ID E7ESF4_HUMAN Unreviewed; 499 AA. AC E7ESF4; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 16-JAN-2019, entry version 68. DE RecName: Full=Plasminogen activator {ECO:0000256|PIRNR:PIRNR001145}; DE EC=3.4.21.68 {ECO:0000256|PIRNR:PIRNR001145}; GN Name=PLAT {ECO:0000313|Ensembl:ENSP00000428886}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000428886, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000428886, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T., RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Glockner G., RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., RA O'Leary S.B., O'Neill K., Parker S.C., Polley A., Raymond C.K., RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., RA Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [2] {ECO:0000313|Ensembl:ENSP00000428886} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=Specific cleavage of Arg-|-Val bond in plasminogen to CC form plasmin.; EC=3.4.21.68; CC Evidence={ECO:0000256|PIRNR:PIRNR001145}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|PIRNR:PIRNR001145, CC ECO:0000256|SAAS:SAAS00748227}. CC -!- SIMILARITY: Belongs to the peptidase S1 family. CC {ECO:0000256|PIRNR:PIRNR001145, ECO:0000256|SAAS:SAAS00559343}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AC083973; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC103724; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; E7ESF4; -. DR jPOST; E7ESF4; -. DR MaxQB; E7ESF4; -. DR PeptideAtlas; E7ESF4; -. DR PRIDE; E7ESF4; -. DR Ensembl; ENST00000519510; ENSP00000428886; ENSG00000104368. DR UCSC; uc064mjr.1; human. DR EuPathDB; HostDB:ENSG00000104368.17; -. DR HGNC; HGNC:9051; PLAT. DR OpenTargets; ENSG00000104368; -. DR eggNOG; KOG3627; Eukaryota. DR eggNOG; COG5640; LUCA. DR GeneTree; ENSGT00940000158930; -. DR ChiTaRS; PLAT; human. DR Proteomes; UP000005640; Chromosome 8. DR Bgee; ENSG00000104368; Expressed in 217 organ(s), highest expression level in metanephric glomerulus. DR ExpressionAtlas; E7ESF4; baseline and differential. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0031639; P:plasminogen activation; IEA:InterPro. DR CDD; cd00061; FN1; 1. DR CDD; cd00108; KR; 1. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 2.40.20.10; -; 1. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR000083; Fibronectin_type1. DR InterPro; IPR000001; Kringle. DR InterPro; IPR013806; Kringle-like. DR InterPro; IPR018056; Kringle_CS. DR InterPro; IPR038178; Kringle_sf. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR026280; Tissue_plasm_act. DR InterPro; IPR034811; tPA. DR InterPro; IPR001254; Trypsin_dom. DR InterPro; IPR018114; TRYPSIN_HIS. DR InterPro; IPR033116; TRYPSIN_SER. DR PANTHER; PTHR44617; PTHR44617; 2. DR Pfam; PF00008; EGF; 1. DR Pfam; PF00039; fn1; 1. DR Pfam; PF00051; Kringle; 1. DR Pfam; PF00089; Trypsin; 1. DR PIRSF; PIRSF001145; Tissue_plasm_act; 2. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00058; FN1; 1. DR SMART; SM00130; KR; 1. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; SSF50494; 1. DR SUPFAM; SSF57440; SSF57440; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. DR PROSITE; PS01253; FN1_1; 1. DR PROSITE; PS51091; FN1_2; 1. DR PROSITE; PS00021; KRINGLE_1; 1. DR PROSITE; PS50070; KRINGLE_2; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|PIRSR:PIRSR001145-3, ECO:0000256|PROSITE- KW ProRule:PRU00076, ECO:0000256|SAAS:SAAS00037407}; KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076, KW ECO:0000256|SAAS:SAAS00729996}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR001145, KW ECO:0000256|RuleBase:RU363034, ECO:0000256|SAAS:SAAS00745848}; KW Kringle {ECO:0000256|PROSITE-ProRule:PRU00121, KW ECO:0000256|SAAS:SAAS00045973}; KW Plasminogen activation {ECO:0000256|PIRNR:PIRNR001145}; KW Protease {ECO:0000256|PIRNR:PIRNR001145, KW ECO:0000256|RuleBase:RU363034, ECO:0000256|SAAS:SAAS00745848}; KW Proteomics identification {ECO:0000213|MaxQB:E7ESF4, KW ECO:0000213|PeptideAtlas:E7ESF4}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Secreted {ECO:0000256|PIRNR:PIRNR001145, KW ECO:0000256|SAAS:SAAS00749664}; KW Serine protease {ECO:0000256|PIRNR:PIRNR001145, KW ECO:0000256|RuleBase:RU363034, ECO:0000256|SAAS:SAAS00745848}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 499 Plasminogen activator. FT {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003217513. FT DOMAIN 39 81 Fibronectin type-I. FT {ECO:0000259|PROSITE:PS51091}. FT DOMAIN 82 120 EGF-like. {ECO:0000259|PROSITE:PS50026}. FT DOMAIN 151 233 Kringle. {ECO:0000259|PROSITE:PS50070}. FT DOMAIN 248 498 Peptidase S1. FT {ECO:0000259|PROSITE:PS50240}. FT REGION 42 52 Important for binding to annexin A2. FT {ECO:0000256|PIRSR:PIRSR001145-2}. FT ACT_SITE 294 294 Charge relay system. FT {ECO:0000256|PIRSR:PIRSR001145-1}. FT ACT_SITE 343 343 Charge relay system. FT {ECO:0000256|PIRSR:PIRSR001145-1}. FT ACT_SITE 450 450 Charge relay system. FT {ECO:0000256|PIRSR:PIRSR001145-1}. FT SITE 102 102 Important for binding to LRP1. FT {ECO:0000256|PIRSR:PIRSR001145-2}. FT SITE 401 401 Important for single-chain activity. FT {ECO:0000256|PIRSR:PIRSR001145-2}. FT SITE 449 449 Important for single-chain activity. FT {ECO:0000256|PIRSR:PIRSR001145-2}. FT DISULFID 41 71 {ECO:0000256|PIRSR:PIRSR001145-3}. FT DISULFID 69 78 {ECO:0000256|PIRSR:PIRSR001145-3}. FT DISULFID 86 97 {ECO:0000256|PIRSR:PIRSR001145-3}. FT DISULFID 91 108 {ECO:0000256|PIRSR:PIRSR001145-3, FT ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 110 119 {ECO:0000256|PIRSR:PIRSR001145-3, FT ECO:0000256|PROSITE-ProRule:PRU00076}. FT DISULFID 152 233 {ECO:0000256|PIRSR:PIRSR001145-3}. FT DISULFID 173 215 {ECO:0000256|PIRSR:PIRSR001145-3}. FT DISULFID 204 228 {ECO:0000256|PIRSR:PIRSR001145-3}. FT DISULFID 236 367 Interchain (between A and B chains). FT {ECO:0000256|PIRSR:PIRSR001145-3}. FT DISULFID 279 295 {ECO:0000256|PIRSR:PIRSR001145-3}. FT DISULFID 287 356 {ECO:0000256|PIRSR:PIRSR001145-3}. FT DISULFID 381 456 {ECO:0000256|PIRSR:PIRSR001145-3}. FT DISULFID 413 429 {ECO:0000256|PIRSR:PIRSR001145-3}. FT DISULFID 446 474 {ECO:0000256|PIRSR:PIRSR001145-3}. SQ SEQUENCE 499 AA; 55895 MW; 7408BB2A554289A4 CRC64; MDAMKRGLCC VLLLCGAVFV SPSQEIHARF RRGARSYQVI CRDEKTQMIY QQHQSWLRPV LRSNRVEYCW CNSGRAQCHS VPVKSCSEPR CFNGGTCQQA LYFSDFVCQC PEGFAGKCCE IDSKPWCYVF KAGKYSSEFC STPACSEGNS DCYFGNGSAY RGTHSLTESG ASCLPWNSMI LIGKVYTAQN PSAQALGLGK HNYCRNPDGD AKPWCHVLKN RRLTWEYCDV PSCSTCGLRQ YSQPQFRIKG GLFADIASHP WQAAIFAKHR RSPGERFLCG GILISSCWIL SAAHCFQERF PPHHLTVILG RTYRVVPGEE EQKFEVEKYI VHKEFDDDTY DNDIALLQLK SDSSRCAQES SVVRTVCLPP ADLQLPDWTE CELSGYGKHE ALSPFYSERL KEAHVRLYPS SRCTSQHLLN RTVTDNMLCA GDTRSGGPQA NLHDACQGDS GGPLVCLNDG RMTLVGIISW GLGCGQKDVP GVYTKVTNYL DWIRDNMRP //