ID A0A8C5DY96_GOUWI Unreviewed; 834 AA.
AC A0A8C5DY96;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
DE AltName: Full=Tyrosine-protein kinase Kit {ECO:0000256|ARBA:ARBA00032147};
GN Name=kita {ECO:0000313|Ensembl:ENSGWIP00000013692.1};
OS Gouania willdenowi (Blunt-snouted clingfish) (Lepadogaster willdenowi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Blenniimorphae; Blenniiformes; Gobiesocoidei; Gobiesocidae;
OC Gobiesocinae; Gouania.
OX NCBI_TaxID=441366 {ECO:0000313|Ensembl:ENSGWIP00000013692.1, ECO:0000313|Proteomes:UP000694680};
RN [1] {ECO:0000313|Ensembl:ENSGWIP00000013692.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Wellcome Sanger Institute Data Sharing;
RL Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGWIP00000013692.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSGWIP00000013692.1}
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}.
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DR AlphaFoldDB; A0A8C5DY96; -.
DR Ensembl; ENSGWIT00000015172.1; ENSGWIP00000013692.1; ENSGWIG00000007650.1.
DR Proteomes; UP000694680; Chromosome 4.
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: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 CDD; cd00096; Ig; 2.
DR FunFam; 1.10.510.10:FF:000177; Mast/stem cell growth factor receptor; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
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; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
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 PANTHER; PTHR24416:SF46; MAST_STEM CELL GROWTH FACTOR RECEPTOR KIT; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF07679; I-set; 2.
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; 2.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
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 Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {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};
KW Reference proteome {ECO:0000313|Proteomes:UP000694680};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT TRANSMEM 380..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 90..187
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 448..781
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 645
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 427
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 455..462
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 482
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 527..533
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 649
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 650
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 663
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
SQ SEQUENCE 834 AA; 94014 MW; D50A0A5E9081ADBF CRC64;
MVYNILSREG NSASIPCLAT DPSLDNLSLK TCSGKALAPG LEYTASLEQG IVISNAQQAY
EGCYVCTGKL MKQPVRSHDY YLTVKPAIAP PLIEMEQSGR MILIRDESLS LSCNTTNVNG
LISLKWVTPP GSQPAKVDSA SHILMESFAH LRSATLQISA VQPQDAGSYK CEARNEKGTS
TKSVWLDIYE RGFISLSSTN NETIHVRTGE TLSLKVTYDA YPRPHISWSY MGQELKNTVN
HVITTLRNEY SLKLLLQHDV YILSNMFTFC LSGKPEIVSH EGPVDGQVRC VAEGFPAPEI
TWYYCEQPYV RCSQQVNATQ EEQNVITITL FSPLFGKTEV ESRVNISRGR FNTLECVASV
EGEQAYTLFS ISERRVPHDL FTPLLIGSVS AACILCLVLI MLFYKYMQKP KYQIQWKVIE
GIHGNSYVYI DPSQLPYDHQ WEFPRNNLRF GKTLGSGAFG KVVEATAYGL SEADSVMTVA
VKMLKSSAHA TEKEALMSEL KVLSIHVVNL LLTCVYFSSG PTLVITEYCC FGDLLNFLRR
KRDSFIYSQI KEDYYYRNVM QQRVTESLND YMTMKPSVAG NPPFRTFSRK RSSLNKGDTY
VDVDAGSEMF DEDGLSLETE DLLSFSYQVA KGMEFLASKN CIHRDLAARN ILLTEGRVAK
ICDFGLARDI TTDSNYVVKG NARLPVKWMS TESIFECVYT FESDVWSYGI LLWEIFSLGN
SPYPGVPVDA KFYKLIKEGY RMDAPDFAPC EMYRIMRSCW NADPFARPSF KKVVERFEQE
LSDTTKHRCS FEPPSLPFLS RQHLTSHRRR MTCSPLISKM SHSSIMACTI GVCL
//
