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Database: UniProt
Entry: A0A2D0Q235_ICTPU
LinkDB: A0A2D0Q235_ICTPU
Original site: A0A2D0Q235_ICTPU 
ID   A0A2D0Q235_ICTPU        Unreviewed;       981 AA.
AC   A0A2D0Q235;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   05-JUN-2019, entry version 12.
DE   RecName: Full=Mast/stem cell growth factor receptor {ECO:0000256|PIRNR:PIRNR500951};
DE            EC=2.7.10.1 {ECO:0000256|PIRNR:PIRNR500951};
GN   Name=kit {ECO:0000313|RefSeq:XP_017311746.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|Proteomes:UP000221080, ECO:0000313|RefSeq:XP_017311746.1};
RN   [1] {ECO:0000313|RefSeq:XP_017311746.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017311746.1};
RG   RefSeq;
RL   Submitted (NOV-2017) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-
CC         tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136,
CC         Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216;
CC         EC=2.7.10.1; Evidence={ECO:0000256|PIRNR:PIRNR500951,
CC         ECO:0000256|SAAS:SAAS01168082};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU000311};
CC       Single-pass type I membrane protein
CC       {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|PIRNR:PIRNR500951, ECO:0000256|RuleBase:RU000311}.
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DR   RefSeq; XP_017311746.1; XM_017456257.1.
DR   GeneID; 108258027; -.
DR   KEGG; ipu:108258027; -.
DR   CTD; 3815; -.
DR   KO; K05091; -.
DR   OrthoDB; 236292at2759; -.
DR   Proteomes; UP000221080; Genome assembly.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019955; F:cytokine binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0038093; P:Fc receptor signaling pathway; IEA:UniProtKB-UniRule.
DR   GO; GO:0038109; P:Kit signaling pathway; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 5.
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; 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; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   PIRSF; PIRSF500951; SCGF_recepter; 1.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 3.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; SSF48726; 4.
DR   SUPFAM; SSF56112; SSF56112; 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|PIRNR:PIRNR500951,
KW   ECO:0000256|PIRSR:PIRSR500951-2, ECO:0000256|SAAS:SAAS00600564};
KW   Cell membrane {ECO:0000256|PIRNR:PIRNR500951};
KW   Complete proteome {ECO:0000313|Proteomes:UP000221080};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00916669};
KW   Immunoglobulin domain {ECO:0000256|RuleBase:RU000311,
KW   ECO:0000256|SAAS:SAAS00941986};
KW   Kinase {ECO:0000256|PIRNR:PIRNR500951, ECO:0000256|SAAS:SAAS00601152};
KW   Magnesium {ECO:0000256|PIRNR:PIRNR500951,
KW   ECO:0000256|PIRSR:PIRSR500951-1};
KW   Membrane {ECO:0000256|PIRNR:PIRNR500951,
KW   ECO:0000256|SAAS:SAAS00602125};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR500951,
KW   ECO:0000256|PIRSR:PIRSR500951-1};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR500951,
KW   ECO:0000256|PIRSR:PIRSR500951-2, ECO:0000256|SAAS:SAAS00600689};
KW   Receptor {ECO:0000256|PIRNR:PIRNR500951,
KW   ECO:0000256|RuleBase:RU000311, ECO:0000256|SAAS:SAAS00600436,
KW   ECO:0000313|RefSeq:XP_017311746.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000221080};
KW   Repeat {ECO:0000256|SAAS:SAAS00295312};
KW   Signal {ECO:0000256|PIRNR:PIRNR500951};
KW   Transferase {ECO:0000256|PIRNR:PIRNR500951,
KW   ECO:0000256|SAAS:SAAS00601608};
KW   Transmembrane {ECO:0000256|PIRNR:PIRNR500951,
KW   ECO:0000256|RuleBase:RU000311, ECO:0000256|SAAS:SAAS00600943};
KW   Transmembrane helix {ECO:0000256|PIRNR:PIRNR500951,
KW   ECO:0000256|SAAS:SAAS00602683};
KW   Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR500951,
KW   ECO:0000256|SAAS:SAAS00582553}.
FT   SIGNAL        1     21       {ECO:0000256|PIRNR:PIRNR500951}.
FT   CHAIN        22    981       Mast/stem cell growth factor receptor.
FT                                {ECO:0000256|PIRNR:PIRNR500951}.
FT                                /FTId=PRO_5011836229.
FT   TRANSMEM    517    541       Helical. {ECO:0000256|PIRNR:PIRNR500951}.
FT   DOMAIN        9    105       Ig-like. {ECO:0000259|PROSITE:PS50835}.
FT   DOMAIN      211    306       Ig-like. {ECO:0000259|PROSITE:PS50835}.
FT   DOMAIN      418    509       Ig-like. {ECO:0000259|PROSITE:PS50835}.
FT   DOMAIN      585    927       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
FT   NP_BIND     592    599       ATP. {ECO:0000256|PIRSR:PIRSR500951-2}.
FT   NP_BIND     667    673       ATP. {ECO:0000256|PIRSR:PIRSR500951-2}.
FT   REGION      944    981       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A2D0Q235}.
FT   COMPBIAS    948    965       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A2D0Q235}.
FT   METAL       564    564       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR500951-1}.
FT   METAL       787    787       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR500951-1}.
FT   METAL       800    800       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR500951-1}.
FT   BINDING     619    619       ATP. {ECO:0000256|PIRSR:PIRSR500951-2}.
FT   BINDING     786    786       ATP. {ECO:0000256|PIRSR:PIRSR500951-2}.
FT   SITE        926    926       Important for interaction with
FT                                phosphotyrosine-binding proteins.
FT                                {ECO:0000256|PIRSR:PIRSR500951-3}.
SQ   SEQUENCE   981 AA;  110320 MW;  D6BB83F5CAD55EAC CRC64;
     MEYHWVLFPV VLQFLFRPGS TKPVISPDGS QIAVQLNGNL VLRCHGDSPV RWFREERPSR
     ILRDEQRDHQ LSTINMTKAK PQDQGKYICM EESSGEKSSI YVYVTAFLLA DPVNAFRKSM
     IPDIMAGAGD IATIPCLATD PRMVDLHLET CDGQQLPTGM RYSASTETGI SMLNVQPTYK
     GCYVCVGFLK EKMARSMEYK LNVRLVPDAP PRISLQEHNR VLLTQGQRLT LSCSTSNVNS
     EIKINWLPPH GVKASVQQSS QLFTEPVLHK RTATLQIEAV TTQDSGSYYC NAENYRGTST
     ERVWVDVYSK GFMNLTHVDN RTWRVREGES LSLRVDMEAY PKPHVFSWSY NRKNLTNTTD
     HVITTHSQAH SYQSQLKLVR LKVSESGVYT FLASNGDASI HLTFEVHVLS KPAIVSHEGP
     VDGQVRCVAE GYPPPQITWY YCDQPHARCS NLLNATQEEE DVVTVTMTNP PFGKGAVESR
     LNITKNNYPT LECVASAEGE IVYTLFSISE RTVPHELFTP LLIGFTAAAA ILCLILFVLI
     YKYIQKPKYQ IQWKVIEGIH GNNYVYIDPT QLPYDHQWEF PRDRLRFGKT LGSGAFGKVV
     EATAYGMSKA DTVMTVAVKM LKPSAHATEK EALMSELKVL SYLGNHINIV NLLGACTVGG
     PTLVITEYCC FGDLLNFLRR KRDCFCCSRL GDDTYYRNVL LHPDSGDGRN GYMTMRPLVL
     GVQSTEKRSL PKGVGSNTDS DVFSEVLQED GLALDTEDLL SFSYQVAKGM DFLASKNCIH
     RDLAARNILL TQGRVAKICD FGLARDITTD SNYVVKGNAR LPVKWMSPES IFECVYTFES
     DVWSYGILLW EIFSLGSSPY PGIPVDAKFY KMIKEGYRME SPEFAPSEMY EIMQSCWDAD
     PSRRPSFGKI VEKVEQQISD STKHIYLNFS SRLPVVTALR EEPFSHSSRR NSGSGHITPT
     QPLLSSDDVF LEEEAPRQPR A
//
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