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Database: UniProt
Entry: Q5D4S1_HORSE
LinkDB: Q5D4S1_HORSE
Original site: Q5D4S1_HORSE 
ID   Q5D4S1_HORSE            Unreviewed;       898 AA.
AC   Q5D4S1;
DT   29-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   29-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 119.
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};
DE   Flags: Fragment;
GN   Name=KIT {ECO:0000313|EMBL:AAX13762.1};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796 {ECO:0000313|EMBL:AAX13762.1};
RN   [1] {ECO:0000313|EMBL:AAX13762.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16284805; DOI=10.1007/s00335-005-2472-y;
RA   Brooks S.A., Bailey E.;
RT   "Exon skipping in the KIT gene causes a Sabino spotting pattern in
RT   horses.";
RL   Mamm. Genome 16:893-902(2005).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   EMBL; AY910688; AAX13762.1; -; mRNA.
DR   AlphaFoldDB; Q5D4S1; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019955; F:cytokine binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro.
DR   GO; GO:0038093; P:Fc receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0038109; P:Kit signaling pathway; IEA:InterPro.
DR   CDD; cd00096; Ig; 1.
DR   CDD; cd05860; IgI_4_SCFR; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 5.
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.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR027263; SCGF_receptor.
DR   InterPro; IPR001245; Ser-Thr/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; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF500951; SCGF_recepter; 2.
DR   PIRSF; PIRSF000615; TyrPK_CSF1-R; 2.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 4.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50835; IG_LIKE; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR500951-
KW   2}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR000615-3};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000615-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR500951-2, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000313|EMBL:AAX13762.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..898
FT                   /note="Mast/stem cell growth factor receptor Kit"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004254496"
FT   TRANSMEM        521..544
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          37..98
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          212..308
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          585..892
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         564
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         592..599
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500951-2"
FT   BINDING         619
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500951-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         667..673
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500951-2"
FT   SITE            891
FT                   /note="Important for interaction with phosphotyrosine-
FT                   binding proteins"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500951-3"
FT   NON_TER         898
FT                   /evidence="ECO:0000313|EMBL:AAX13762.1"
SQ   SEQUENCE   898 AA;  100837 MW;  8FDCAB465336B652 CRC64;
     MRGARGAWDF LCVLLLLFRV QTGSSQPSVS PGELSPPSIH PAKSELIVSV GDEIRLLCAD
     PGFVKWTFET WGQLSENTHK EWVTEKAEAT NTGSYTCTNE GGLSSSIYVF VRDPAKLFLF
     DPSLYGKEGS DTLVRCPLTD PEVTNYSLMA CEGKSLPKDL TFVADPKAGI TIRNVKREYH
     RLCLRCSADK DGKSVLSNKF TLKVRAAIRA VPVVSVSKAS YLLREGEEFS VTCLIKDVSS
     SVDSMWIREN SRTKEQVKSS SSHQGDFNFV RQERLTISPA RVNDSGVFMC YANNTFGSAN
     VTTTLEVVDK GFINVFPMMN TTVFVNDGEN VDLIVEYESY PKPEHQQWIY MNRTSTDKWE
     DYPKSENESN IRYVSELHLT RLKGTEGGTY TFLVSNSDVD SSVTFNVYVN TKPEILTRDR
     LMNGMLQCVA AGFPEPTIDW YFCPGTEQRC SIPVGPVDVK IQNSSVSPFG KLVVQSSIDY
     SAFKHNGTVE CRAYNDVGKS SAFFNFAFKE QIHPHTLFTP LLIGFVAAAG MMCVIVMVLT
     YKYLQKPMYE VQWKVVEEIN GNNYVYIDPT QLPYDHKWEF PRNRLSFGKT LGAGAFGKVV
     EATAYGLIKS DAAMTVAVKM LKPSAHLTER EALMSELKVL SYLGNHMNIV NLLGACTVGG
     PTLVITEYCC YGDLLNFLRR KRDSFICSKQ EDHAEAALYK NLLHSKESSC NDSTNEYMDM
     KPGVSYVVPT KTDKRRAARI GSYIERDVAP SIMEDDELAL DLEDLLSFSY QVAKGMAFLA
     SKNARLPVKW MAPESIFNCV YTFESDVWSY GIFLWELFSL GSSPYPGMPV DSKFYKMIKE
     GFRMLSPEHA PAEMYDIMKT CWDADPLKRP TFKQIVQLIE KQISDSTNHI YSNLANCS
//
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