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Database: UniProt
Entry: E2AY54_CAMFO
LinkDB: E2AY54_CAMFO
Original site: E2AY54_CAMFO 
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};
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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
//
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