYVVADRTLCYITGWGETKGTPGAGRLKEAQLPVIENKVCNRAEYLNNRVKSTELCAGHLAGGIDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRYVNWIEREMRND
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