ID F4WUP1_ACREC Unreviewed; 1411 AA.
AC F4WUP1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN ORFNames=G5I_09618 {ECO:0000313|EMBL:EGI62038.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI62038.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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; GL888375; EGI62038.1; -; Genomic_DNA.
DR RefSeq; XP_011060106.1; XM_011061804.1.
DR STRING; 103372.F4WUP1; -.
DR EnsemblMetazoa; XM_011061804.1; XP_011060106.1; LOC105149416.
DR GeneID; 105149416; -.
DR eggNOG; KOG0200; Eukaryota.
DR InParanoid; F4WUP1; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000007755; 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; 7.
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; 2.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 2.
DR SMART; SM00409; IG; 7.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; Immunoglobulin; 6.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 4.
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:EGI62038.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1411
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003323879"
FT TRANSMEM 751..773
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 228..323
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 428..529
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 544..614
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 646..740
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 827..1182
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1312..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1388..1411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1312..1327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1396..1411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1047
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 861
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1052
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 1065
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
SQ SEQUENCE 1411 AA; 161221 MW; 3A92B51FC94393CE CRC64;
MLPYRARLRV QTLIVLALCQ VTASNKPIIS PNQDQIVINE GEPLEITCTG STPIQFIYPN
DFGESVNTST PKKTKENDEI NNIYKYVFER PNTVFGDTGW YGCADHNVEI ITNSYEREDP
EMNWLYVYVK SNTNLFVEAD TYAHLSAVAG GSIIIPCRLT SPDLIPILSD NNEEELKNAS
FDPRIGFTIR NLLVKDSNWY KCSIEKDGEE HAVNYVLSVH LKRTLPDPKI QDESLLHVTR
GQDLYVNCTV EVEISMRYVF DWNTPQQNSG RISTQQFRKQ LDGNSVLVTC QLTILNVTDE
DAGEYECVIR SIHDIKKITK NITIHDPQMK YIHLIPQHTD KYYQAESGNY VQWVVYVDGW
PKPHLEWFKP NSEEIIESPK YFVNTSVTAT ILKIMSLSVM DSGNYTLEAK NDYMIEKLNF
TLNVIAKPVS ILTRIDSYYP PNESTEFHCE VISNPSPNIT WSFLRCPNYP SLENSTTIYP
TDMTQSAAYS SSYRFESILK MPIEESGKIT CKACNVLACD SVTDNILVSD GLGAFGIIGP
KEPVTKGDDI ELICAASVYN YTDEFTWTIS VNETEEPLME TERLQIVRHK TPFTYRSTLK
LYRVQESDAE NYFCIGKIMT TVYYEAPDIL SDYANYKLII HDPVSPYFTK TNMNETKIRT
IDVMAEGHKT VILQCFTEGM PKPTVTWYKD NVLLKENDQY FFKYNYQELN IKYLKHHDSG
KYSCRAISRL GTNETYQQIT VKNAKWHKLD IILATSIAIL GFFLVILAIF FTIKVRREKK
MRKELMEAGL MHFEEGALEC LNPDLTVDDQ AELLPYDKKW EFPRERLKLG KQLGSGEFGV
VMKAEAHGIC ESETVTTVAV KMVRRTTNPT YVRALASELK IMVHLGKHLN VVNLLGACTK
NISKRELLVI VEYCRFGNLH NYLLRHRNDF INQIDPKTGK LDLNIGMDIL MRTSSVSSNN
SLSANSDTGD VVVHYCPGTN PDSPEINFSP DGCINSNSSQ PGWRSNYCGD YKDQHLKPIC
TQDLLSWAFQ VARGMEYLCQ RNVLHGDLAA RNILLAEDNI VKICDFGLAK TMYKDGNYKK
KGDGPVPIKW MAIESIRDRV FSTQSDIWSF GIVLWEFFTL AETPYPGMEA EKQYQKLIEG
YRMEQPDYAI REVYDIMLQC WKAKPTLRPS FTDLVESIGN LLEENVRLHY ISLNTPYMDM
NTMNLESGKN DYLTMMSAPD HTVLSSPSHD YVNSPFSKGA PDSSYLCMSP GCPTDESGIF
SPRPHQEHSH FEFPSPASDS EDAVELSPML KHTEEDPYLK PINVHERRAE FARQRQAMKD
QTVDRPIDRD SGYCNAPRNL HLIDLNDMDV NDAQMDTTDL KKKDYAPSII CMQDNYVNMP
KQKNDLRKGI PDSFSNPSYV MISNHEVDQK T
//
