Result Untitled Document Tissue-type plasminogen activatorSourceRattus norvegicus (Norway rat) Taxonomy Rattus norvegicus Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.KeywordsCleavage on pair of basic residues; Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Kringle; Plasminogen activation; Protease; Repeat; Secreted; Serine protease; Signal; Zymogen.DetailsFunction: 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. SequenceMKGELLCVLLLCGVAFTLPDQGIHRRFRRGARSYRATCRDEQTQTTYQQHQSWLRPMLRGNRVEYCRCNSGLAQCHSVPVRSCSEPRCFNGGTCQQALYFSDFVCQCPDGFVGKRCDIDTRATCFEGQGITYRGTWSTAENGAECINWNSSALSQKPYSARRPNAIKLGLGNHNYCRNPDRDVKPWCYVFKAGKYTTEFCSTPACPKGPTEDCYVGKGVTYRGTHSFTTSKASCLPWNSMILIGKTYTAWRANSQALGLGRHNYCRNPDGDAKPWCHVMKDRKLTWEYCDMSPCSTCGLRQYKQPQFRIKGGLFTDITSHPWQAAIFVKNKRSPGERFLCGGVLISSCWVLSAAHCFVERFPPHHLKVVLGRTYRVVPGEEEQTFEIEKYIVHKEFDDDTYDNDIALLQLRSDSSQCAQESSSVGTACLPDPDVQLPDWTECELSGYGKHEASSPFFSDRLKEAHVRLYPSSRCTSQHLFNKTITSNMLCAGDTRTGGNQDVHDACQGDSGGPLVCMIDKRMTLLGIISWGLGCGQKDVPGIYTKVTNYLNWIQDNMKQAccession NumberP19637 PubMed ID3148445, 2105315, 15489334 CTD DB25692eggNOG DBroNOG14617Ensembl DBENSRNOT00000025763CATHG3DSA:2.10.70.10, G3DSA:2.40.20.10GeneID DB25692GermOnline DBENSRNOG00000019018GO DB0005615, 0045202, 0004252, 0048514, 0048167, 0051591, 0051384, 0043434, 0035249InterPro DBIPR016060, IPR006209, IPR006210, IPR013032, IPR000742, IPR000083, IPR000001, IPR013806, IPR018056, IPR018059, IPR018114, IPR001254, IPR001314, IPR009003IPI DBIPI00332012KEGGrno:25692NCBIM23697, AAA41812, M31197, AAA42261, M31185, M31186, M31187, M31188, M31189, M31190, M31191, M31192, M31193, M31194, M31195, M31196, BC061565, AAH61565, NP_037283.2OMATCGLRQYOMIM105200, 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, 217090OrthoDBEOG9TQPVKPfamPF00008, PF00039, PF00051, PF00089PROSITE DBPS00022, PS01186, PS50026, PS01253, PS51091, PS00021, PS50070, PS50240, PS00134, PS00135SMART DBSM00181, SM00058, SM00130, SM00020UCSCNM_013151UniGeneRn.107102
Result
Tissue-type plasminogen activator
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.
MKGELLCVLLLCGVAFTLPDQGIHRRFRRGARSYRATCRDEQTQTTYQQHQSWLRPMLRGNRVEYCRCNSGLAQCHSVPVRSCSEPRCFNGGTCQQALYFSDFVCQCPDGFVGKRCDIDTRATCFEGQGITYRGTWSTAENGAECINWNSSALSQKPYSARRPNAIKLGLGNHNYCRNPDRDVKPWCYVFKAGKYTTEFCSTPACPKGPTEDCYVGKGVTYRGTHSFTTSKASCLPWNSMILIGKTYTAWRANSQALGLGRHNYCRNPDGDAKPWCHVMKDRKLTWEYCDMSPCSTCGLRQYKQPQFRIKGGLFTDITSHPWQAAIFVKNKRSPGERFLCGGVLISSCWVLSAAHCFVERFPPHHLKVVLGRTYRVVPGEEEQTFEIEKYIVHKEFDDDTYDNDIALLQLRSDSSQCAQESSSVGTACLPDPDVQLPDWTECELSGYGKHEASSPFFSDRLKEAHVRLYPSSRCTSQHLFNKTITSNMLCAGDTRTGGNQDVHDACQGDSGGPLVCMIDKRMTLLGIISWGLGCGQKDVPGIYTKVTNYLNWIQDNMKQ
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