ID A0A2I0MLB7_COLLI Unreviewed; 1000 AA.
AC A0A2I0MLB7;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN Name=EPHB6 {ECO:0000313|EMBL:PKK30466.1};
GN ORFNames=A306_00003616 {ECO:0000313|EMBL:PKK30466.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK30466.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK30466.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK30466.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKK30466.1}.
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DR EMBL; AKCR02000007; PKK30466.1; -; Genomic_DNA.
DR RefSeq; XP_005506370.1; XM_005506313.1.
DR AlphaFoldDB; A0A2I0MLB7; -.
DR STRING; 8932.A0A2I0MLB7; -.
DR GeneID; 102096618; -.
DR KEGG; clv:102096618; -.
DR InParanoid; A0A2I0MLB7; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000053872; Unassembled WGS sequence.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd10475; EphR_LBD_B6; 1.
DR CDD; cd00063; FN3; 2.
DR CDD; cd05065; PTKc_EphR_B; 1.
DR CDD; cd09555; SAM_EPH-B6; 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 InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
DR PANTHER; PTHR46877; EPH RECEPTOR A5; 1.
DR PANTHER; PTHR46877:SF15; EPHRIN TYPE-B RECEPTOR 6; 1.
DR Pfam; PF14575; EphA2_TM; 1.
DR Pfam; PF01404; Ephrin_lbd; 1.
DR Pfam; PF07699; Ephrin_rec_like; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF07647; SAM_2; 1.
DR PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR PRINTS; PR00014; FNTYPEIII.
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:ARBA00022777};
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, ECO:0000313|EMBL:PKK30466.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053872};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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 TRANSMEM 559..583
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 31..213
FT /note="Eph LBD"
FT /evidence="ECO:0000259|PROSITE:PS51550"
FT DOMAIN 342..450
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 451..546
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 635..898
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 927..991
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT ACT_SITE 760
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT BINDING 641..649
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 73..195
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT DISULFID 108..118
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ SEQUENCE 1000 AA; 111802 MW; D6B5E4D3DEECBCEF CRC64;
MDSNAGISAR SVAGMGWLWM VCFFHLVTSL EEKLLDTTGE TSEIGWTTHP SNGWDEVSVL
DDKKRLIRTF DVCNVAEPGQ NNWLRTHFIE RRGAHRVHVR LRFSVRDCAS MHIVASSCKE
TFTLYYHQSE ADLASQELPE WREGPWTKVD TIAADESFSQ VDSTGKVVKM NVKVRSFGPL
TKHGFYLAFQ DSGACMSLVA VQVFFYKCPA VVKGFASFPE TFAGGERTSL VESPGICVPN
AEETSTTGSS GIRLHCNGEG EWMVAIGRCV CKAGYQPIDD ERVCQACPLG FFKVSVGHDP
CLPCPAHSHA PLPGSRECVC QNRYYRSPMD NSDAPCTGIP SAPRDLSYEI VGSNVLLTWR
LPKDLGGRKD IFFNVICKVC PAGSSGPCVR CGDRVQFEPR QVGLTESRVQ VSNLLARVHY
TFEIQAVNLV TELSPEAPHY ATINVSTSQT VPSAVPMMHQ VSRTTSSITL SWPQPDQPNG
IILDYQLRYF DKAEDEDNSF ILTSETNMAT ISNLSPGKIY AFQVRARTAV GYGAYSGKMY
FQTLMGGERS DMVQDRLPLI VGSALGGLAF LVIAAISTLA IIFKSKRQET PYTDRLQQYI
SARGLGVKYY IDPSTYEDPN EAIREFAKEI DVSFIKIEEV IGSGEFGQVC FGRLKHPGKR
EYTVAIKTLK SGYTDEQWRE FLSEASIMGQ FEHPNVIHLE GVVTKNRPVM IVTEFMENGS
LDSFLRQKEG QFSVLQLVGM LRGIAAGMRY LSDMNYVHRD LAARNILVNS NLVCKVSDFG
LSRFLEDDAS NPTYTGALGC KIPIRWTAPE AIQYRKFTSS SDVWSYGIVM WEVMSYGERP
YWDMSNQDVI NAIDQDYRLP PPPDCPTVLH LLMLDCWQKE RVQRPRFEQI VSALDKMIRK
PSALKATGTG SNRPSQPLLS NCPPDFPSLS NAHEWLDAIK MGRYKENFDQ AGLITFDVIS
RMTLEDIQRI GITLVGHQKK ILNSIQLMRV HLNQLEPVEV
//
