ID Q5D184_APIME Unreviewed; 996 AA.
AC Q5D184; A0A8B6WZ05;
DT 29-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 29-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 145.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
DE Flags: Precursor;
GN Name=EphR {ECO:0000313|RefSeq:NP_001013024.1};
GN Synonyms=Eph {ECO:0000313|RefSeq:NP_001013024.1};
OS Apis mellifera (Honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Apis.
OX NCBI_TaxID=7460 {ECO:0000313|Proteomes:UP000005203, ECO:0000313|RefSeq:NP_001013024.1};
RN [1] {ECO:0000313|RefSeq:NP_001013024.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17073008; DOI=10.1038/nature05260;
RG Honeybee Genome Sequencing Consortium;
RT "Insights into social insects from the genome of the honeybee Apis
RT mellifera.";
RL Nature 443:931-949(2006).
RN [2] {ECO:0000313|RefSeq:NP_001013024.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17443785; DOI=10.1002/dneu.20341;
RA Vidovic M., Nighorn A., Koblar S., Maleszka R.;
RT "Eph receptor and ephrin signaling in developing and adult brain of the
RT honeybee (Apis mellifera).";
RL Dev. Neurobiol. 67:233-251(2007).
RN [3] {ECO:0000313|RefSeq:NP_001013024.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24479613;
RG HGSC production teams;
RG Honey Bee Genome Sequencing Consortium;
RA Elsik C.G., Worley K.C., Bennett A.K., Beye M., Camara F., Childers C.P.,
RA de Graaf D.C., Debyser G., Deng J., Devreese B., Elhaik E., Evans J.D.,
RA Foster L.J., Graur D., Guigo R., Hoff K.J., Holder M.E., Hudson M.E.,
RA Hunt G.J., Jiang H., Joshi V., Khetani R.S., Kosarev P., Kovar C.L., Ma J.,
RA Maleszka R., Moritz R.F., Munoz-Torres M.C., Murphy T.D., Muzny D.M.,
RA Newsham I.F., Reese J.T., Robertson H.M., Robinson G.E., Rueppell O.,
RA Solovyev V., Stanke M., Stolle E., Tsuruda J.M., Vaerenbergh M.V.,
RA Waterhouse R.M., Weaver D.B., Whitfield C.W., Wu Y., Zdobnov E.M.,
RA Zhang L., Zhu D., Gibbs R.A.;
RT "Finding the missing honey bee genes: lessons learned from a genome
RT upgrade.";
RL BMC Genomics 15:86-86(2014).
RN [4] {ECO:0000313|RefSeq:NP_001013024.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25331961;
RA Shelomi M., Jasper W.C., Atallah J., Kimsey L.S., Johnson B.R.;
RT "Differential expression of endogenous plant cell wall degrading enzyme
RT genes in the stick insect (Phasmatodea) midgut.";
RL BMC Genomics 15:917-917(2014).
RN [5] {ECO:0000313|RefSeq:NP_001013024.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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 RefSeq; NP_001013024.1; NM_001013006.1.
DR AlphaFoldDB; Q5D184; -.
DR GeneID; 408489; -.
DR KEGG; ame:408489; -.
DR CTD; 408489; -.
DR Proteomes; UP000005203; Linkage group LG14.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005003; F:ephrin receptor activity; IEA:InterPro.
DR GO; GO:0022008; P:neurogenesis; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0000003; P:reproduction; IEA:UniProt.
DR CDD; cd10319; EphR_LBD; 1.
DR CDD; cd00063; FN3; 2.
DR CDD; cd05033; PTKc_EphR; 1.
DR CDD; cd09488; SAM_EPH-R; 1.
DR Gene3D; 2.60.40.1770; ephrin a2 ectodomain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 1.
DR InterPro; IPR027936; Eph_TM.
DR InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
DR PANTHER; PTHR46877; EPH RECEPTOR A5; 1.
DR PANTHER; PTHR46877:SF14; RECEPTOR PROTEIN-TYROSINE KINASE; 1.
DR Pfam; PF14575; EphA2_TM; 1.
DR Pfam; PF01404; Ephrin_lbd; 1.
DR Pfam; PF07699; Ephrin_rec_like; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00536; SAM_1; 1.
DR PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00615; EPH_lbd; 1.
DR SMART; SM01411; Ephrin_rec_like; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS51550; EPH_LBD; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000666-
KW 2}; Disulfide bond {ECO:0000256|PIRSR:PIRSR000666-3};
KW Kinase {ECO:0000313|RefSeq:NP_001013024.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000666-2};
KW Receptor {ECO:0000256|ARBA:ARBA00023170,
KW ECO:0000313|RefSeq:NP_001013024.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005203};
KW Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001013024.1};
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 SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP,
FT ECO:0000313|RefSeq:NP_001013024.1"
FT CHAIN 19..996
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP,
FT ECO:0000313|RefSeq:NP_001013024.1"
FT /id="PRO_5035544037"
FT TRANSMEM 533..556
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 760
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT BINDING 639..647
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT BINDING 667
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 62..178
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT DISULFID 97..107
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ SEQUENCE 996 AA; 109976 MW; 8D1BA9F4BED2B85D CRC64;
MFPVRSIFFL SLVSVVLLDT TQEEKLEWTK YPFGAEANTP GWVEESFTNF DKGINWRSYV
VCDVAYNNVN NWLWTPFIER GPANRMYIEI KFTTRDCSLF PGNALSCKET FSLLYYEFDV
ATKEPPPWET DSYKLIGRIA AGEGRFNTNT EVVINTEVKS IPVTKKGVYF AFRDQGACIS
ILAIKVYYIS CPEISVNFAH FPATPTGREV ALIEQTIGTC VANAVVIEQP TFLCKGDGKW
YLPSGGCHCK PGYQADVEKQ ECTECPIGKF KHEAGSHSCE ACPAHSKSSD YGFTECRCDP
GYFRAEKDPK KMPCTQPPSA PQNLTVNFVD QSTVFLSWNA PHMLGGRTDT TYRVVCDACS
MGVKYIPNTE VFNDTKITIT GLNAVTTYRF QVFAENGVSA LAGKSEYVDI TVTTDASVPS
LVSNVRITSV KSSELSISWD APITEIGGDS DLVERYEVRC YPRYDDATNA TVIQTSELSA
TFKGLKPSTD YAIQVRAKTT RGWGEYTPVV YKKTPHAMGL DYVGEDDNMQ VRIIAGAIVA
VVVLLVIIII MTVLILRRAS DECNKKQPSD CDTLEYRNGE VTTPLFTPAV GVAAASAGGA
GGGGARSYVD PHTYEDPNQA VREFAREIDA GYITIEAIIG GGEFGDVCRG KLKLPPDGRT
EIDVAIKTLK PGSADKARND FLTEASIMGQ FEHPNVIFLQ GVVTKSNPVM IITEFMENGS
LDTFLRANDG KFQVLQLVGM LRGIASGMQY LAEMNYVHRD LAARNVLVNA ALVCKIADFG
LSREIESATE GAYTTRGGKI PVRWTAPEAI AFRKFTSASD VWSMGIVCWE VMSYGERPYW
NWSNQDVIKS IEKGYRLPAP MDCPEAIYQL MLDCWQKERT HRPTFANLTQ TLDKLIRSPD
TLRKIAQNRG TNPLAPDAVD LTQLTSVSEW LASIKMSRYA ESFERSGVTT LEAAARVTVQ
ELTALGVTLV GHQKKIMNSV TALRAQMSAT SQGFLV
//
