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   24-JAN-2024, entry version 190.
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   GlyCosmos; Q9R098; 6 sites, No reported glycans.
DR   GlyGen; Q9R098; 6 sites.
DR   iPTMnet; Q9R098; -.
DR   PhosphoSitePlus; Q9R098; -.
DR   CPTAC; non-CPTAC-3581; -.
DR   MaxQB; Q9R098; -.
DR   PaxDb; 10090-ENSMUSP00000030985; -.
DR   ProteomicsDB; 269565; -.
DR   Antibodypedia; 3925; 199 antibodies from 23 providers.
DR   DNASU; 54426; -.
DR   Ensembl; ENSMUST00000030985.10; ENSMUSP00000030985.7; ENSMUSG00000029102.10.
DR   GeneID; 54426; -.
DR   KEGG; mmu:54426; -.
DR   UCSC; uc008xdj.2; mouse.
DR   AGR; MGI:1859281; -.
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; 4629979at2759; -.
DR   PhylomeDB; Q9R098; -.
DR   TreeFam; TF329901; -.
DR   Reactome; R-MMU-6806942; MET Receptor Activation.
DR   BioGRID-ORCS; 54426; 2 hits in 79 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 cell types or tissues.
DR   ExpressionAtlas; Q9R098; baseline and differential.
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:0031638; P:zymogen activation; IBA:GO_Central.
DR   CDD; cd00054; EGF_CA; 2.
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; Fibronectin, type II, collagen-binding; 1.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 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   PANTHER; PTHR24264:SF43; HEPATOCYTE GROWTH FACTOR ACTIVATOR; 1.
DR   PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR   Pfam; PF00008; EGF; 2.
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   PRINTS; PR00013; FNTYPEII.
DR   PRINTS; PR00018; KRINGLE.
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; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF57440; Kringle-like; 2.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
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.
DR   Genevisible; Q9R098; MM.
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
//