Result Untitled Document PlasminogenSourceHomo sapiens (human) Taxonomy Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.Keywords3D-structure; Blood coagulation; Cleavage on pair of basic residues; Complete proteome; Direct protein sequencing; Disease mutation; Disulfide bond; Fibrinolysis; Glycoprotein; Hydrolase; Kringle; Phosphoprotein; Polymorphism; Protease; Repeat; Secreted; Serine protease; Signal; Thrombophilia; 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. Post-translational modification: N-linked glycan contains N-acetyllactosamine and sialic acid. O-linked glycans consist of Gal-GalNAc disaccharide modified with up to 2 sialic acid residues (microheterogeneity). In the presence of the inhibitor, the activation involves only cleavage after Arg-580, 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. 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 AMOT and CSPG4 (also true for angiostatin). Tissue specificity: Present in plasma and many other extracellular fluids. It is synthesized in the liver. Disease: Defects in PLG are a cause of thrombophilia Defects in PLG may be associated with ligneous conjunctivitis Interaction: Q6V4K9:- (xeno); NbExp=1; IntAct=EBI-999394, EBI-984399; Q6V4L1:- (xeno); NbExp=2; IntAct=EBI-999394, EBI-984250; Q6V4L4:- (xeno); NbExp=2; IntAct=EBI-999394, EBI-984286; Q6V4L5:- (xeno); NbExp=2; IntAct=EBI-999394, EBI-984118; Q6V4L9:- (xeno); NbExp=2; IntAct=EBI-999394, EBI-984197; P00779:skc (xeno); NbExp=1; IntAct=EBI-999394, EBI-1035089. Sequence length: 810 AA. SequenceMEHKEVVLLLLLFLKSGQGEPLDDYVNTQGASLFSVTKKQLGAGSIEECAAKCEEDEEFTCRAFQYHSKEQQCVIMAENRKSSIIIRMRDVVLFEKKVYLSECKTGNGKNYRGTMSKTKNGITCQKWSSTSPHRPRFSPATHPSEGLEENYCRNPDNDPQGPWCYTTDPEKRYDYCDILECEEECMHCSGENYDGKISKTMSGLECQAWDSQSPHAHGYIPSKFPNKNLKKNYCRNPDRELRPWCFTTDPNKRWELCDIPRCTTPPPSSGPTYQCLKGTGENYRGNVAVTVSGHTCQHWSAQTPHTHNRTPENFPCKNLDENYCRNPDGKRAPWCHTTNSQVRWEYCKIPSCDSSPVSTEQLAPTAPPELTPVVQDCYHGDGQSYRGTSSTTTTGKKCQSWSSMTPHRHQKTPENYPNAGLTMNYCRNPDADKGPWCFTTDPSVRWEYCNLKKCSGTEASVVAPPPVVLLPDVETPSEEDCMFGNGKGYRGKRATTVTGTPCQDWAAQEPHRHSIFTPETNPRAGLEKNYCRNPDGDVGGPWCYTTNPRKLYDYCDVPQCAAPSFDCGKPQVEPKKCPGRVVGGCVAHPHSWPWQVSLRTRFGMHFCGGTLISPEWVLTAAHCLEKSPRPSSYKVILGAHQEVNLEPHVQEIEVSRLFLEPTRKDIALLKLSSPAVITDKVIPACLPSPNYVVADRTECFITGWGETQGTFGAGLLKEAQLPVIENKVCNRYEFLNGRVQSTELCAGHLAGGTDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVTWIEGVMRNNAccession NumberP00747 PubMed ID2318848, 3030813, 14574404, 15489334, 122932, 6148961, 126863, 142009, 4694729, 4240117, 6919539, 6094526, 9201958, 3356193, 9054441, 7525077, 9102221, 9548733, 10889192, 16043488, 18780401, 1657148, 1657149, 8054447, 8611560, 15299951, 9783753, 9521645, 10656799, 11350170, 12054798, 12456874, 15211511, 2157850, 8181475, 8181476, 8652577, 9305949, 1986355, 8392398, 6216475, 6238949, 1427790, 9242524, 9858247, 10233898 CEX DBHS_PLGCTD DB5340eggNOG DBprNOG15519Ensembl DBENST00000308192CATHG3DSA:2.40.20.10Genecard DBGC06P161093GeneID DB5340GermOnline DBENSG00000122194GO DB0005615, 0034185, 0005509, 0004252, 0007596, 0042730, 0006917, 0016525, 0043537, 0008285, 0051918, 0051919, 0048771HGNC DB9071HOGENOM DBHBG755338HPA DBCAB000668, CAB016678, HPA021602InterPro DBIPR000001, IPR013806, IPR018056, IPR018059, IPR003014, IPR003609, IPR011358, IPR018114, IPR001254, IPR001314, IPR003966, IPR009003H-InvDBHIX0032909IPI DBIPI00019580KEGGhsa:5340NCBIM34276, AAA60113, M33272, M33274, M33275, M33278, M33279, M33280, M33282, M33283, M33284, M33285, M33286, M33287, M33288, M33289, M33290, M34272, M34273, M34275, X05199, CAA28831, M74220, AAA36451, AY192161, AAN85555, AL109933.25, CAI22908, BC060513, AAH60513, K02922, AAA60124, NP_000292OMAENKVCNROMIM105200, 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, 217090Orphanet DB722, 97231OrthoDBEOG9C2KVWPDB1B2I_A, 1BML_A, 1BML_B, 1BUI_A, 1BUI_B, 1CEA_A, 1CEA_B, 1CEB_A, 1CEB_B, 1DDJ_A, 1DDJ_B, 1DDJ_C, 1DDJ_D, 1HPJ_A, 1HPK_A, 1I5K_A, 1I5K_B, 1KI0_A, 1KRN_A, 1L4D_A, 1L4Z_A, 1PK4_A, 1PKR_A, 1PMK_A, 1PMK_B, 1QRZ_A, 1QRZ_B, 1QRZ_C, 1QRZ_D, 1RJX_B, 2DOH_X, 2DOI_A, 2DOI_X, 2KNF_A, 2PK4_A, 5HPG_A, 5HPG_BPfamPF00051, PF00024, PF00089PharmaGKBPA33405PROSITE DBPS00021, PS50070, PS50948, PS50240, PS00134, PS00135SMART DBSM00130, SM00473, SM00020UCSCuc003qtm.2UniGeneHs.143436
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. Post-translational modification: N-linked glycan contains N-acetyllactosamine and sialic acid. O-linked glycans consist of Gal-GalNAc disaccharide modified with up to 2 sialic acid residues (microheterogeneity). In the presence of the inhibitor, the activation involves only cleavage after Arg-580, 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. 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 AMOT and CSPG4 (also true for angiostatin). Tissue specificity: Present in plasma and many other extracellular fluids. It is synthesized in the liver. Disease: Defects in PLG are a cause of thrombophilia Defects in PLG may be associated with ligneous conjunctivitis Interaction: Q6V4K9:- (xeno); NbExp=1; IntAct=EBI-999394, EBI-984399; Q6V4L1:- (xeno); NbExp=2; IntAct=EBI-999394, EBI-984250; Q6V4L4:- (xeno); NbExp=2; IntAct=EBI-999394, EBI-984286; Q6V4L5:- (xeno); NbExp=2; IntAct=EBI-999394, EBI-984118; Q6V4L9:- (xeno); NbExp=2; IntAct=EBI-999394, EBI-984197; P00779:skc (xeno); NbExp=1; IntAct=EBI-999394, EBI-1035089. Sequence length: 810 AA.
MEHKEVVLLLLLFLKSGQGEPLDDYVNTQGASLFSVTKKQLGAGSIEECAAKCEEDEEFTCRAFQYHSKEQQCVIMAENRKSSIIIRMRDVVLFEKKVYLSECKTGNGKNYRGTMSKTKNGITCQKWSSTSPHRPRFSPATHPSEGLEENYCRNPDNDPQGPWCYTTDPEKRYDYCDILECEEECMHCSGENYDGKISKTMSGLECQAWDSQSPHAHGYIPSKFPNKNLKKNYCRNPDRELRPWCFTTDPNKRWELCDIPRCTTPPPSSGPTYQCLKGTGENYRGNVAVTVSGHTCQHWSAQTPHTHNRTPENFPCKNLDENYCRNPDGKRAPWCHTTNSQVRWEYCKIPSCDSSPVSTEQLAPTAPPELTPVVQDCYHGDGQSYRGTSSTTTTGKKCQSWSSMTPHRHQKTPENYPNAGLTMNYCRNPDADKGPWCFTTDPSVRWEYCNLKKCSGTEASVVAPPPVVLLPDVETPSEEDCMFGNGKGYRGKRATTVTGTPCQDWAAQEPHRHSIFTPETNPRAGLEKNYCRNPDGDVGGPWCYTTNPRKLYDYCDVPQCAAPSFDCGKPQVEPKKCPGRVVGGCVAHPHSWPWQVSLRTRFGMHFCGGTLISPEWVLTAAHCLEKSPRPSSYKVILGAHQEVNLEPHVQEIEVSRLFLEPTRKDIALLKLSSPAVITDKVIPACLPSPNYVVADRTECFITGWGETQGTFGAGLLKEAQLPVIENKVCNRYEFLNGRVQSTELCAGHLAGGTDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVTWIEGVMRNN
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