ID E2AY54_CAMFO Unreviewed; 1124 AA.
AC E2AY54;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN ORFNames=EAG_05954 {ECO:0000313|EMBL:EFN61650.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN61650.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL443762; EFN61650.1; -; Genomic_DNA.
DR AlphaFoldDB; E2AY54; -.
DR STRING; 104421.E2AY54; -.
DR EnsemblMetazoa; XM_025413886.1; XP_025269671.1; LOC105257298.
DR InParanoid; E2AY54; -.
DR OMA; SGFNEDK; -.
DR Proteomes; UP000000311; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0022008; P:neurogenesis; IEA:UniProt.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
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; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
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; IPR001824; Tyr_kinase_rcpt_3_CS.
DR PANTHER; PTHR24416:SF600; PDGF-AND VEGF-RECEPTOR RELATED, ISOFORM J; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 2.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
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.
DR PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:EFN61650.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000311};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 466..488
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 208..302
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 361..457
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 542..897
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 762
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 576
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 767
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 780
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
SQ SEQUENCE 1124 AA; 128161 MW; 98AC8E77724F89B7 CRC64;
MQKFSESNKP IISPNQEEIV LNEGEFLEII CTGTAPLKFV YPDTFDKEVF NTSTPRISKN
EENGVYKYIF QRPKIIFGDT GWYGCADYNV EIPNFFDNSE VNWLYVYVKS NTNLFVEADT
YAHLNAVAGD SIVIPCRPTS PDLDPDLSNN NEDELEGKAS FDPRIGFTIK NLTVKDSDWY
KCSIQKDNEE HQVNYVLAVH LRQTLPDPKI HDDTLRHVTR GQDLFVNCTV EIDASVRYVF
NWSTPQSNSR VSTQQFRKQL DDNYLLVTCQ LTVFNVTDED AGEYKCIIRS IHDTKDTKKN
ITIHDGIGAF GIIGPKELVT KDDTVELICA ASVYNYTDDL TWTKLENETE TPVIETNPVS
PFFTKTNMNE TIVKNIDVIA EGHKTVILQC FADGMPKPII AWYKDNVLLV ENDQYLFKFN
YQELNIKYFK EYDSGRYSCR AINRLGTNET YQEIMVKNAK LQKLDVILAV SIAILGITLV
ILAIFFTIKV RREKKMRKEL MEAGLMHFEE GALECLNPDL TVDDQAELLP YDKKWEFPRE
QLKLGKQLGS GAFGVVMKAE AQGISENETV TTVAVKMVRR TTDPTYVRAL ASELKIMVHL
GKHLNVVNLL GACTKNISKR ELLVIVEYCR FGNLHNYLLK HRSNFINQID PNTGKLDLTI
GVDILTRTAS ISSNNSISAN SGTDTVVHYC PGTSSDTQEI NFSPDGCVLS NNSFQPDWRT
NYRGDYKDQN LKPICTQDLL SYAFQVARGM EYLSQRRVLH GDLAARNILL CENNIVKICD
FGLAKTMYKD DNYKKKGDGP LPIKWMAIES IRDRIFSTQS DIWSFGIVLW EFFTLSETPY
PSMEAEKLYQ KLIEGYRMEQ PEYSIREIYE IMSQCWKAKP TLRPSFTDLV ESIGNLLEES
VKSHYISLNT PYMDMNTMIL ESGKNDYLTM MSAPDHGALS SPGHYANSPF SEGAPDSSYL
CMSPNCQTNE SGIFSPRPHE DRSHFEFPSP ASDSEDAVEL SPMLKHEEDP YLKPINVQER
RAEFARQREA MKNQMTERSI DRDSGYCNAP RNLHLIDLND MDENDAAHRA DADSKKDYVP
PIISTQDNYV NMPKQKSDLR LGVPDGFSNP SYVMMNTREM DQRV
//