ID A0A087RE68_APTFO Unreviewed; 701 AA.
AC A0A087RE68;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, 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=AS27_15268 {ECO:0000313|EMBL:KFM11772.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM11772.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM11772.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM11772.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-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; KL226332; KFM11772.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087RE68; -.
DR STRING; 9233.A0A087RE68; -.
DR Proteomes; UP000053286; 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; 3.
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:UP000053286};
KW Serine protease homolog {ECO:0000256|ARBA:ARBA00022542}.
FT DOMAIN 8..94
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 98..177
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 181..259
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 275..354
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 361..442
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 468..696
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 182..259
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 203..242
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 231..254
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 297..336
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 325..348
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM11772.1"
FT NON_TER 701
FT /evidence="ECO:0000313|EMBL:KFM11772.1"
SQ SEQUENCE 701 AA; 80244 MW; 5AD561227DD050DA CRC64;
EGKGKRRNPL HDFRKTGELM LIKINKTLEI KTKLLNTTEQ CAKRCSRNKG LSFTCKAFAY
DRVTKRCHWL SFNSLTNGVR KKQDHAFDLY EKKDYVRNCI IGKGADYKGT ISVTKSGIQC
QAWNSMIPHE HSFLPSSYRG KDLRENYCRN PRGEEGGPWC FTTSPETRHE VCDIPLCSQV
ECMTCNGESY RGPMDHTESG KECQRWDLQR PHKHKFRPER YPDKGFDDNY CRNPDGKLRP
WCYTLDPNTP WEFCAIKTCD ENIVNSTEAA AETSTCIQGQ GEGYRGTVNT IWSGIQCQRW
DSQFPHQHNI TPENFKCKDL RENYCRNPDG SESPWCFTTD PNIRIGYCSQ IPKCDVSNEQ
DCYRGNGKSY MGNLSKTRFG LNCATWDKNI EDLRRHIQIF REPDVSKLKK NYCRNPDDDF
HGPWCYTDDP LVPWDYCPIS RCEGDTTPTT TSLDDTVIPC ASTKHLRVVN GIPTQTNEGW
VVSLTYRNKH ICGGTLIKEE WVLTARQCFP SRYKDLKDYK AWLGVHNIKG KGEEKHRQIL
NISQLVYGPA GSDLVLLKLS RTAILTNFVE IIRLPISGCT IPEKTSCSVY GWGYTGLINY
DGLLRVANLF ILGNEEKCKY LKGKITVNES EICAVAETVG AGPCERDYGG PLVCEQNRLK
IVVGVIVPGR GCAIRNRPGI FVRVSYYSRW IHKIMMTYRK P
//
