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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
 
 
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