EPHAA_HUMAN
ID EPHAA_HUMAN Reviewed; 1008 AA.
AC Q5JZY3; A4FU89; J3KPB5; Q6NW42;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Ephrin type-A receptor 10;
DE EC=2.7.10.1;
DE Flags: Precursor;
GN Name=EPHA10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2),
RP ALTERNATIVE SPLICING, FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=15777695; DOI=10.1016/j.bbagen.2005.01.011;
RA Aasheim H.-C., Patzke S., Hjorthaug H.S., Finne E.F.;
RT "Characterization of a novel Eph receptor tyrosine kinase, EphA10,
RT expressed in testis.";
RL Biochim. Biophys. Acta 1723:1-7(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 501-1008 (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP VARIANTS [LARGE SCALE ANALYSIS] HIS-150; LYS-220; ILE-281; PRO-630; ARG-775
RP AND THR-956.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Receptor for members of the ephrin-A family. Binds to EFNA3,
CC EFNA4 and EFNA5. {ECO:0000269|PubMed:15777695}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC -!- INTERACTION:
CC Q5JZY3-3; Q8N9N5: BANP; NbExp=3; IntAct=EBI-10244652, EBI-744695;
CC Q5JZY3-3; Q13557: CAMK2D; NbExp=3; IntAct=EBI-10244652, EBI-351018;
CC Q5JZY3-3; Q13643: FHL3; NbExp=3; IntAct=EBI-10244652, EBI-741101;
CC Q5JZY3-3; Q12800: TFCP2; NbExp=3; IntAct=EBI-10244652, EBI-717422;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000305}; Single-
CC pass type I membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane {ECO:0000305}; Single-
CC pass type I membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5JZY3-1; Sequence=Displayed;
CC Name=2; Synonyms=Epha10s;
CC IsoId=Q5JZY3-2; Sequence=VSP_015772, VSP_015773;
CC Name=3; Synonyms=Epha10*;
CC IsoId=Q5JZY3-3; Sequence=VSP_015774, VSP_015775;
CC -!- TISSUE SPECIFICITY: Mainly expressed in testis.
CC {ECO:0000269|PubMed:15777695}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI12934.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ872185; CAI43321.1; -; Genomic_DNA.
DR EMBL; AJ781169; CAG77605.1; -; mRNA.
DR EMBL; AC104336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC067734; AAH67734.1; -; mRNA.
DR EMBL; BC112933; AAI12934.1; ALT_INIT; mRNA.
DR CCDS; CCDS41305.1; -. [Q5JZY3-1]
DR CCDS; CCDS425.1; -. [Q5JZY3-2]
DR RefSeq; NP_001092909.1; NM_001099439.1. [Q5JZY3-1]
DR RefSeq; NP_775912.2; NM_173641.2. [Q5JZY3-2]
DR AlphaFoldDB; Q5JZY3; -.
DR SMR; Q5JZY3; -.
DR BioGRID; 129927; 5.
DR IntAct; Q5JZY3; 5.
DR STRING; 9606.ENSP00000362139; -.
DR ChEMBL; CHEMBL2363043; -.
DR GlyGen; Q5JZY3; 2 sites.
DR iPTMnet; Q5JZY3; -.
DR PhosphoSitePlus; Q5JZY3; -.
DR BioMuta; EPHA10; -.
DR DMDM; 476007830; -.
DR jPOST; Q5JZY3; -.
DR MassIVE; Q5JZY3; -.
DR PaxDb; Q5JZY3; -.
DR PeptideAtlas; Q5JZY3; -.
DR PRIDE; Q5JZY3; -.
DR ProteomicsDB; 63538; -. [Q5JZY3-1]
DR ProteomicsDB; 63539; -. [Q5JZY3-2]
DR ProteomicsDB; 63540; -. [Q5JZY3-3]
DR Antibodypedia; 51311; 280 antibodies from 31 providers.
DR DNASU; 284656; -.
DR Ensembl; ENST00000319637.6; ENSP00000316395.6; ENSG00000183317.17. [Q5JZY3-2]
DR Ensembl; ENST00000373048.9; ENSP00000362139.4; ENSG00000183317.17. [Q5JZY3-1]
DR GeneID; 284656; -.
DR KEGG; hsa:284656; -.
DR MANE-Select; ENST00000373048.9; ENSP00000362139.4; NM_001099439.2; NP_001092909.1.
DR UCSC; uc001cbw.5; human. [Q5JZY3-1]
DR CTD; 284656; -.
DR DisGeNET; 284656; -.
DR GeneCards; EPHA10; -.
DR HGNC; HGNC:19987; EPHA10.
DR HPA; ENSG00000183317; Tissue enhanced (brain, intestine, testis).
DR MIM; 611123; gene.
DR neXtProt; NX_Q5JZY3; -.
DR OpenTargets; ENSG00000183317; -.
DR PharmGKB; PA134938798; -.
DR VEuPathDB; HostDB:ENSG00000183317; -.
DR eggNOG; KOG0196; Eukaryota.
DR GeneTree; ENSGT00940000160752; -.
DR HOGENOM; CLU_000288_141_4_1; -.
DR InParanoid; Q5JZY3; -.
DR OMA; FGCLQLP; -.
DR TreeFam; TF314013; -.
DR PathwayCommons; Q5JZY3; -.
DR Reactome; R-HSA-2682334; EPH-Ephrin signaling.
DR Reactome; R-HSA-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
DR SignaLink; Q5JZY3; -.
DR BioGRID-ORCS; 284656; 11 hits in 1109 CRISPR screens.
DR ChiTaRS; EPHA10; human.
DR GeneWiki; EPHA10; -.
DR GenomeRNAi; 284656; -.
DR Pharos; Q5JZY3; Tbio.
DR PRO; PR:Q5JZY3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5JZY3; protein.
DR Bgee; ENSG00000183317; Expressed in sperm and 127 other tissues.
DR ExpressionAtlas; Q5JZY3; baseline and differential.
DR Genevisible; Q5JZY3; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0005005; F:transmembrane-ephrin receptor activity; IDA:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
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; IPR016257; Tyr_kinase_ephrin_rcpt.
DR InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
DR Pfam; PF14575; EphA2_TM; 1.
DR Pfam; PF01404; Ephrin_lbd; 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; SM00060; FN3; 2.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS51550; EPH_LBD; 1.
DR PROSITE; PS50853; FN3; 2.
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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Glycoprotein; Kinase;
KW Membrane; Nucleotide-binding; Receptor; Reference proteome; Repeat;
KW Secreted; Signal; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..1008
FT /note="Ephrin type-A receptor 10"
FT /id="PRO_0000042157"
FT TOPO_DOM 34..565
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 566..586
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 587..1008
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..216
FT /note="Eph LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00883"
FT DOMAIN 340..452
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 456..554
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 645..900
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 933..997
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 322..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 284..295
FT /note="ACPPGFYKVSPR -> GIQLAGGRGVGV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15777695"
FT /id="VSP_015772"
FT VAR_SEQ 296..1008
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15777695"
FT /id="VSP_015773"
FT VAR_SEQ 889..892
FT /note="ERPR -> LPPH (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015774"
FT VAR_SEQ 893..1008
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015775"
FT VARIANT 103
FT /note="V -> L (in dbSNP:rs34557762)"
FT /id="VAR_055992"
FT VARIANT 150
FT /note="R -> H (in a gastric adenocarcinoma sample; somatic
FT mutation; dbSNP:rs771803475)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042159"
FT VARIANT 220
FT /note="T -> K (in dbSNP:rs56276182)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042160"
FT VARIANT 281
FT /note="F -> I (in dbSNP:rs4653328)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042161"
FT VARIANT 629
FT /note="L -> P (in dbSNP:rs17511304)"
FT /id="VAR_055993"
FT VARIANT 630
FT /note="L -> P"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042162"
FT VARIANT 645
FT /note="V -> I (in dbSNP:rs12405650)"
FT /id="VAR_055994"
FT VARIANT 749
FT /note="G -> E (in dbSNP:rs6671088)"
FT /id="VAR_055995"
FT VARIANT 775
FT /note="H -> R (in a breast infiltrating ductal carcinoma
FT sample; somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042163"
FT VARIANT 807
FT /note="R -> Q (in dbSNP:rs6670599)"
FT /id="VAR_055996"
FT VARIANT 956
FT /note="A -> T"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042164"
FT CONFLICT 458
FT /note="D -> G (in Ref. 1; CAI43321)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="T -> A (in Ref. 1; CAI43321)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1008 AA; 109716 MW; 82D60740B7B6B9BD CRC64;
METCAGPHPL RLFLCRMQLC LALLLGPWRP GTAEEVILLD SKASQAELGW TALPSNGWEE
ISGVDEHDRP IRTYQVCNVL EPNQDNWLQT GWISRGRGQR IFVELQFTLR DCSSIPGAAG
TCKETFNVYY LETEADLGRG RPRLGGSRPR KIDTIAADES FTQGDLGERK MKLNTEVREI
GPLSRRGFHL AFQDVGACVA LVSVRVYYKQ CRATVRGLAT FPATAAESAF STLVEVAGTC
VAHSEGEPGS PPRMHCGADG EWLVPVGRCS CSAGFQERGD FCEACPPGFY KVSPRRPLCS
PCPEHSRALE NASTFCVCQD SYARSPTDPP SASCTRPPSA PRDLQYSLSR SPLVLRLRWL
PPADSGGRSD VTYSLLCLRC GREGPAGACE PCGPRVAFLP RQAGLRERAA TLLHLRPGAR
YTVRVAALNG VSGPAAAAGT TYAQVTVSTG PGAPWEEDEI RRDRVEPQSV SLSWREPIPA
GAPGANDTEY EIRYYEKGQS EQTYSMVKTG APTVTVTNLK PATRYVFQIR AASPGPSWEA
QSFNPSIEVQ TLGEAASGSR DQSPAIVVTV VTISALLVLG SVMSVLAIWR RPCSYGKGGG
DAHDEEELYF HFKVPTRRTF LDPQSCGDLL QAVHLFAKEL DAKSVTLERS LGGGRFGELC
CGCLQLPGRQ ELLVAVHMLR DSASDSQRLG FLAEALTLGQ FDHSHIVRLE GVVTRGSTLM
IVTEYMSHGA LDGFLRRHEG QLVAGQLMGL LPGLASAMKY LSEMGYVHRG LAARHVLVSS
DLVCKISGFG RGPRDRSEAV YTTMSGRSPA LWAAPETLQF GHFSSASDVW SFGIIMWEVM
AFGERPYWDM SGQDVIKAVE DGFRLPPPRN CPNLLHRLML DCWQKDPGER PRFSQIHSIL
SKMVQDPEPP KCALTTCPRP PTPLADRAFS TFPSFGSVGA WLEALDLCRY KDSFAAAGYG
SLEAVAEMTA QDLVSLGISL AEHREALLSG ISALQARVLQ LQGQGVQV
