HGFA_CANLF
ID HGFA_CANLF Reviewed; 654 AA.
AC Q6QNF4;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liao A.T., Chien M.B., London C.A.;
RT "Characterization of the receptor tyrosine kinase Met and its ligand HGF on
RT canine osteosarcoma cell line.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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. Note=Secreted as an inactive single-
CC chain precursor and is then activated to a heterodimeric form.
CC -!- TISSUE SPECIFICITY: Liver.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AY532633; AAS48370.1; -; mRNA.
DR RefSeq; NP_001026985.1; NM_001031815.2.
DR AlphaFoldDB; Q6QNF4; -.
DR SMR; Q6QNF4; -.
DR STRING; 9615.ENSCAFP00000021566; -.
DR MEROPS; S01.228; -.
DR PaxDb; Q6QNF4; -.
DR GeneID; 403432; -.
DR KEGG; cfa:403432; -.
DR CTD; 3083; -.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q6QNF4; -.
DR OrthoDB; 1314811at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR001881; EGF-like_Ca-bd_dom.
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; 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 SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 1.
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; 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 2: Evidence at transcript level;
KW Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Kringle;
KW Protease; Reference proteome; Repeat; Secreted; Serine protease; Signal;
KW Zymogen.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT PROPEP 34..370
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000041840"
FT CHAIN 371..406
FT /note="Hepatocyte growth factor activator short chain"
FT /id="PRO_0000041841"
FT CHAIN 407..654
FT /note="Hepatocyte growth factor activator long chain"
FT /id="PRO_0000041842"
FT DOMAIN 101..148
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478,
FT ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 158..196
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 198..238
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 239..277
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 283..365
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 407..645
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 34..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 446
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 496
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 597
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 106..131
FT /evidence="ECO:0000250"
FT DISULFID 120..146
FT /evidence="ECO:0000250"
FT DISULFID 162..173
FT /evidence="ECO:0000250"
FT DISULFID 167..184
FT /evidence="ECO:0000250"
FT DISULFID 186..195
FT /evidence="ECO:0000250"
FT DISULFID 200..228
FT /evidence="ECO:0000250"
FT DISULFID 226..235
FT /evidence="ECO:0000250"
FT DISULFID 243..254
FT /evidence="ECO:0000250"
FT DISULFID 248..265
FT /evidence="ECO:0000250"
FT DISULFID 267..276
FT /evidence="ECO:0000250"
FT DISULFID 284..365
FT /evidence="ECO:0000250"
FT DISULFID 305..347
FT /evidence="ECO:0000250"
FT DISULFID 336..360
FT /evidence="ECO:0000250"
FT DISULFID 393..520
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 431..447
FT /evidence="ECO:0000250"
FT DISULFID 439..509
FT /evidence="ECO:0000250"
FT DISULFID 534..603
FT /evidence="ECO:0000250"
FT DISULFID 566..582
FT /evidence="ECO:0000250"
FT DISULFID 593..621
FT /evidence="ECO:0000250"
SQ SEQUENCE 654 AA; 70245 MW; 4D9371D2680B2977 CRC64;
MGRWAWGPSL CPLPGMALLL LLLLLLVPHG AQPQAGGNLT EPPEPNATVT PGTPMIPVTS
VTPVTPATSA PEAQGPRGRG LTPPPRAAPS SSSPGDPVLT VDGQPCRFPF RYGGRMLHAC
TSEGSAHRKW CATTHNYDRD RAWGYCVQAP VSREGPAALD SCASSPCLNG GSCSHTQDPG
SYHCTCPMAF TGRNCDTEKC FDETRYEHLE AGDRWARVSQ GQVEQCECAG GQIRCEGTRH
TACLSSPCLN GGTCHLIVAT GTTVCSCPPG HAGRLCNIVP SQRCFVGNGT EYRGVASTAA
SGLSCLAWNS DLLYQELHVD SVGAAALLGL GPHAYCRNPD KDERPWCYVV KDSALSWEYC
RLAACESLAR IPSLTTAVLL SQAEPAPVGR QTCGKRHKKR TFLRPRIIGG SSSLPGSHPW
LAAIYIGDSF CAGSLVHTCW VVSAAHCFSN SPRRESVLVV LGQHFFNQTT DVTQTFGIEK
YIPYPMYSVF NPSDHDLVLI RLKKKGDRCA IRSQFVQPIC LPEPSSPFPA GHKCQIAGWG
HQDENVSGYS SSLREALVPL VADHKCSSPE VYGADISPNM LCAGYFDCKS DACQGDSGGP
LACEKNGVAY LYGIISWGDG CGRLNKPGVY TRVAKYVDWI KDRIWPSKRP SDPS
