Mast/stem cell growth factor receptor (EC 2.7.10.1)

 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

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