ID HGF_RAT Reviewed; 728 AA. AC P17945; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 02-NOV-2016, entry version 148. DE RecName: Full=Hepatocyte growth factor; DE AltName: Full=Hepatopoietin-A; DE AltName: Full=Scatter factor; DE Short=SF; DE Contains: DE RecName: Full=Hepatocyte growth factor alpha chain; DE Contains: DE RecName: Full=Hepatocyte growth factor beta chain; DE Flags: Precursor; GN Name=Hgf; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=Wistar; TISSUE=Liver; RX PubMed=2139229; DOI=10.1073/pnas.87.8.3200; RA Toshiro K., Hagiya M., Nishizawa T., Seki T., Shimonishi M., RA Shimizu S., Nakamura T.; RT "Deduced primary structure of rat hepatocyte growth factor and RT expression of the mRNA in rat tissues."; RL Proc. Natl. Acad. Sci. U.S.A. 87:3200-3204(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Wistar; TISSUE=Liver; RX PubMed=2146117; DOI=10.1111/j.1432-1033.1990.tb19349.x; RA Okajima A., Miyazawa K., Kitamura N.; RT "Primary structure of rat hepatocyte growth factor and induction of RT its mRNA during liver regeneration following hepatic injury."; RL Eur. J. Biochem. 193:375-381(1990). CC -!- FUNCTION: Potent mitogen for mature parenchymal hepatocyte cells, CC seems to be a hepatotrophic factor, and acts as a growth factor CC for a broad spectrum of tissues and cell types. Activating ligand CC for the receptor tyrosine kinase MET by binding to it and CC promoting its dimerization (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Dimer of an alpha chain and a beta chain linked by a CC disulfide bond. Interacts with SRPX2; the interaction increases CC HGF mitogenic activity. CC -!- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}. CC -!- SIMILARITY: Contains 4 kringle domains. {ECO:0000255|PROSITE- CC ProRule:PRU00121}. CC -!- SIMILARITY: Contains 1 PAN domain. {ECO:0000255|PROSITE- CC ProRule:PRU00315}. CC -!- SIMILARITY: Contains 1 peptidase S1 domain. {ECO:0000255|PROSITE- CC ProRule:PRU00274}. CC -!- CAUTION: Has lost two of the three essential catalytic residues CC and so probably has no enzymatic activity. {ECO:0000305}. 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; D90102; BAA14133.1; -; mRNA. DR EMBL; X54400; CAA38266.1; -; mRNA. DR PIR; A35644; A35644. DR RefSeq; NP_058713.1; NM_017017.2. DR UniGene; Rn.10468; -. DR ProteinModelPortal; P17945; -. DR BioGrid; 246610; 2. DR MINT; MINT-219643; -. DR STRING; 10116.ENSRNOP00000009764; -. DR MEROPS; S01.978; -. DR PaxDb; P17945; -. DR PRIDE; P17945; -. DR Ensembl; ENSRNOT00000009763; ENSRNOP00000009764; ENSRNOG00000007027. DR GeneID; 24446; -. DR KEGG; rno:24446; -. DR CTD; 3082; -. DR RGD; 2794; Hgf. DR eggNOG; ENOG410IDXR; Eukaryota. DR eggNOG; COG5640; LUCA. DR GeneTree; ENSGT00760000119133; -. DR HOGENOM; HOG000112892; -. DR HOVERGEN; HBG004381; -. DR InParanoid; P17945; -. DR KO; K05460; -. DR OMA; GSESPWC; -. DR OrthoDB; EOG091G0AH5; -. DR PhylomeDB; P17945; -. DR TreeFam; TF329901; -. DR Reactome; R-RNO-114608; Platelet degranulation. DR PMAP-CutDB; P17945; -. DR PRO; PR:P17945; -. DR Proteomes; UP000002494; Chromosome 4. DR Bgee; ENSRNOG00000007027; -. DR Genevisible; P17945; RN. DR GO; GO:0005615; C:extracellular space; IDA:RGD. DR GO; GO:0016020; C:membrane; IEA:Ensembl. DR GO; GO:0042056; F:chemoattractant activity; IEA:Ensembl. DR GO; GO:0008083; F:growth factor activity; IMP:RGD. DR GO; GO:0046982; F:protein heterodimerization activity; IDA:RGD. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0000187; P:activation of MAPK activity; IEA:Ensembl. DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD. DR GO; GO:0060326; P:cell chemotaxis; IEA:Ensembl. DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl. DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IEA:Ensembl. DR GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; IBA:GO_Central. DR GO; GO:0030212; P:hyaluronan metabolic process; IEP:RGD. DR GO; GO:0001889; P:liver development; IEA:Ensembl. DR GO; GO:0061138; P:morphogenesis of a branching epithelium; IBA:GO_Central. DR GO; GO:0051450; P:myoblast proliferation; IEA:Ensembl. DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD. DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl. DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl. DR GO; GO:1901299; P:negative regulation of hydrogen peroxide-mediated programmed cell death; IEA:Ensembl. DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl. DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IEA:Ensembl. DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IEA:Ensembl. DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IEA:Ensembl. DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:RGD. DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl. DR GO; GO:0008284; P:positive regulation of cell proliferation; TAS:RGD. DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IEA:Ensembl. DR GO; GO:0032733; P:positive regulation of interleukin-10 production; IEA:Ensembl. DR GO; GO:0031643; P:positive regulation of myelination; IDA:RGD. DR GO; GO:0070572; P:positive regulation of neuron projection regeneration; IDA:RGD. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl. DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl. DR GO; GO:0060665; P:regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling; IEA:Ensembl. DR GO; GO:1900744; P:regulation of p38MAPK cascade; IEA:Ensembl. DR GO; GO:1902947; P:regulation of tau-protein kinase activity; IEA:Ensembl. DR CDD; cd00190; Tryp_SPc; 1. DR InterPro; IPR027284; Hepatocyte_GF. DR InterPro; IPR024174; HGF-like. DR InterPro; IPR000001; Kringle. DR InterPro; IPR013806; Kringle-like. DR InterPro; IPR018056; Kringle_CS. DR InterPro; IPR003609; Pan_app. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR001254; Trypsin_dom. DR Pfam; PF00051; Kringle; 4. DR Pfam; PF00024; PAN_1; 1. DR Pfam; PF00089; Trypsin; 1. DR PIRSF; PIRSF500183; Hepatocyte_GF; 1. DR PIRSF; PIRSF001152; HGF_MST1; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00130; KR; 4. DR SMART; SM00473; PAN_AP; 1. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; SSF50494; 1. DR SUPFAM; SSF57440; SSF57440; 4. DR PROSITE; PS00021; KRINGLE_1; 4. DR PROSITE; PS50070; KRINGLE_2; 4. DR PROSITE; PS50948; PAN; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Growth factor; Kringle; Pyrrolidone carboxylic acid; KW Reference proteome; Repeat; Serine protease homolog; Signal. FT SIGNAL 1 32 {ECO:0000250}. FT CHAIN 33 495 Hepatocyte growth factor alpha chain. FT /FTId=PRO_0000028095. FT CHAIN 496 728 Hepatocyte growth factor beta chain. FT /FTId=PRO_0000028096. FT DOMAIN 38 124 PAN. {ECO:0000255|PROSITE- FT ProRule:PRU00315}. FT DOMAIN 129 207 Kringle 1. {ECO:0000255|PROSITE- FT ProRule:PRU00121}. FT DOMAIN 212 289 Kringle 2. {ECO:0000255|PROSITE- FT ProRule:PRU00121}. FT DOMAIN 306 384 Kringle 3. {ECO:0000255|PROSITE- FT ProRule:PRU00121}. FT DOMAIN 392 470 Kringle 4. {ECO:0000255|PROSITE- FT ProRule:PRU00121}. FT DOMAIN 496 724 Peptidase S1. {ECO:0000255|PROSITE- FT ProRule:PRU00274}. FT MOD_RES 33 33 Pyrrolidone carboxylic acid. FT {ECO:0000250|UniProtKB:P14210}. FT CARBOHYD 295 295 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 403 403 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 569 569 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 656 656 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 71 97 {ECO:0000250}. FT DISULFID 75 85 {ECO:0000250}. FT DISULFID 129 207 {ECO:0000250}. FT DISULFID 150 190 {ECO:0000250}. FT DISULFID 178 202 {ECO:0000250}. FT DISULFID 212 289 {ECO:0000250}. FT DISULFID 233 272 {ECO:0000250}. FT DISULFID 261 284 {ECO:0000250}. FT DISULFID 306 384 {ECO:0000250}. FT DISULFID 327 366 {ECO:0000250}. FT DISULFID 355 378 {ECO:0000250}. FT DISULFID 392 470 {ECO:0000250}. FT DISULFID 413 453 {ECO:0000250}. FT DISULFID 441 465 {ECO:0000250}. FT DISULFID 488 607 Interchain (between alpha and beta FT chains). {ECO:0000255|PROSITE- FT ProRule:PRU00121, ECO:0000255|PROSITE- FT ProRule:PRU00274, ECO:0000255|PROSITE- FT ProRule:PRU00315}. FT DISULFID 520 536 {ECO:0000250}. FT DISULFID 615 682 {ECO:0000250}. FT DISULFID 645 661 {ECO:0000250}. FT DISULFID 672 700 {ECO:0000250}. SQ SEQUENCE 728 AA; 82906 MW; 3E0BF1F96ADCEDFF CRC64; MMWGTKLLPV LLLQHVLLHL LLLPVTIPYA EGQKKRRNTL HEFKKSAKTT LTKEDPLVKI KTKKVNSADE CANRCIRNKG FPFTCKAFVF DKSRKRCYWY PFNSMSSGVK KGFGHEFDLY ENKDYIRNCI IGKGGSYKGT VSITKSGIKC QPWNSMIPHE HSFLPSSYRG KDLQENYCRN PRGEEGGPWC FTSNPEVRYE VCDIPQCSEV ECMTCNGESY RGPMDHTESG KTCQRWDQQT PHRHKFLPER YPDKGFDDNY CRNPDGKPRP WCYTLDPDTP WEYCAIKMCA HSAVNETDVP METTECIKGQ GEGYRGTTNT IWNGIPCQRW DSQYPHKHDI TPENFKCKDL RENYCRNPDG AESPWCFTTD PNIRVGYCSQ IPKCDVSSGQ DCYRGNGKNY MGNLSKTRSG LTCSMWDKNM EDLHRHIFWE PDASKLTKNY CRNPDDDAHG PWCYTGNPLV PWDYCPISRC EGDTTPTIVN LDHPVISCAK TKQLRVVNGI PTQTTVGWMV SLKYRNKHIC GGSLIKESWV LTARQCFPAR NKDLKDYEAW LGIHDVHERG EEKRKQILNI SQLVYGPEGS DLVLLKLARP AILDNFVSTI DLPSYGCTIP EKTTCSIYGW GYTGLINADG LLRVAHLYIM GNEKCSQHHQ GKVTLNESEL CAGAEKIGSG PCEGDYGGPL ICEQHKMRMV LGVIVPGRGC AIPNRPGIFV RVAYYAKWIH KVILTYKL //