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Database: UniProt
Entry: A0A8D0BD67_SALMN
LinkDB: A0A8D0BD67_SALMN
Original site: A0A8D0BD67_SALMN 
ID   A0A8D0BD67_SALMN        Unreviewed;       876 AA.
AC   A0A8D0BD67;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 21.
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};
OS   Salvator merianae (Argentine black and white tegu) (Tupinambis merianae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Laterata;
OC   Teiioidea; Teiidae; Salvator.
OX   NCBI_TaxID=96440 {ECO:0000313|Ensembl:ENSSMRP00000006365.1, ECO:0000313|Proteomes:UP000694421};
RN   [1] {ECO:0000313|Ensembl:ENSSMRP00000006365.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSSMRP00000006365.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A8D0BD67; -.
DR   Ensembl; ENSSMRT00000007463.1; ENSSMRP00000006365.1; ENSSMRG00000005119.1.
DR   GeneTree; ENSGT00940000155626; -.
DR   Proteomes; UP000694421; 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:0030183; P:B cell differentiation; IEA:TreeGrafter.
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   CDD; cd00096; Ig; 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:000469; 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; 4.
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; 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; 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; PF13927; Ig_3; 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; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 2.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 3.
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:PIRSR000615-
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|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|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR000615-2};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000311};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694421};
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};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..876
FT                   /note="receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5034683722"
FT   TRANSMEM        430..453
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          120..209
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          494..838
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        693
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT   BINDING         473
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         501..508
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         528
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         576..582
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         697
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         698
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         711
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   SITE            837
FT                   /note="Important for interaction with phosphotyrosine-
FT                   binding proteins"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
SQ   SEQUENCE   876 AA;  98374 MW;  1389E506D609C754 CRC64;
     MKGAWAFGAV ALLALVLFKP TDPSILFFHE SLTYVTEDDD ALIQCPVTDP DVSNFTLRRC
     NGKPLPEDMV LVPDPQKGIT IKNVQRSFRG CYLCVAQQNG VEKKSDTISL IVWAVHKSLP
     VITLSKANQL LKRGEEFEVT CTIRDVDSTL QANWIFQGNA NVTRKSKNMG DYEYEQKLTL
     SIRSVGVNDS GVFMCQGRNP FGTSNATITL KVLGKGYVNL LSSTNTTVTV NDGENLDLIV
     TYETYPKPEE EIWMYMNETL QNSSDHFVRI TNIDKNRYSS ELHLTRLKGR EGGIYAFFVS
     NSDANFSITF HVYVNTKPEI ITSNRLSNGM LHCVAEGYPA PKIDWYFCPT AEQRCSDSPN
     ISPVEAKTNY KDSPFSPFGK IIVESTVDAS MFKNNGTIAC EASNDFDRSS AFFNFAIKEQ
     ISTHTLFTPL LLGFGVAAGL MCIMVIILVY KYLQKPKYEV QWKVVDEING NNYVYIDPTQ
     LPYDDKWEFP RNRLSFGKTL GAGAFGKVVE ATAYGLFKPD GAMRVAVKML KPSAHFTEKE
     ALMSELKVLS YLGNHINIVN LLGACTVGGP TLVITEYCCY GDLLNFLRRK RDSFICPKHE
     ETAVYKNLLY QKEQLYDGNN EYMDMKPGVS QIIQAKATKR KPARTGAFAN QDVTIAILED
     DEFALDIEDL LSFSYQVAKG MSFLSSKNCI HRDLAARNIL LTHGRITKIC DFGLARDIRN
     DSNYVVKGNA RLPVKWMAPE SIFDCVYTFE SDVWSYGILL WELFSLGSSP YPGMPVDSKF
     YKRIKEGYRM FSPEFAPAEM YEIMKSCWDA DPVKRPTFKQ IVQLIEQQIS DTTNHIYSNV
     TNGVCSQGNA TDHSMRINSV GSSASSTQPL LTHEDA
//
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