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Database: UniProt
Entry: A0A672LYG1_SINGR
LinkDB: A0A672LYG1_SINGR
Original site: A0A672LYG1_SINGR 
ID   A0A672LYG1_SINGR        Unreviewed;       980 AA.
AC   A0A672LYG1;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   28-JAN-2026, entry version 29.
DE   RecName: Full=Mast/stem cell growth factor receptor {ECO:0000256|PIRNR:PIRNR500951};
DE            EC=2.7.10.1 {ECO:0000256|PIRNR:PIRNR500951};
GN   Name=kita {ECO:0000313|Ensembl:ENSSGRP00000029199.1};
OS   Sinocyclocheilus grahami (Dianchi golden-line fish) (Barbus grahami).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Sinocyclocheilus.
OX   NCBI_TaxID=75366 {ECO:0000313|Ensembl:ENSSGRP00000029199.1, ECO:0000313|Proteomes:UP000472262};
RN   [1] {ECO:0000313|Ensembl:ENSSGRP00000029199.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSSGRP00000029199.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:61978, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00051243,
CC         ECO:0000256|PIRNR:PIRNR500951};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Membrane {ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane
CC       protein {ECO:0000256|RuleBase:RU000311}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. CSF-1/PDGF receptor subfamily.
CC       {ECO:0000256|PIRNR:PIRNR500951, ECO:0000256|RuleBase:RU000311}.
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DR   RefSeq; XP_016149745.1; XM_016294259.1.
DR   AlphaFoldDB; A0A672LYG1; -.
DR   FunCoup; A0A672LYG1; 1074.
DR   Ensembl; ENSSGRT00000031399.1; ENSSGRP00000029199.1; ENSSGRG00000015937.1.
DR   GeneID; 107601906; -.
DR   KEGG; sgh:107601906; -.
DR   CTD; 30256; -.
DR   InParanoid; A0A672LYG1; -.
DR   OMA; CDSTNEY; -.
DR   OrthoDB; 6077854at2759; -.
DR   Proteomes; UP000472262; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043235; C:receptor complex; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019955; F:cytokine binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019838; F:growth factor binding; IEA:TreeGrafter.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030183; P:B cell differentiation; IEA:TreeGrafter.
DR   GO; GO:0038093; P:Fc receptor signaling pathway; IEA:UniProtKB-UniRule.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:TreeGrafter.
DR   GO; GO:0038109; P:Kit signaling pathway; IEA:InterPro.
DR   GO; GO:0030318; P:melanocyte differentiation; IEA:UniProtKB-ARBA.
DR   GO; GO:0097324; P:melanocyte migration; IEA:UniProtKB-ARBA.
DR   GO; GO:0030335; P:positive regulation of cell migration; IEA:TreeGrafter.
DR   GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IEA:TreeGrafter.
DR   CDD; cd00096; Ig; 1.
DR   FunFam; 1.10.510.10:FF:000177; Mast/stem cell growth factor receptor; 1.
DR   FunFam; 2.60.40.10:FF:000422; Mast/stem cell growth factor receptor; 1.
DR   FunFam; 3.30.200.20:FF:000025; Platelet-derived growth factor receptor alpha; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013151; Immunoglobulin_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR050122; RTK.
DR   InterPro; IPR027263; SCGF_receptor.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
DR   PANTHER; PTHR24416:SF46; MAST_STEM CELL GROWTH FACTOR RECEPTOR KIT; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF13927; Ig_3; 1.
DR   Pfam; PF25305; Ig_PDGFR_d4; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PIRSF; PIRSF500951; SCGF_recepter; 1.
DR   PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 4.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 4.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50835; IG_LIKE; 3.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR500951};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|PIRNR:PIRNR500951};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319,
KW   ECO:0000256|RuleBase:RU000311};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR500951};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR500951};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR500951};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR500951};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR500951};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR500951};
KW   Reference proteome {ECO:0000313|Proteomes:UP000472262};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PIRNR:PIRNR500951};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR500951};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|PIRNR:PIRNR500951};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|PIRNR:PIRNR500951};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW   ECO:0000256|PIRNR:PIRNR500951};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|PIRNR:PIRNR500951"
FT   CHAIN           22..980
FT                   /note="Mast/stem cell growth factor receptor"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR500951"
FT                   /id="PRO_5025720985"
FT   TRANSMEM        516..538
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR500951"
FT   DOMAIN          23..100
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          209..305
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          403..508
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          584..926
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        781
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT   BINDING         563
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         591..598
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         618
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         666..672
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         785
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         786
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         799
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   SITE            925
FT                   /note="Important for interaction with phosphotyrosine-
FT                   binding proteins"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
SQ   SEQUENCE   980 AA;  109953 MW;  47FBCFAFFA3FCAA4 CRC64;
     MEYHCVLFTV LLQLIVQPAR SRPTITPEGP QLIVPLNDDF SLHCQSDSSV RWLREDRPTR
     ILKEQRQGQV TVLKVSKAGP QHMGKYSCRE EASGEKSSIY VYVKAFLSAD PENPFRRNIM
     FDFVVGEGET TTLPCLATDP RMTDLHLQKC DGQPLPNTLR YSSSIETGIT LEDVRKDFEG
     CYVCVGTLEG NTVKSGLYQL NVRLVPDAPP VITLGQPQRV LLIQGEVLSL SCNTSNVNSD
     ITIRWKAPQG VQPSVQQFSN ILTKPISHLR NATLNLGSVT KQDAGSYNCE ARNERGTSTK
     TVWVEIYDKG FIILRSVNNS TKRVRAGESL SLRVVMDAYP KPHTFSWSYS GVKLTNTTDH
     VITSRSHGNS YTSELKLVRL KVLESGVYIF SCSNRDTTVH QSFEVHVISK PQIVSHDGPI
     DGQVRCVAEG YPTPQIKWYY CDQPHSRCSN SLNATQEEED VVTVTMTNPP FGKGTVESRL
     NITKNSYATL ECVASANGEI VYTLFSISEN TVPHELFTPL LIGFVAAAVI LILILIVLSY
     KYMQKPKYQI QWKVIEGIHG NSYVYIDPTQ LPYDHQWEFP RDKLRFGKIL GSGAFGKVVE
     ATAYGMSKAD TVMTVAVKML KPSAHATEKE ALMSELKVLS YLGNHINIVN LLGACTIGGP
     TLVITEYCCF GDLLNFLRRR RESFYFTTLG EDSYYRNVML QPEPNESRHE YMTMKPSILG
     LLSSENRRSL NKGDSYRDSD AVSEIMQEDG MTLDTEDLLS FSYQVAKGMD FLASKNCIHR
     DLAARNILLT QGRVAKICDF GLARDITTDS NYVVKGNARL PVKWMSPESI FECVYTFESD
     VWSYGILLWE IFSLGSSPYP GMPVDSNFYK MIKEGYRMES PEFAPSEMYE IMHSCWDADP
     FKRPSFGKIV EKIEQQISDS TKHIYLNFSS RLPAAPGSHE ESGSHVQRLN SFGSHITATQ
     PLLSSNDVFL EGTSPRHPPV
//
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