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Database: UniProt
Entry: A0A7F8RWX8_LEPWE
LinkDB: A0A7F8RWX8_LEPWE
Original site: A0A7F8RWX8_LEPWE 
ID   A0A7F8RWX8_LEPWE        Unreviewed;       768 AA.
AC   A0A7F8RWX8;
DT   10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2021, sequence version 1.
DT   28-JAN-2026, entry version 25.
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=KIT {ECO:0000313|RefSeq:XP_030897761.1};
OS   Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC   Monachinae; Lobodontini; Leptonychotes.
OX   NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_030897761.1};
RN   [1] {ECO:0000313|RefSeq:XP_030897761.1}
RP   IDENTIFICATION.
RC   TISSUE=Liver {ECO:0000313|RefSeq:XP_030897761.1};
RG   RefSeq;
RL   Submitted (AUG-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}.
CC       Membrane {ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane
CC       protein {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|RuleBase:RU000311}.
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DR   RefSeq; XP_030897761.1; XM_031041901.1.
DR   AlphaFoldDB; A0A7F8RWX8; -.
DR   GeneID; 102726034; -.
DR   KEGG; lww:102726034; -.
DR   CTD; 3815; -.
DR   OrthoDB; 6077854at2759; -.
DR   Proteomes; UP000245341; Unplaced.
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:0048513; P:animal organ development; IEA:UniProtKB-ARBA.
DR   GO; GO:0030183; P:B cell differentiation; IEA:TreeGrafter.
DR   GO; GO:0008283; P:cell population proliferation; IEA:UniProtKB-ARBA.
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   GO; GO:0042127; P:regulation of cell population proliferation; IEA:UniProtKB-ARBA.
DR   GO; GO:0050793; P:regulation of developmental process; IEA:UniProtKB-ARBA.
DR   CDD; cd00096; Ig; 1.
DR   CDD; cd05104; PTKc_Kit; 1.
DR   FunFam; 1.10.510.10:FF:000177; Mast/stem cell growth factor receptor; 1.
DR   FunFam; 2.60.40.10:FF:000422; Mast/stem cell growth factor receptor; 1.
DR   FunFam; 2.60.40.10:FF:000544; Mast/stem cell growth factor receptor; 1.
DR   FunFam; 2.60.40.10:FF:000815; Mast/stem cell growth factor receptor; 1.
DR   FunFam; 3.30.200.20:FF:000025; Platelet-derived growth factor receptor alpha; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
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; 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   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; 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; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
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.
DR   PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR500951-
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   ECO:0000256|RuleBase:RU000311}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR500951-1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR500951-1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR500951-2};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000311};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245341};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000311};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..768
FT                   /note="receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5028939469"
FT   TRANSMEM        317..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          209..303
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          381..729
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         360
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500951-1"
FT   BINDING         388..395
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500951-2"
FT   BINDING         415
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500951-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         463..469
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500951-2"
FT   BINDING         588
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500951-2"
FT   BINDING         589
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500951-1"
FT   BINDING         602
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500951-1"
FT   SITE            728
FT                   /note="Important for interaction with phosphotyrosine-
FT                   binding proteins"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500951-3"
SQ   SEQUENCE   768 AA;  86195 MW;  71E348BFF313EC80 CRC64;
     MRGARGAWDF LCVLLILFRV QTGSSQPSVS PGELSLPSIH PAKSELIVSV GDEIRLLCTD
     PGFVKWTFET PGQLSENTRN EWITEKAEAA NTGNYTCTNR DGLSRSIYVF VRDPAQLFLI
     DLRLYGKEDN DTLVRCPLTD PEVTNYSLRG CEGKPLPKDL TFVTDPKAGI TIRHVKREYH
     RLCLHCSADQ KGKSVLSTKF TLKVRAAKPE ILTHESLVNG MLQCVVAGFP EPTVDWYFCP
     GTEQRCSIPV GPMDVQMQNS SVSPSGKLVV QSSIDYSAFK HNGTVECRAY NNVGRSSAFF
     NFAFKEQIHP HTLFTPLLIG FVIAAGMMCI IVMILTYKYL QKPMYEVQWK VVEEINGNNY
     VYIDPTQLPY DHKWEFPRNR LSFGKTLGAG AFGKVVEATA YGLIKSDAAM TVAVKMLKPS
     AHLTEREALM SELKVLSYLG NHMNIVNLLG ACTVGGPTLV ITEYCCYGDL LNFLRRKRDS
     FICSKQEDHA EVALYKNLLH SKESSCNDSA NEYMDMKPGV SYVVPTKADK RRSARIGSYI
     ERDVTPAIME DDELALDLED LLSFSYQVAK GMAFLASKNC IHRDLAARNI LLTHGRITKI
     CDFGLARDIK NDSNYVVKGN ARLPVKWMAP ESIFNCVYTF ESDVWSYGIF LWELFSLGSS
     PYPGMPVDSK FYKMIKEGFR MLSPEHAPAE MYDIMKTCWD ADPLKRPTFK QIVQLIEKQI
     SDSTNHIYSN LVNCSPHQER PVVDHSVRIN SVGSSASSTQ PLLVHEDV
//
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