ID L5JNS7_PTEAL Unreviewed; 688 AA.
AC L5JNS7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=PAL_GLEAN10013659 {ECO:0000313|EMBL:ELK01000.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK01000.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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; KB031154; ELK01000.1; -; Genomic_DNA.
DR AlphaFoldDB; L5JNS7; -.
DR STRING; 9402.L5JNS7; -.
DR MEROPS; S01.976; -.
DR eggNOG; ENOG502QR40; Eukaryota.
DR InParanoid; L5JNS7; -.
DR Proteomes; UP000010552; 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:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00108; KR; 4.
DR CDD; cd00129; PAN_APPLE; 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:UP000010552};
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..445
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 453..681
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:ELK01000.1"
SQ SEQUENCE 688 AA; 78686 MW; 21B8858A431CF1C6 CRC64;
EGQKKRRNTL HEFKKSAKTT LHKEDPLLKI KTKKMNTADQ CANRCIRNKG LPFTCKAFVF
DKARKRCLWF PFNSMSSGVK KEFGHEFDLY ENKDYIRNCI IGKGGSYKGT VSITKSGIKC
QPWNSMIPHE HSFLPSSYRG KDLQENYCRN PRGEEGGPWC FTSNPEVRYE VCDIPQCSEV
ECMTCNGESY RGPMDHTESG KICQRWDQQM PHRHKFLPER YPDKGFDDNY CRNPDGKPRP
WCYTLDPDTP WEYCAIKMCA HSSMNDSNVP METTECIQAQ GEGYRGTINT IWNGIPCQRW
DSQYPHQHDI TPENFKCKDL RENYCRNPDG AESPWCFTTD PNIRVGYCSQ IPKCDVSSGQ
DCYRGNGKNY MGNLSKTRSG LTCSMWDKNM EDLHRHIFWE PDASKLNKNY CRNPDDDAHG
PWCYTGNPLI PWDYCPISRY PVISCAKTKQ LRVVNGIPTR TNVGWMVSLK YRNKHICGGS
LIKESWILTA RQCFPSRNKD LKDYEAWLGI HDVHGRGDEK RRQVLNVSQL VYGPEGSDLV
LLKLARPAVL DDFVSTIDLP NYGCTIPEKT TCSVYGWGYT GLINSDGLLR VAHLYIMGNE
KCSQYHQGKV TLNESEICAG AENIVTGPCE GDYGGPLVCE QHKMRMVLGV IVPGRGCAIP
NRPGIFVRVA YYAKWIHKII LTYKVPQS
//
