ID A0A669EJ31_ORENI Unreviewed; 920 AA.
AC A0A669EJ31;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 19.
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:ENSONIP00000072900.1};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000072900.1, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Ensembl:ENSONIP00000072900.1}
RP IDENTIFICATION.
RG Ensembl;
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}.
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DR AlphaFoldDB; A0A669EJ31; -.
DR Ensembl; ENSONIT00000085228.1; ENSONIP00000072900.1; ENSONIG00000004324.2.
DR GeneTree; ENSGT00940000154490; -.
DR OMA; YKNNFVA; -.
DR Proteomes; UP000005207; 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; 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; 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; 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; 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:UP000005207};
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 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 534..557
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..201
FT /note="Eph LBD"
FT /evidence="ECO:0000259|PROSITE:PS51550"
FT DOMAIN 320..430
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 434..523
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 594..855
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 886..920
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT ACT_SITE 719
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT BINDING 600..608
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT BINDING 626
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 65..183
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT DISULFID 100..110
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ SEQUENCE 920 AA; 103695 MW; 80D7342A4B1C73B2 CRC64;
MIFFFFFYLN VVWTEMVLLA VSFTLVQRRI SEQLNVLLSK FGLNTWDAIT EMDEHNRPIH
TFQVCNVMEP NQNNWLRSNW ISRQAAQKVY VELRFTLRDC NSIPWVSGTC KETFNLFYHE
TDEAHGVKFR PAQYTKIDTI AADESFTQMD LGDRILKLNT EVREVGPINR KGFYLAFQDI
GACIALVSVR VYYKKCPFTL RNLASFPDTV PRVDSSSLVE VRGACVDHAE ERDTPKLFCG
ADGDWLVPLG RCVCSVGYEE IDGSCVACRP GFYKAYAGNI KCSKCPPHSF SYGDASAICR
CEKGFFRAEK DPPTMACTRP PSPPRNLIFN LNDTCLLLEW SPPSDTGGRR DLTYNVQCKR
CGPEPDHCQL CEDELRFLPG PLGLTNATVT VLDFSAHANY TFEIESLNGV SDMSSFPRQV
AIITVSTDQG GPSLVGTLKK DWASPNSIAL SWQQPEQTTL PIIDYEVKYY EKVLKYSVYD
SKAPSVIVSG LKPATWYVFS VRTRTAAGYS SYSPKYEYET TGDSSNMASD QGQVLVIVTA
AVGGFTLLVI LTLFLLITGS EYFTAWLTYV DPDTYEDPTQ AVHEFTKEID PSRIRIERVI
GAGEFGEVCS GRLRTPGKKE IAVAIKTLKG GYVERQRRDF LREASIMGQF DHPNIIRLEG
VVTKSRPVMI VVEYMENGSL DSFLRQHDGH FTVIQLVGML RGIASGMKYL SDMGYVHRDL
AARNILVNSN LVCKVSDFGL SRVLEDDPEA AYTTTGGKIP IRWTAPEAIS YRKFSSASDA
WSYGIVMWEV MSYGERPYWE MSNQDVILSI EEGYRLPAPM GCPVALHQLM LHCWQKERNH
RPKFTDIVSF LDKLIRNPSS LLPLVEDIQS LPESPGEEMD YPMFISVGDW LDSIKMSQYK
SNFMAAGYNT LDSVARMSIE
//
