ID G3SFQ6_GORGO Unreviewed; 891 AA.
AC G3SFQ6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=EPH receptor A10 {ECO:0000313|Ensembl:ENSGGOP00000026942.2};
GN Name=EPHA10 {ECO:0000313|Ensembl:ENSGGOP00000026942.2};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000026942.2, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000026942.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000026942.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000026942.2}
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 EMBL; CABD030002491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030002492; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030002493; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030002494; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030002495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030002496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_018871146.1; XM_019015601.1.
DR AlphaFoldDB; G3SFQ6; -.
DR Ensembl; ENSGGOT00000024275.2; ENSGGOP00000026942.2; ENSGGOG00000007724.3.
DR KEGG; ggo:101135682; -.
DR eggNOG; KOG0196; Eukaryota.
DR GeneTree; ENSGT00940000160752; -.
DR OMA; FGCLQLP; -.
DR OrthoDB; 1614410at2759; -.
DR TreeFam; TF314013; -.
DR Proteomes; UP000001519; Chromosome 1.
DR Bgee; ENSGGOG00000007724; Expressed in testis and 2 other cell types or tissues.
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; cd10487; EphR_LBD_A10; 1.
DR CDD; cd00063; FN3; 1.
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; 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; 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; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR001245; Ser-Thr/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:SF16; EPHRIN TYPE-A RECEPTOR 10; 1.
DR Pfam; PF14575; EphA2_TM; 1.
DR Pfam; PF01404; Ephrin_lbd; 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; 2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00615; EPH_lbd; 1.
DR SMART; SM01411; Ephrin_rec_like; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00454; SAM; 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; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 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 Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000666-2}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..891
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014141040"
FT DOMAIN 35..216
FT /note="Eph LBD"
FT /evidence="ECO:0000259|PROSITE:PS51550"
FT DOMAIN 339..437
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 528..783
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 816..880
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT BINDING 534..542
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT DISULFID 77..198
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT DISULFID 112..122
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ SEQUENCE 891 AA; 97462 MW; 6CBFA12A8061D1A8 CRC64;
METCAGPHPL RLFLCRMQLC LALLLGPWRP GTAEEVILLD SKASQAELGW TALPSNGWEE
ISGVDEHDRP IRTYQVCNVL EPNQDNWLQT GWISRGRGQR IFVELQFTLR DCSSIPGAAG
TCKETFNVYY LETEADLGRK RPRLGGSRPR KIDTIAADES FTQGDLGERK MKLNTEVREI
GPLSRRGFHL AFQDVGACVA LVSVRVYYKQ CRATVRGLAT FPATAAESAF STLVEVAGTC
VAHSEGEPGS PPRMHCGADG EWLVPVGRCS CSAGFQERGD ICEACPPGFY KVSPRRPLCS
PCPEHSRALE NASTFCVCQD SYARSPTDPP SASCTPPWEE DEIRRDRVEP QSVSLSWREP
IPAGAPGAND TEYEIRYYEK GQSEQTYSMV KTGAPTVTVT NLKPATRYVF QIRAASLGPS
WEAQSFNPSI EVQTLGEAAS GSRDQSPAIV VTVVTISALL VLGSVMSVLA IWRRPCSYGK
GGGDAHDEEE LYFHFKVPTR RTFLDPQSCG DPLQAVHLFA KELDAKSVTL ERSLGGGRFG
ELCCGCLQLP GRQELPVAVH TLRDSASDSQ RLGFLAEALT LGQFDHSHIV RLEGVVTRGS
TLMIVTEYMS HGALDGFLRR HEGQLVAGQL MGLLPGLASA MKYLSEMGYV HRGLAARHVL
VSSDLVCKIS GFGRGPRDRS EAVYTTMSGR SPALWAAPET LQFGHFSSAS DVWSFGIIMW
EVMAFGERPY WDMSGQDVIK AVEDGFRLPP PRNCPNPLHR LMLDCWQKDP GERPRFSQIH
SILSKMVQDP EPPKCALTTC PRTPTPLADR AFSTFPSFGS VGAWLEALDL CRYKDSFAAA
GYGSLEAVAE MTAQDLVSLG ISSAEHREAL LSGISALQAR VLQLQGQGVQ V
//
