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Database: UniProt
Entry: A0A671X5Y5_SPAAU
LinkDB: A0A671X5Y5_SPAAU
Original site: A0A671X5Y5_SPAAU 
ID   A0A671X5Y5_SPAAU        Unreviewed;      1010 AA.
AC   A0A671X5Y5;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   Name=EPHA6 {ECO:0000313|Ensembl:ENSSAUP00010046554.1};
OS   Sparus aurata (Gilthead sea bream).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Spariformes; Sparidae; Sparus.
OX   NCBI_TaxID=8175 {ECO:0000313|Ensembl:ENSSAUP00010046554.1, ECO:0000313|Proteomes:UP000472265};
RN   [1] {ECO:0000313|Ensembl:ENSSAUP00010046554.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   AlphaFoldDB; A0A671X5Y5; -.
DR   Ensembl; ENSSAUT00010048921.1; ENSSAUP00010046554.1; ENSSAUG00010019347.1.
DR   GeneTree; ENSGT00940000154490; -.
DR   Proteomes; UP000472265; Unplaced.
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   CDD; cd10484; EphR_LBD_A6; 1.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd05066; PTKc_EphR_A; 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; IPR034280; EphA6_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; 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:SF10; EPHRIN TYPE-A 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; 2.
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}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000472265};
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   TRANSMEM        533..558
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          19..197
FT                   /note="Eph LBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51550"
FT   DOMAIN          316..426
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          430..522
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          616..908
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          939..999
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   ACT_SITE        772
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT   BINDING         622..630
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT   BINDING         648
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   DISULFID        61..179
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT   DISULFID        96..106
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ   SEQUENCE   1010 AA;  113907 MW;  1EF1D467793164D8 CRC64;
     MNMFMTDFSI SGAKVGLFVF VLLDTTSVLG ELGWKTYPIN GWDAITEMDE HNRPIHTFQV
     CNVMEPNQNN WLRSNWISRQ AAQKIYVELR FTLRDCNSIP WVSGTCKETF NLFYHETDEA
     HGVKFKPPQY TKIDTIAADE SFTQMDLGDR ILKLNTEVRE VGPMTRKGFY LAFQDIGACI
     ALVSVRVYYK KCPFTLRNLA SFPDTVPRVD SSSLVEVRGA CIDHAEERDT PKLFCGADGD
     WLVPLGKCVC SVGYEEIDGS CSACHPGFYK AYAGNIKCSK CPPHSFSYGE GAAICRCEKG
     FFRAEKDPPT MACTRPPSPP RNPMFNLNDT CLMLEWLPPS DTGGRRDLTY NVQCKRCGPE
     PNHCQLCEED LRFLPRPLGL TNATVTVMEF SAHANYTFEI ESLNGVSDMS SFPRQVAIIT
     VSTDQGGPSL IGALKKDWAS PNSIALSWQQ PEQTTLPILD YEIKYYEKEH EQLSYSSTRT
     RAPSVIISGL KPATWYVFSV RTRSPAGYSS YSHKYEYETT GDSSDIASDQ GQVLVIVTAA
     VGGFTLLVIL TLFLLITGRC QWYFKAKMTS EEKRRTNYQN GHVPFPGIKT YVDPDTYEDP
     TQAVHEFTKE IDPSRIRIER VIGAGEFGEV CSGRLRTPGK KEIAVAIKTL KGGYVERQRR
     DFLREASIMG QFDHPNIIRL EGVVTKRDFV EAACPFFGGG NFYHSQFHVC VVFCVFAGRP
     VMIVVEYMEN GSLDSFLRQH DGHFTVIQLV GMLRGIASGM KYLSDMGYVH RDLAARNILV
     NSNLVCKVSD FGLSRVLEDD PEAAYTTTGG KIPIRWTAPE AISYRKFSSA SDAWSYGIVM
     WEVMSYGERP YWEMSNQDVI LSIEEGYRLP APMGCPVALH QLMLHCWQKE RSHRPKFTDV
     VSFLDKLIRN PSSLLPLVED IQSLPESPGE EMDYPMFISI GDWLDSIKMS QYKSNFMAAG
     YDTLDSVARM SIEDVRNLGV ELIGHQRRII SSVQTLRLQL LHEQEKGFHV
//
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