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Database: UniProt
Entry: E1BJ31_BOVIN
LinkDB: E1BJ31_BOVIN
Original site: E1BJ31_BOVIN 
ID   E1BJ31_BOVIN            Unreviewed;       975 AA.
AC   E1BJ31;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   Name=EPHA2 {ECO:0000313|Ensembl:ENSBTAP00000001080.4,
GN   ECO:0000313|VGNC:VGNC:28534};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000001080.4, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000001080.4, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000001080.4,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000001080.4}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000001080.4};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC       protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   RefSeq; NP_001192660.1; NM_001205731.1.
DR   AlphaFoldDB; E1BJ31; -.
DR   SMR; E1BJ31; -.
DR   STRING; 9913.ENSBTAP00000001080; -.
DR   PaxDb; 9913-ENSBTAP00000001080; -.
DR   Ensembl; ENSBTAT00000001080.5; ENSBTAP00000001080.4; ENSBTAG00000000815.5.
DR   GeneID; 512798; -.
DR   KEGG; bta:512798; -.
DR   CTD; 1969; -.
DR   VEuPathDB; HostDB:ENSBTAG00000000815; -.
DR   VGNC; VGNC:28534; EPHA2.
DR   eggNOG; KOG0196; Eukaryota.
DR   GeneTree; ENSGT00940000160786; -.
DR   HOGENOM; CLU_000288_141_0_1; -.
DR   InParanoid; E1BJ31; -.
DR   OMA; CLECPVH; -.
DR   OrthoDB; 1614410at2759; -.
DR   TreeFam; TF315608; -.
DR   Reactome; R-BTA-2682334; EPH-Ephrin signaling.
DR   Reactome; R-BTA-3928663; EPHA-mediated growth cone collapse.
DR   Reactome; R-BTA-3928665; EPH-ephrin mediated repulsion of cells.
DR   Reactome; R-BTA-9013149; RAC1 GTPase cycle.
DR   Reactome; R-BTA-9013404; RAC2 GTPase cycle.
DR   Reactome; R-BTA-9013408; RHOG GTPase cycle.
DR   Reactome; R-BTA-9013420; RHOU GTPase cycle.
DR   Reactome; R-BTA-9013423; RAC3 GTPase cycle.
DR   Reactome; R-BTA-9013424; RHOV GTPase cycle.
DR   Reactome; R-BTA-9696264; RND3 GTPase cycle.
DR   Reactome; R-BTA-9696270; RND2 GTPase cycle.
DR   Reactome; R-BTA-9696273; RND1 GTPase cycle.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000000815; Expressed in esophagus and 102 other cell types or tissues.
DR   ExpressionAtlas; E1BJ31; baseline.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005003; F:ephrin receptor activity; IEA:InterPro.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   CDD; cd10480; EphR_LBD_A2; 1.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd09543; SAM_EPH-A2; 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; 1.20.5.510; Single helix bin; 1.
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; IPR034263; EphA2_rcpt_lig-bd.
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; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
DR   InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
DR   PANTHER; PTHR46877; EPH RECEPTOR A5; 1.
DR   PANTHER; PTHR46877:SF12; EPHRIN TYPE-A RECEPTOR 3; 1.
DR   Pfam; PF14575; EphA2_TM; 1.
DR   Pfam; PF01404; Ephrin_lbd; 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; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
DR   PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 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:0000256|ARBA:ARBA00023137};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR000666-2};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW   Signal {ECO:0000256|SAM:SignalP};
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..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..975
FT                   /note="receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003144056"
FT   TRANSMEM        535..558
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          28..206
FT                   /note="Eph LBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51550"
FT   DOMAIN          328..437
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          438..529
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          613..874
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          903..967
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   ACT_SITE        738
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT   BINDING         619..627
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT   BINDING         645
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   DISULFID        70..188
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT   DISULFID        105..115
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ   SEQUENCE   975 AA;  107918 MW;  D09768D6C1CAF60D CRC64;
     MGRRAPPACL ALLWGCALAA ASAAQGKEVV LLDFAAAKGE LGWLTHPYGK GWDLLQNIMN
     DMPIYMYSVC NVVAGDQDNW LRTNWVYRGE AERIFIELKF TVRDCNSFPG GASSCKETFN
     LYYAESDVDY GTNFQKRQFT KIDTIAPDEI TGSSDFEARH VKLNVEERSV GPLTRKGFYL
     AFQDVGACVA LLSVRVYYKK CPELLKGLAR FPETIAGSDA PALATVAGNC VEHAVVPPGG
     EEPRMHCAVD GEWLVPIGQC LCQAGYEKVE DACQACSPGF FKPEASESPC LECPAHTLPS
     SEGATACECE DGYFRAPQDP LSLPCTRPPS APHYLTAVGM GAKVELRWTP PQDSGGREDL
     TYSVSCEQCW PESGECGPCE ASVRYSEPPL GLTRTSVTVS DLEPHMNYTF TVEARNGVSG
     LVSTRSFRTA SVSINQTEPP KVKLESRSTT SLSISWIIPP LQQSRVWKYE VTYRKKGDSN
     SYNVRRTEGF SVTLDDLAPD TVYLVQVQAL TQEGQGAGSK VHEFQTLSTG GSGNMAVVGG
     VAVGAVLLLV LAGIGFFIHR RRKSLRTRQS SEDVYFSKSE QLKPLKTYVD PHTYEDPNQA
     VLKFTTEIHP SCVTRQKVIG AGEFGEVYKG TLKASGKKEV PVAIKTLKAG YTEKQRVDFL
     SEASIMGQFS HHNIIRLEGV VSKYKPLMII TEYMENGALD KFLREKDGEF SVLQLVGMLR
     GVAAGMKYLA NMSYVHRDLA ARNILVNSNL VCKVSDFGLS RVLEDDPEAT YTTSGGKIPI
     RWTAPEAISY RKFTSASDVW SYGIVMWEVM TYGERPYWEL SNHEVMKAIN DGFRLPTPMD
     CPSAIYQLMM QCWQQERTRR PKFADIVSIL DKLIRAPDSL KTLADFDPRV SIRLPSTSGS
     EGVPFRTVSE WLESIKMQQY TEHFLVAGYT TIEKVVQMTN DDIKRIGVRL PGHQKRIAYS
     LLGLKDQVNT VGVPI
//
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