HGFA_MOUSE
ID HGFA_MOUSE Reviewed; 653 AA.
AC Q9R098; Q9JKV4;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Hepatocyte growth factor activator;
DE Short=HGF activator;
DE Short=HGFA;
DE EC=3.4.21.-;
DE Contains:
DE RecName: Full=Hepatocyte growth factor activator short chain;
DE Contains:
DE RecName: Full=Hepatocyte growth factor activator long chain;
DE Flags: Precursor;
GN Name=Hgfac;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=10760594; DOI=10.1016/s0167-4781(00)00029-4;
RA Itoh H., Hamasuna R., Kataoka H., Yamauchi M., Miyazawa K., Kitamura N.,
RA Koono M.;
RT "Mouse hepatocyte growth factor activator gene: its expression not only in
RT the liver but also in the gastrointestinal tract.";
RL Biochim. Biophys. Acta 1491:295-302(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11032833; DOI=10.1074/jbc.m006634200;
RA van Adelsberg J.S., Sehgal S., Kukes A., Brady C., Barasch J., Yang J.,
RA Huan Y.;
RT "Activation of hepatocyte growth factor (HGF) by endogenous HGF activator
RT is required for metanephric kidney morphogenesis in vitro.";
RL J. Biol. Chem. 276:15099-15106(2001).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-466.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-287.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
CC -!- FUNCTION: Activates hepatocyte growth factor (HGF) by converting it
CC from a single chain to a heterodimeric form. {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of a short chain and a long chain linked by a
CC disulfide bond. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Secreted as an
CC inactive single-chain precursor and is then activated to a
CC heterodimeric form. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AF099017; AAF02489.1; -; mRNA.
DR EMBL; AF224724; AAF34712.1; -; mRNA.
DR CCDS; CCDS19223.1; -.
DR RefSeq; NP_062320.2; NM_019447.3.
DR AlphaFoldDB; Q9R098; -.
DR SMR; Q9R098; -.
DR STRING; 10090.ENSMUSP00000030985; -.
DR MEROPS; S01.228; -.
DR GlyGen; Q9R098; 6 sites.
DR iPTMnet; Q9R098; -.
DR PhosphoSitePlus; Q9R098; -.
DR CPTAC; non-CPTAC-3581; -.
DR MaxQB; Q9R098; -.
DR PaxDb; Q9R098; -.
DR PRIDE; Q9R098; -.
DR ProteomicsDB; 269565; -.
DR Antibodypedia; 3925; 158 antibodies from 23 providers.
DR DNASU; 54426; -.
DR Ensembl; ENSMUST00000030985; ENSMUSP00000030985; ENSMUSG00000029102.
DR GeneID; 54426; -.
DR KEGG; mmu:54426; -.
DR UCSC; uc008xdj.2; mouse.
DR CTD; 3083; -.
DR MGI; MGI:1859281; Hgfac.
DR VEuPathDB; HostDB:ENSMUSG00000029102; -.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000159778; -.
DR HOGENOM; CLU_006842_18_1_1; -.
DR InParanoid; Q9R098; -.
DR OMA; ETRYEYF; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q9R098; -.
DR TreeFam; TF329901; -.
DR Reactome; R-MMU-6806942; MET Receptor Activation.
DR BioGRID-ORCS; 54426; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Hgfac; mouse.
DR PRO; PR:Q9R098; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9R098; protein.
DR Bgee; ENSMUSG00000029102; Expressed in left lobe of liver and 59 other tissues.
DR ExpressionAtlas; Q9R098; baseline and differential.
DR Genevisible; Q9R098; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0007596; P:blood coagulation; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0031638; P:zymogen activation; IBA:GO_Central.
DR CDD; cd00061; FN1; 1.
DR CDD; cd00062; FN2; 1.
DR CDD; cd00108; KR; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.10.10.10; -; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 2.40.20.10; -; 1.
DR InterPro; IPR014394; Coagulation_fac_XII/HGFA.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000083; Fibronectin_type1.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
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; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00039; fn1; 1.
DR Pfam; PF00040; fn2; 1.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001146; Factor_XII_HGFA; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00058; FN1; 1.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00130; KR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57440; SSF57440; 2.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01253; FN1_1; 1.
DR PROSITE; PS51091; FN1_2; 1.
DR PROSITE; PS00023; FN2_1; 1.
DR PROSITE; PS51092; FN2_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 Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Kringle;
KW Protease; Reference proteome; Repeat; Secreted; Serine protease; Signal;
KW Zymogen.
FT SIGNAL 1..34
FT /evidence="ECO:0000250"
FT PROPEP 35..369
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000027914"
FT CHAIN 370..405
FT /note="Hepatocyte growth factor activator short chain"
FT /id="PRO_0000027915"
FT CHAIN 406..653
FT /note="Hepatocyte growth factor activator long chain"
FT /id="PRO_0000027916"
FT DOMAIN 100..147
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478,
FT ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 157..195
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 197..237
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 238..276
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 283..364
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 406..644
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 34..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 445
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 495
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 596
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 105..130
FT /evidence="ECO:0000250"
FT DISULFID 119..145
FT /evidence="ECO:0000250"
FT DISULFID 161..172
FT /evidence="ECO:0000250"
FT DISULFID 166..183
FT /evidence="ECO:0000250"
FT DISULFID 185..194
FT /evidence="ECO:0000250"
FT DISULFID 199..227
FT /evidence="ECO:0000250"
FT DISULFID 225..234
FT /evidence="ECO:0000250"
FT DISULFID 242..253
FT /evidence="ECO:0000250"
FT DISULFID 247..264
FT /evidence="ECO:0000250"
FT DISULFID 266..275
FT /evidence="ECO:0000250"
FT DISULFID 283..364
FT /evidence="ECO:0000250"
FT DISULFID 304..346
FT /evidence="ECO:0000250"
FT DISULFID 335..359
FT /evidence="ECO:0000250"
FT DISULFID 392..519
FT /note="Interchain (between short and long chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000255|PROSITE-ProRule:PRU00121, ECO:0000255|PROSITE-
FT ProRule:PRU00274, ECO:0000255|PROSITE-ProRule:PRU00478,
FT ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 430..446
FT /evidence="ECO:0000250"
FT DISULFID 438..508
FT /evidence="ECO:0000250"
FT DISULFID 533..602
FT /evidence="ECO:0000250"
FT DISULFID 565..581
FT /evidence="ECO:0000250"
FT DISULFID 592..620
FT /evidence="ECO:0000250"
FT CONFLICT 164
FT /note="G -> W (in Ref. 2; AAF34712)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 653 AA; 70568 MW; 88B4B20255DF7FDC CRC64;
MGRQAWISSL CPLPRPCPFL LLLLLLVVPR GAQPQAGRNH TEPPGPNVTA TPVTPTIPVI
SGNVSTSTES APAAETEGPQ SERYPPPSSS SPPGGQVLTE SGQPCRFPFR YGGRMLHSCT
SEGSAYRKWC ATTHNYDRDR AWGYCAEVTL PVEGPAILDP CASGPCLNGG TCSSTHDHGS
YHCSCPLAFT GKDCGTEKCF DETRYEYFEV GDHWARVSEG HVEQCGCMEG QARCEDTHHT
ACLSSPCLNG GTCHLIVGTG TSVCTCPLGY AGRFCNIVPT EHCFLGNGTE YRGVASTAAS
GLSCLAWNSD LLYQELHVDS VAAAVLLGLG PHAYCRNPDK DERPWCYVVK DNALSWEYCR
LTACESLARV HSQTPEILAA LPESAPAVRP TCGKRHKKRT FLRPRIIGGS SSLPGSHPWL
AAIYIGNSFC AGSLVHTCWV VSAAHCFANS PPRDSITVVL GQHFFNRTTD VTQTFGIEKY
VPYTLYSVFN PNNHDLVLIR LKKKGERCAV RSQFVQPICL PEAGSSFPTG HKCQIAGWGH
MDENVSSYSN SLLEALVPLV ADHKCSSPEV YGADISPNML CAGYFDCKSD ACQGDSGGPL
VCEKNGVAYL YGIISWGDGC GRLNKPGVYT RVANYVDWIN DRIRPPKRPV ATS
