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F1PUW9_CANLF Unreviewed; 963 AA.
F1PUW9;
03-MAY-2011, integrated into UniProtKB/TrEMBL.
31-OCT-2012, sequence version 2.
16-OCT-2019, entry version 67.
RecName: Full=Mast/stem cell growth factor receptor {ECO:0000256|PIRNR:PIRNR500951};
EC=2.7.10.1 {ECO:0000256|PIRNR:PIRNR500951};
Name=KIT {ECO:0000313|Ensembl:ENSCAFP00000003042,
ECO:0000313|VGNC:VGNC:42422};
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000003042, ECO:0000313|Proteomes:UP000002254};
[1] {ECO:0000313|Ensembl:ENSCAFP00000003042, ECO:0000313|Proteomes:UP000002254}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000003042,
ECO:0000313|Proteomes:UP000002254};
PubMed=16341006; DOI=10.1038/nature04338;
Broad Sequencing Platform;
Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C.,
Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A.,
Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F.,
Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A.,
Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M.,
Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L.,
Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J.,
Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L.,
Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A.,
Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L.,
Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N.,
Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A.,
Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N.,
Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N.,
Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K.,
Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G.,
Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E.,
Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C.,
Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L.,
Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C.,
Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T.,
Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J.,
Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J.,
Marabella R., Maru K., Matthews C., McDonough S., Mehta T.,
Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K.,
Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J.,
Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K.,
Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F.,
Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C.,
Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S.,
Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J.,
Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S.,
Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S.,
Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T.,
Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T.,
Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X.,
Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.;
"Genome sequence, comparative analysis and haplotype structure of the
domestic dog.";
Nature 438:803-819(2005).
[2] {ECO:0000313|Ensembl:ENSCAFP00000003042}
IDENTIFICATION.
STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000003042};
Ensembl;
Submitted (JUL-2011) to UniProtKB.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-
tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136,
Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216;
EC=2.7.10.1; Evidence={ECO:0000256|PIRNR:PIRNR500951,
ECO:0000256|SAAS:SAAS01168082};
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU000311};
Single-pass type I membrane protein
{ECO:0000256|RuleBase:RU000311}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. CSF-1/PDGF receptor subfamily.
{ECO:0000256|PIRNR:PIRNR500951, ECO:0000256|RuleBase:RU000311}.
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EMBL; AAEX03009077; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AAEX03009078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
SMR; F1PUW9; -.
Ensembl; ENSCAFT00000003274; ENSCAFP00000003042; ENSCAFG00000002065.
VGNC; VGNC:42422; KIT.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00940000155626; -.
Proteomes; UP000002254; Chromosome 13.
Bgee; ENSCAFG00000002065; Expressed in 3 organ(s), highest expression level in prefrontal cortex.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
GO; GO:0042629; C:mast cell granule; IEA:GOC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0019955; F:cytokine binding; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0042169; F:SH2 domain binding; IEA:Ensembl.
GO; GO:0005020; F:stem cell factor receptor activity; IEA:Ensembl.
GO; GO:0031532; P:actin cytoskeleton reorganization; IEA:Ensembl.
GO; GO:0000187; P:activation of MAPK activity; IEA:Ensembl.
GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEA:Ensembl.
GO; GO:0002371; P:dendritic cell cytokine production; IEA:Ensembl.
GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IEA:Ensembl.
GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl.
GO; GO:0035162; P:embryonic hemopoiesis; IEA:Ensembl.
GO; GO:0030218; P:erythrocyte differentiation; IEA:Ensembl.
GO; GO:0038162; P:erythropoietin-mediated signaling pathway; IEA:Ensembl.
GO; GO:0038093; P:Fc receptor signaling pathway; IEA:UniProtKB-UniRule.
GO; GO:0006687; P:glycosphingolipid metabolic process; IEA:Ensembl.
GO; GO:0035701; P:hematopoietic stem cell migration; IEA:Ensembl.
GO; GO:0002327; P:immature B cell differentiation; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
GO; GO:0030032; P:lamellipodium assembly; IEA:Ensembl.
GO; GO:0002320; P:lymphoid progenitor cell differentiation; IEA:Ensembl.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0002551; P:mast cell chemotaxis; IEA:Ensembl.
GO; GO:0032762; P:mast cell cytokine production; IEA:Ensembl.
GO; GO:0043303; P:mast cell degranulation; IEA:Ensembl.
GO; GO:0060374; P:mast cell differentiation; IEA:Ensembl.
GO; GO:0035855; P:megakaryocyte development; IEA:Ensembl.
GO; GO:0097326; P:melanocyte adhesion; IEA:Ensembl.
GO; GO:0030318; P:melanocyte differentiation; IEA:Ensembl.
GO; GO:0097324; P:melanocyte migration; IEA:Ensembl.
GO; GO:0002318; P:myeloid progenitor cell differentiation; IEA:Ensembl.
GO; GO:0043069; P:negative regulation of programmed cell death; IEA:Ensembl.
GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
GO; GO:1905065; P:positive regulation of vascular smooth muscle cell differentiation; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
GO; GO:0009314; P:response to radiation; IEA:Ensembl.
GO; GO:0007286; P:spermatid development; IEA:Ensembl.
GO; GO:0048863; P:stem cell differentiation; IEA:Ensembl.
GO; GO:0030217; P:T cell differentiation; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 5.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013151; Immunoglobulin.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR027263; SCGF_receptor.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
Pfam; PF00047; ig; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PIRSF; PIRSF500951; SCGF_recepter; 1.
SMART; SM00409; IG; 4.
SMART; SM00408; IGc2; 2.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 4.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50835; IG_LIKE; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|PIRNR:PIRNR500951,
ECO:0000256|PIRSR:PIRSR500951-2, ECO:0000256|SAAS:SAAS00600564};
Cell membrane {ECO:0000256|PIRNR:PIRNR500951};
Complete proteome {ECO:0000313|Proteomes:UP000002254};
Disulfide bond {ECO:0000256|SAAS:SAAS00916669};
Immunoglobulin domain {ECO:0000256|RuleBase:RU000311,
ECO:0000256|SAAS:SAAS00290237};
Kinase {ECO:0000256|PIRNR:PIRNR500951, ECO:0000256|SAAS:SAAS00582553};
Magnesium {ECO:0000256|PIRNR:PIRNR500951,
ECO:0000256|PIRSR:PIRSR500951-1};
Membrane {ECO:0000256|PIRNR:PIRNR500951,
ECO:0000256|SAAS:SAAS00602683};
Metal-binding {ECO:0000256|PIRNR:PIRNR500951,
ECO:0000256|PIRSR:PIRSR500951-1};
Nucleotide-binding {ECO:0000256|PIRNR:PIRNR500951,
ECO:0000256|PIRSR:PIRSR500951-2, ECO:0000256|SAAS:SAAS00600564};
Receptor {ECO:0000256|PIRNR:PIRNR500951,
ECO:0000256|RuleBase:RU000311, ECO:0000256|SAAS:SAAS00600436};
Reference proteome {ECO:0000313|Proteomes:UP000002254};
Repeat {ECO:0000256|SAAS:SAAS00295312};
Signal {ECO:0000256|SAM:SignalP};
Transferase {ECO:0000256|PIRNR:PIRNR500951,
ECO:0000256|SAAS:SAAS00582553};
Transmembrane {ECO:0000256|PIRNR:PIRNR500951,
ECO:0000256|SAAS:SAAS00602683};
Transmembrane helix {ECO:0000256|PIRNR:PIRNR500951,
ECO:0000256|SAAS:SAAS00602683};
Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR500951,
ECO:0000256|SAAS:SAAS00582553}.
SIGNAL 1 15 {ECO:0000256|SAM:SignalP}.
CHAIN 16 963 Mast/stem cell growth factor receptor.
{ECO:0000256|SAM:SignalP}.
/FTId=PRO_5013311319.
TRANSMEM 512 535 Helical. {ECO:0000256|PIRNR:PIRNR500951}.
DOMAIN 202 299 Ig-like. {ECO:0000259|PROSITE:PS50835}.
DOMAIN 404 498 Ig-like. {ECO:0000259|PROSITE:PS50835}.
DOMAIN 576 924 Protein kinase.
{ECO:0000259|PROSITE:PS50011}.
NP_BIND 583 590 ATP. {ECO:0000256|PIRSR:PIRSR500951-2}.
NP_BIND 658 664 ATP. {ECO:0000256|PIRSR:PIRSR500951-2}.
METAL 555 555 Magnesium.
{ECO:0000256|PIRSR:PIRSR500951-1}.
METAL 784 784 Magnesium.
{ECO:0000256|PIRSR:PIRSR500951-1}.
METAL 797 797 Magnesium.
{ECO:0000256|PIRSR:PIRSR500951-1}.
BINDING 610 610 ATP. {ECO:0000256|PIRSR:PIRSR500951-2}.
BINDING 783 783 ATP. {ECO:0000256|PIRSR:PIRSR500951-2}.
SITE 923 923 Important for interaction with
phosphotyrosine-binding proteins.
{ECO:0000256|PIRSR:PIRSR500951-3}.
SEQUENCE 963 AA; 108118 MW; 2166A161AD7FC403 CRC64;
VLFLLFLSRV SACSSQPSVS PGEPSLPSIH PAKSELIVSV GDELRLSCTD PGFVKWTFET
LGQLNENTHN EWITEKAEAG HTGNYTCTNR DGLSRSIYVF VRDPAKLFLV DLPLYGKEGN
DTLVRCPLTD PEVTNYSLRG CEGKPLPKDL TFVADPKAGI TIRNVKREYH RLCLHCSADQ
KGRTVLSKKF TLKVRAAIRA VPVVSVSKTS SLLKEGEAFS VMCFIKDVSS FVDSMWIKEN
SQQTNAQTQS NSWHHGDFNF ERQEKLIISS ARVNDSGVFM CYANNTFGSA NVTTTLEVVD
KGFINIFPMM STTIFVNDGE NVDLIVEYEA YPKPEHQQWI YMNRTFTDKW EDYPKSDNES
NIRYVSELHL TRLKGNEGGT YTFQVSNSDV NSSVTFNVYV NTKPEILTHE SLTNGMLQCV
VAGFPEPAVD WYFCPGAEQR CSVPIGPMDV QMQNSSLSPS GKLVVQSSID YSAFKHNGTV
ECRAYNNVGR SSAFFNFAFK EQIHPHTLFT PLLIGFVIAA GMMCIIVMIL TYKYLQKPMY
EVQWKVVEEI NGNNYVYIDP TQLPYDHKWE FPRNRLSFGK TLGAGAFGKV VEATAYGLIK
SDAAMTVAVK MLKPSAHLTE REALMSELKV LSYLGNHMNI VNLLGACTVG GPTLVITEYC
CYGDLLNFLR RKRDSFICSK QEDHGEVALY KNLLHSKESS CSDSTNEYMD MKPGVSYVVP
TKADKRRSAR IGSYIERDVT PAIMEDDELA LDLEDLLSFS YQVAKGMAFL ASKNCIHRDL
AARNILLTHG RITKICDFGL ARDIKNDSNY VVKGNARLPV KWMAPESIFN CVYTFESDVW
SYGIFLWELF SLGSSPYPGM PVDSKFYKMI KEGFRMLSPE HAPAEMYDIM KTCWDADPLK
RPTFKQIVQL IEKQISDSTN HIYSNLANCS PNPERPVVDH SVRINSVGSS ASSTQPLLVH
EDV