GenomeNet

Database: UniProt
Entry: Q6QNF4
LinkDB: Q6QNF4
Original site: Q6QNF4 
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   08-MAY-2019, entry version 99.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   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
RT   HGF on canine osteosarcoma cell line.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Activates hepatocyte growth factor (HGF) by converting
CC       it 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
CC       single-chain precursor and is then activated to a heterodimeric
CC       form.
CC   -!- TISSUE SPECIFICITY: Liver.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; AY532633; AAS48370.1; -; mRNA.
DR   RefSeq; NP_001026985.1; NM_001031815.2.
DR   SMR; Q6QNF4; -.
DR   STRING; 9612.ENSCAFP00000021566; -.
DR   MEROPS; S01.228; -.
DR   PaxDb; Q6QNF4; -.
DR   PRIDE; Q6QNF4; -.
DR   GeneID; 403432; -.
DR   KEGG; cfa:403432; -.
DR   CTD; 3083; -.
DR   eggNOG; KOG1217; Eukaryota.
DR   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   HOGENOM; HOG000237314; -.
DR   InParanoid; Q6QNF4; -.
DR   KO; K09631; -.
DR   OrthoDB; 1314811at2759; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005791; C:rough endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; 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; 2.40.20.10; -; 1.
DR   InterPro; IPR014394; Coagulation_fac_XII/HGFA.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
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; 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   Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Hydrolase; Kringle; Protease; Reference proteome; Repeat; Secreted;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL        1     33       {ECO:0000255}.
FT   PROPEP       34    370       Removed in mature form. {ECO:0000250}.
FT                                /FTId=PRO_0000041840.
FT   CHAIN       371    406       Hepatocyte growth factor activator short
FT                                chain.
FT                                /FTId=PRO_0000041841.
FT   CHAIN       407    654       Hepatocyte growth factor activator long
FT                                chain.
FT                                /FTId=PRO_0000041842.
FT   DOMAIN      101    148       Fibronectin type-II.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000255|PROSITE-ProRule:PRU00479}.
FT   DOMAIN      158    196       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      198    238       Fibronectin type-I. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00478}.
FT   DOMAIN      239    277       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      283    365       Kringle. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00121}.
FT   DOMAIN      407    645       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    446    446       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    496    496       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    597    597       Charge relay system. {ECO:0000250}.
FT   CARBOHYD     38     38       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     46     46       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    288    288       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    467    467       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    545    545       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    106    131       {ECO:0000250}.
FT   DISULFID    120    146       {ECO:0000250}.
FT   DISULFID    162    173       {ECO:0000250}.
FT   DISULFID    167    184       {ECO:0000250}.
FT   DISULFID    186    195       {ECO:0000250}.
FT   DISULFID    200    228       {ECO:0000250}.
FT   DISULFID    226    235       {ECO:0000250}.
FT   DISULFID    243    254       {ECO:0000250}.
FT   DISULFID    248    265       {ECO:0000250}.
FT   DISULFID    267    276       {ECO:0000250}.
FT   DISULFID    284    365       {ECO:0000250}.
FT   DISULFID    305    347       {ECO:0000250}.
FT   DISULFID    336    360       {ECO:0000250}.
FT   DISULFID    393    520       Interchain (between short and long
FT                                chains). {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076, ECO:0000255|PROSITE-
FT                                ProRule:PRU00121, ECO:0000255|PROSITE-
FT                                ProRule:PRU00274, ECO:0000255|PROSITE-
FT                                ProRule:PRU00478, ECO:0000255|PROSITE-
FT                                ProRule:PRU00479}.
FT   DISULFID    431    447       {ECO:0000250}.
FT   DISULFID    439    509       {ECO:0000250}.
FT   DISULFID    534    603       {ECO:0000250}.
FT   DISULFID    566    582       {ECO:0000250}.
FT   DISULFID    593    621       {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
//
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