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Database: UniProt
Entry: G5BQY7_HETGA
LinkDB: G5BQY7_HETGA
Original site: G5BQY7_HETGA 
ID   G5BQY7_HETGA            Unreviewed;       970 AA.
AC   G5BQY7;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   ORFNames=GW7_17937 {ECO:0000313|EMBL:EHB11698.1};
OS   Heterocephalus glaber (Naked mole rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Heterocephalus.
OX   NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB11698.1, ECO:0000313|Proteomes:UP000006813};
RN   [1] {ECO:0000313|EMBL:EHB11698.1, ECO:0000313|Proteomes:UP000006813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993625; DOI=10.1038/nature10533;
RA   Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA   Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA   Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA   Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA   Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA   Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT   "Genome sequencing reveals insights into physiology and longevity of the
RT   naked mole rat.";
RL   Nature 479:223-227(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001171};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. {ECO:0000256|ARBA:ARBA00006692}.
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DR   EMBL; JH171425; EHB11698.1; -; Genomic_DNA.
DR   RefSeq; XP_004844370.1; XM_004844313.2.
DR   RefSeq; XP_004844371.1; XM_004844314.2.
DR   RefSeq; XP_004844372.1; XM_004844315.2.
DR   AlphaFoldDB; G5BQY7; -.
DR   STRING; 10181.G5BQY7; -.
DR   GeneID; 101718876; -.
DR   CTD; 10461; -.
DR   eggNOG; ENOG502QQQ3; Eukaryota.
DR   InParanoid; G5BQY7; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000006813; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd00096; Ig; 1.
DR   CDD; cd05749; IgI_2_Axl_Tyro3_like; 1.
DR   CDD; cd14204; PTKc_Mer; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
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; IPR013151; Immunoglobulin.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   PANTHER; PTHR24416:SF257; TYROSINE-PROTEIN KINASE MER; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF13927; Ig_3; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Kinase {ECO:0000313|EMBL:EHB11698.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000256|ARBA:ARBA00023137};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   TRANSMEM        473..494
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          63..158
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          169..245
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          258..353
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          358..456
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          558..828
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         590
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   970 AA;  107563 MW;  648358B3FA3F3D5A CRC64;
     MREETKPYQP FPRSLQVDHR PFSYPHTSGY QPSSMLSPTQ PRRSHPGNTA DPQATPAATK
     LRPPVAFNHT VGHIILSEHK DVKFNCSINI PNVYQETESV SWWKDGKELR RAHNTVTQYY
     PDNEVMSIIA SFSITSVQRS DNGSYICKMK VNNIEIVSDP IDIEVQGLPY FTKQPESLNV
     TRNTAFNLTC QAVGPPEPVN IFWVRNSSRI NEQPEKSPSV LTVPGLTEMA IFSCEAHNDK
     GLTVSKGVQV NIKAIPSPPT EVHIHNSTAH SILISWVPGF DGYSPFKNCS VQVKEVDPLS
     KGSVMIFNTS ASPHLYQIQQ LQALANYSIG VSCMNEIGWS SVSPWILAST IEGAPTIAPL
     NVTVFLDESA GNVDIRWIRP SIKQQDGELV GYRISHVWQS DRTSKEFFEE VGQNGSQAQI
     SVKVYNATYS VRIAAITKGG VGPFSDPVKI FIPAQGMDSA PSSTPAPGST DPVLVILGCL
     CGFILIGLIL YISLAIRKRA QETKFGTAFT EEDSELVVNY TAKKSYCRRA IELTLQSLGV
     SEELQNKLED VVIDRNLLIL GKVLGEGEFG SVMEGNLKQQ AGTSQKVAVK TMKLDNFSQR
     EIEEFLSEAA CMKDFSHPNV IRLLGVCIEM SSQGIPKPMV ILPFMKYGDL HTYLLYSRLE
     TGPKHIPLQT LLKFMVDIAL GMEYLSNRNF LHRDLAARNC MLRDDMTVCV ADFGLSKKIY
     SGDYYRQGRI AKMPVKWIAL ESLADRVYTS KSDVWAFGVT MWEIATRGMT PYPGVQNHEM
     YDYLLYGHRL KQPEDCLDEL YEIMFSCWSA DPLDRPTFSV LRLQLEKLSE SLPDAQDKAA
     VVYVNTPLSK SCDGLAEGLA LAQLDMNIDP DSIIASCTPS AGASVVKVEV HENKPQEERY
     ILNGGSEEWD NQASVPLATA PGEKNSVLPE DRLGQNGVLW SHCSTLPLGS TSPDELLFAD
     DSLEDSEVLM
//
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