ID A0A087YDJ9_POEFO Unreviewed; 709 AA.
AC A0A087YDJ9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 28-JAN-2026, entry version 57.
DE SubName: Full=Macrophage stimulating 1 {ECO:0000313|Ensembl:ENSPFOP00000016102.2};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000016102.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000016102.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSPFOP00000016102.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen subfamily.
CC {ECO:0000256|PIRNR:PIRNR001152}.
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; AYCK01000406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007550580.1; XM_007550518.2.
DR RefSeq; XP_007550587.1; XM_007550525.2.
DR AlphaFoldDB; A0A087YDJ9; -.
DR STRING; 48698.ENSPFOP00000016102; -.
DR MEROPS; S01.977; -.
DR Ensembl; ENSPFOT00000016124.2; ENSPFOP00000016102.2; ENSPFOG00000015941.2.
DR GeneID; 103137009; -.
DR KEGG; pfor:103137009; -.
DR CTD; 4485; -.
DR eggNOG; ENOG502QRJ0; Eukaryota.
DR GeneTree; ENSGT00940000159461; -.
DR OrthoDB; 41905at2759; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:TreeGrafter.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0046425; P:regulation of receptor signaling pathway via JAK-STAT; IEA:TreeGrafter.
DR CDD; cd00108; KR; 4.
DR CDD; cd01099; PAN_AP_HGF; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR FunFam; 2.40.10.10:FF:000063; Hepatocyte growth factor; 1.
DR FunFam; 2.40.20.10:FF:000002; Hepatocyte growth factor; 2.
DR FunFam; 2.40.20.10:FF:000004; Hepatocyte growth factor; 1.
DR FunFam; 2.40.10.10:FF:000055; Hepatocyte growth factor-like 1; 1.
DR FunFam; 2.40.20.10:FF:000009; Hepatocyte growth factor-like 1; 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; 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; IPR050759; Serine_protease_kringle.
DR InterPro; IPR001254; Trypsin_dom.
DR PANTHER; PTHR24261:SF12; HEPATOCYTE GROWTH FACTOR-LIKE PROTEIN-RELATED; 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; 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; 3.
DR PROSITE; PS50070; KRINGLE_2; 4.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease homolog {ECO:0000256|ARBA:ARBA00022542,
KW ECO:0000256|PIRNR:PIRNR001152};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..709
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001834347"
FT DOMAIN 20..104
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 108..185
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 189..267
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 283..362
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 370..449
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 482..707
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 190..267
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 211..250
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 239..262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 305..344
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 333..356
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 709 AA; 81012 MW; 25700747D8B738A1 CRC64;
MKPFLLCILL ITGLTTALRS SLNDYQRSEG RELVPTAWNA ARMQMLPGLN LEECASRCSQ
SQDCRAFNYE IRPVGTCKHL PWVADGSNAE VKRNVNCDLY EKKVYVRKCI VGKGEDYRGK
VFTTKSGLTC QQWWSKFPHD HRWTPSPTNG LELNYCRNPD GDRIGPWCYT TDPERRYESC
NIPQCKDEVC ITCNGEDYRG QVDHTESGKE CQRWDQQFPH QHIYQPEKYP DKSLDDNYCR
NPDASPVPWC YTTDPETERE SCDISKCTEV LVEKRQRSSF TTNCFRGRGE DYRGKVNETA
SGIACQRWDV QVPHRHPFIP NIYECKGLEE NYCRNPDGSE APWCFTSVPE MRTVLCLQIK
RCADDIEAED CYNENGKNYR GVVRKTRKGI TCQKWNVNTP HQTRINPRTH PDANLTENYC
RNPDGDQHGP WCYTTDPKTE FDYCAIKQCA GEKLPLTETV ETVEFSECGK RDDRPQPTRL
RIVNGIPGNS PWTVSLRDRK GNHFCGGSLV NPRWVISTKQ CFSSCYVDLP GYSAMMGTLF
RDPQEGEPGV QTIPLTKIVC GPSESQLVML QLEYPAQFNE RVSQICLPPE RYIVPEHTKC
EIAGWGETRG TGDETVLNVA HVPVISNTEC NRYFRGRVRE NEMCTNSFQA GVGACEKDYG
GPLACQNADC WVLEGVIIPM RRCGHPGQPN IFIRVSVYVD WIKKVMEMA
//
