UniProt: A0A672QGI2

Database: UniProt
Entry: A0A672QGI2_SINGR

LinkDB:  A0A672QGI2_SINGR 
Original site:  A0A672QGI2_SINGR

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Ontology (14)   
   GO (14)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (28)   
   InterPro (15)   
   Pfam (5)   
   PROSITE (5)   
   SMART (3)   
All databases (46)   

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ID   A0A672QGI2_SINGR        Unreviewed;       784 AA.
AC   A0A672QGI2;
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 Kit {ECO:0000256|ARBA:ARBA00014417};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
DE   AltName: Full=Proto-oncogene c-Kit {ECO:0000256|ARBA:ARBA00032530};
DE   AltName: Full=Tyrosine-protein kinase Kit {ECO:0000256|ARBA:ARBA00032147};
GN   Name=LOC107597437 {ECO:0000313|Ensembl:ENSSGRP00000075056.1};
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:ENSSGRP00000075056.1, ECO:0000313|Proteomes:UP000472262};
RN   [1] {ECO:0000313|Ensembl:ENSSGRP00000075056.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSSGRP00000075056.1}
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   -!- 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|RuleBase:RU000311}.
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DR   AlphaFoldDB; A0A672QGI2; -.
DR   Ensembl; ENSSGRT00000079904.1; ENSSGRP00000075056.1; ENSSGRG00000038098.1.
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:InterPro.
DR   GO; GO:0019838; F:growth factor binding; IEA:TreeGrafter.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0001667; P:ameboidal-type cell migration; IEA:UniProtKB-ARBA.
DR   GO; GO:0030183; P:B cell differentiation; IEA:TreeGrafter.
DR   GO; GO:0038093; P:Fc receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:TreeGrafter.
DR   GO; GO:0038109; P:Kit signaling pathway; IEA:InterPro.
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   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   PRINTS; PR01832; VEGFRECEPTOR.
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|PIRSR:PIRSR000615-
KW   2}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR000615-3};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000615-3};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR000615-2};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000311};
KW   Reference proteome {ECO:0000313|Proteomes:UP000472262};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000311};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          8..85
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          189..285
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          383..488
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          545..784
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        740
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT   BINDING         524
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         552..559
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         579
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         627..633
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         744
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         745
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         758
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
SQ   SEQUENCE   784 AA;  87288 MW;  674013B9FA8C7DDD CRC64;
     MTVCVSRPTI IPEGPQVTVP LNSDFSLRCQ SDSSVRWLRE DRPTRILKAQ RQGQVTVLKV
     NKAGPQHMGK YSCREEASGE KSSIYVYVKD PENPFRRNIM FDFVAGEGET ATIPCLATDP
     HMTDLHLQKC DGQSLPNSLR YSSSIETGIT LEDVRKDFKG CYVCVGTLEG NTVKSGQYQL
     NVRLVPDMPP VITLGQPPRV LLIQGEELSL SCNTSNVNSD ITVRWKAPQG VQPSVQRFSS
     ILTEPISHLR NATLNLGSVT MQDAGIYNCE ARNERGTSAK AVLVEIYEKS FINLTSVNNC
     TKRVRAGESL SLRVVMDAYP KPHPFSWSYS GVKLTNTTDH VITSHSHGNR YTSELKLVRL
     KVLESGVYTF SCSNRDATVH QMFEVHVISK PQIVSHEGPI DGQVRCVAEG YPTPQIKWYY
     CDQPHSRCSN LLNATQEEED VVTVTMTNPP FGKGTVESRL NITKNSYSTL ECVASANGEI
     VYTLFSISGE AHTLAVTGSN VKGCFKPKYQ IQWKVIEGIH GNSYVYIDPT QLPYDHLWEF
     PRDKLRFGKT LGSGAFGKVV EATAYGMSKA DTVMTVAVKM LKPSAHATEK EALMSELKVL
     SYLGNHINIV NLLGACTIGG PTLVITEYCC FGDLLNFLRR RRESFYYTTL GEDSYYRNFV
     FDYSESRNGY VTMKPSVMGI LSSENRRSLN KGDSYNDSDA VSEILHEDGM TLDTEDLLSF
     SYQVAKGMDF LASKNCIHRD LAARNILLTQ GRVAKICDFG LARDITTDSN YVVKGNVSIN
     CHYM
//

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