ID A0A099ZKM4_TINGU Unreviewed; 700 AA.
AC A0A099ZKM4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Hepatocyte growth factor {ECO:0000256|ARBA:ARBA00021784};
DE AltName: Full=Hepatopoietin-A {ECO:0000256|ARBA:ARBA00033078};
DE AltName: Full=Scatter factor {ECO:0000256|ARBA:ARBA00031997};
DE Flags: Fragment;
GN ORFNames=N309_03563 {ECO:0000313|EMBL:KGL82342.1};
OS Tinamus guttatus (White-throated tinamou).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL82342.1, ECO:0000313|Proteomes:UP000053641};
RN [1] {ECO:0000313|EMBL:KGL82342.1, ECO:0000313|Proteomes:UP000053641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL82342.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Dimer of an alpha chain and a beta chain linked by a disulfide
CC bond. Interacts with SRPX2; the interaction increases HGF mitogenic
CC activity. {ECO:0000256|ARBA:ARBA00025867}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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DR EMBL; KL895134; KGL82342.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099ZKM4; -.
DR STRING; 94827.A0A099ZKM4; -.
DR Proteomes; UP000053641; Unassembled WGS sequence.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0010629; P:negative regulation of gene expression; ISS:AgBase.
DR GO; GO:1902725; P:negative regulation of satellite cell differentiation; ISS:AgBase.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:AgBase.
DR GO; GO:1902724; P:positive regulation of skeletal muscle satellite cell proliferation; ISS:AgBase.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00108; KR; 4.
DR CDD; cd01099; PAN_AP_HGF; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 4.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR027284; Hepatocyte_GF.
DR InterPro; IPR024174; HGF/MST1.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR PANTHER; PTHR24261:SF8; HEPATOCYTE GROWTH FACTOR; 1.
DR PANTHER; PTHR24261; PLASMINOGEN-RELATED; 1.
DR Pfam; PF00051; Kringle; 4.
DR Pfam; PF00024; PAN_1; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF500183; Hepatocyte_GF; 1.
DR PIRSF; PIRSF001152; HGF_MST1; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00018; KRINGLE.
DR SMART; SM00130; KR; 4.
DR SMART; SM00473; PAN_AP; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57414; Hairpin loop containing domain-like; 1.
DR SUPFAM; SSF57440; Kringle-like; 4.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00021; KRINGLE_1; 4.
DR PROSITE; PS50070; KRINGLE_2; 4.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Growth factor {ECO:0000256|ARBA:ARBA00023030};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Pyrrolidone carboxylic acid {ECO:0000256|ARBA:ARBA00023283};
KW Reference proteome {ECO:0000313|Proteomes:UP000053641};
KW Serine protease homolog {ECO:0000256|ARBA:ARBA00022542}.
FT DOMAIN 5..95
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 99..178
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 182..260
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 276..355
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 362..443
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 469..697
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 183..260
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 204..243
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 232..255
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 298..337
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 326..349
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL82342.1"
FT NON_TER 700
FT /evidence="ECO:0000313|EMBL:KGL82342.1"
SQ SEQUENCE 700 AA; 79724 MW; BDBF0583B66EFC21 CRC64;
SEGKAKRRNP LHDFKKTGEM MLIKVNKSLE VKTKLLNTTE QCAKRCNRNK GLSFTCKAFA
YDRVTKRCHW LSFTSLTNGV RKKQDHAFDL YEKKDYVRNC IIGKGANYKG TISVTRSGIQ
CQAWNSMIPH EHSFLPSSYR GKDLRENYCR NPRGEEGGPW CFTTSPETRH EVCDIPLCSA
VECMTCNGES YRGPMDHTES GKECQRWDLQ RPHKHKFRPE RYPDKGFDDN YCRNPDGKLR
PWCYTLDPNT PWEFCAIKTC DPSVVNSTDA AAETLTCSQG QGEGYRGTVS TIWSGVPCQR
WDSQFPHQHN ITPENFKCKD LRENYCRNPD GSESPWCFTT DPNIRIGYCS QIPKCDISNE
QDCYRGNGKS YMGNLSKTRF GLTCSTWDKN IEDLRRHIPI FREPDVSKLK KNYCRNPDDD
AHGPWCYTDD PLVPWDYCPI SRCEGDTTPI TTNLDDTVIP CASTKQVRVV NGNPTQTNKG
WMVSLTYRNK HICGGSLIKE DWVLTARQCF PSRYKDLKDY EAWLGVHNIK GRGEEKHKQV
RNISQLVYGP EGSDLVLLKL SRPAILTNFV DIIRLPISGC TIPEKTACSV YGWGYTGLVH
YDGLLRAANL FILGNEKCNQ YLKGKITVNE SEICAAAETV GAGPCERDYG GPLVCEQNRV
KIVVGVIVPG RGCAIRNRPG IFVRVAFYSK WIRKILLTYR
//
