ID I3K7K0_ORENI Unreviewed; 1027 AA.
AC I3K7K0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=EPH receptor A10 {ECO:0000313|Ensembl:ENSONIP00000017095.1};
GN Name=epha10 {ECO:0000313|Ensembl:ENSONIP00000017095.1};
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:ENSONIP00000017095.1, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000017095.1}
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 RefSeq; XP_013128044.1; XM_013272590.2.
DR AlphaFoldDB; I3K7K0; -.
DR STRING; 8128.ENSONIP00000050541; -.
DR Ensembl; ENSONIT00000017110.2; ENSONIP00000017095.1; ENSONIG00000013593.2.
DR GeneID; 100701099; -.
DR KEGG; onl:100701099; -.
DR CTD; 284656; -.
DR eggNOG; KOG0196; Eukaryota.
DR GeneTree; ENSGT00940000164552; -.
DR HOGENOM; CLU_000288_141_4_1; -.
DR OrthoDB; 1614410at2759; -.
DR TreeFam; TF315608; -.
DR Proteomes; UP000005207; Linkage group LG22.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005003; F:ephrin receptor activity; IEA:InterPro.
DR CDD; cd00063; FN3; 2.
DR CDD; cd05064; PTKc_EphR_A10; 1.
DR CDD; cd09549; SAM_EPH-A10; 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; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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; IPR016257; Tyr_kinase_ephrin_rcpt.
DR InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
DR PANTHER; PTHR46877; EPH RECEPTOR A5; 1.
DR PANTHER; PTHR46877:SF16; EPHRIN TYPE-A RECEPTOR 10; 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 SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 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; PS50011; PROTEIN_KINASE_DOM; 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 Membrane {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 Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1027
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003673424"
FT TRANSMEM 583..607
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..205
FT /note="Eph LBD"
FT /evidence="ECO:0000259|PROSITE:PS51550"
FT DOMAIN 326..434
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 438..536
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 661..917
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 952..1016
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 519..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 693
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT DISULFID 68..187
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT DISULFID 104..114
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ SEQUENCE 1027 AA; 113423 MW; FCD472784E735984 CRC64;
MDLRKTLISV LWILLLNEVK DYNAEEVVLL NSKETQAELG WTSYPPNGWE EISGVDEKYK
PIRTYQVCNV MEPTQQNNWL QTGWVARRGG QRIFVELQFT LRDCNSIPGV AGTCKETFNL
LYVESDRDLG GVTREDRYTK IDTIAADESF TQGDLGERKM KLNTEVREIG HLNRKGFHLA
FQDVGACVAL VAVRVYYKRC LATVQNLAVF PDTVAEAAFA TLVEVRGTCV NNSEVDTDSP
PRMHCSAEGE WLVPIGKCSC SAGYEEGHSS CEACPPGSYK MSSRQQECFP CPANSVAEEE
GSMVCLCEED HFRTPLDNPS APCTRPPSPP RDLTYTLKQS TLILDWAAPS DTGGRVDLTY
SVGCRKCIGR QCEPCGASVG FVPQQVGLTE RTVTVVNLLP NTNYTFTVEA LNGVSELLPN
KRFYTQVNVS TSLPAPSLIS ELRAEKIEQK SITLVWREPS YPNSSRTGYE VKYYEKEQKD
QSYSTVKTAA TRISVNNLKP GTTYVFLIRP FSTPAPSSAL SSSPLSSSSS SSTSSSSSTS
SSSSSSSSSS SSPPPIDYGA YSTPLELQTL GELALASSEQ NPVVIIVVVS VAALIMLLSM
GVGLLIWRRQ CGYSKASQEG DEELYFQFKI PTRRTYIDPE TCEDLLQAVH AFAKELDNSS
IKIERIVHTG DFGEVCRGCL KLPSKRELPV AIKTLRAGCS DKQRRSFLSE AGILGQFDHS
NIIRLEGVIT TGNTMMIIVE CMSNGALDSF LRKHEGQLSI MQLMDMLTGV ASGMKYLTEM
GFVHKRLAAH KVLVNSNLGC KVSGFRPLQE DKIEAIYTTL HGGKSVVLWT APEAIQYHRF
SSASDVWSFG IVMWEVMSYG ERPYWDMGNQ DVIKAIEDGF RLPAPVNCPP HLHQLMLDCW
QKERTERPSF SQIHSALSKS IRSPDGIGSS TLARRTLSSS ITLADRPLPT FPSFNSVGEW
LDAVDMGRYK DNFTAAGYCY LESVARMTVQ DVLSLGITSL EHQKLILAAI QTLRAQVIQM
HGRGVQV
//
