GenomeNet

Database: UniProt
Entry: Q8BYG9
LinkDB: Q8BYG9
Original site: Q8BYG9 
ID   EPHAA_MOUSE             Reviewed;        1007 AA.
AC   Q8BYG9; A2A7J5; Q3UPV5;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   24-JAN-2024, entry version 157.
DE   RecName: Full=Ephrin type-A receptor 10;
DE            EC=2.7.10.1;
DE   Flags: Precursor;
GN   Name=Epha10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Eye, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   TISSUE SPECIFICITY.
RX   PubMed=36048850; DOI=10.1093/hmg/ddac223;
RA   Huang S., Ma L., Liu X., He C., Li J., Hu Z., Jiang L., Liu Y., Liu X.,
RA   Feng Y., Cai X.;
RT   "A non-coding variant in 5' untranslated region drove up-regulation of
RT   pseudo-kinase EPHA10 and caused non-syndromic hearing loss in humans.";
RL   Hum. Mol. Genet. 32:720-731(2023).
CC   -!- FUNCTION: Receptor for members of the ephrin-A family. Binds to EFNA3,
CC       EFNA4 and EFNA5 (By similarity). {ECO:0000250|UniProtKB:Q5JZY3}.
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BYG9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BYG9-2; Sequence=VSP_023676, VSP_023677;
CC   -!- TISSUE SPECIFICITY: Expressed in the cochlea, in the organ of Corti,
CC       spiral ganglion, and stria vascularis. {ECO:0000269|PubMed:36048850}.
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
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=CAM16104.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AK039700; BAC30423.1; -; mRNA.
DR   EMBL; AK143168; BAE25289.1; -; mRNA.
DR   EMBL; AL606933; CAM16103.1; -; Genomic_DNA.
DR   EMBL; AL606933; CAM16104.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC116991; AAI16992.1; -; mRNA.
DR   EMBL; BC119084; AAI19085.1; -; mRNA.
DR   CCDS; CCDS18630.1; -. [Q8BYG9-2]
DR   RefSeq; NP_808339.2; NM_177671.5. [Q8BYG9-2]
DR   AlphaFoldDB; Q8BYG9; -.
DR   SMR; Q8BYG9; -.
DR   STRING; 10090.ENSMUSP00000050810; -.
DR   GlyCosmos; Q8BYG9; 2 sites, No reported glycans.
DR   GlyGen; Q8BYG9; 2 sites.
DR   iPTMnet; Q8BYG9; -.
DR   PhosphoSitePlus; Q8BYG9; -.
DR   jPOST; Q8BYG9; -.
DR   MaxQB; Q8BYG9; -.
DR   PaxDb; 10090-ENSMUSP00000050810; -.
DR   PeptideAtlas; Q8BYG9; -.
DR   ProteomicsDB; 277886; -. [Q8BYG9-1]
DR   ProteomicsDB; 277887; -. [Q8BYG9-2]
DR   Antibodypedia; 51311; 307 antibodies from 31 providers.
DR   DNASU; 230735; -.
DR   Ensembl; ENSMUST00000059343.7; ENSMUSP00000050810.6; ENSMUSG00000028876.8. [Q8BYG9-2]
DR   GeneID; 230735; -.
DR   KEGG; mmu:230735; -.
DR   UCSC; uc008urh.2; mouse. [Q8BYG9-2]
DR   UCSC; uc008uri.2; mouse. [Q8BYG9-1]
DR   AGR; MGI:3586824; -.
DR   CTD; 284656; -.
DR   MGI; MGI:3586824; Epha10.
DR   VEuPathDB; HostDB:ENSMUSG00000028876; -.
DR   GeneTree; ENSGT00940000160752; -.
DR   HOGENOM; CLU_000288_141_3_1; -.
DR   InParanoid; Q8BYG9; -.
DR   OMA; CEGIQGP; -.
DR   OrthoDB; 1614410at2759; -.
DR   PhylomeDB; Q8BYG9; -.
DR   Reactome; R-MMU-2682334; EPH-Ephrin signaling.
DR   Reactome; R-MMU-3928663; EPHA-mediated growth cone collapse.
DR   Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
DR   BioGRID-ORCS; 230735; 2 hits in 46 CRISPR screens.
DR   ChiTaRS; Epha10; mouse.
DR   PRO; PR:Q8BYG9; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q8BYG9; Protein.
DR   Bgee; ENSMUSG00000028876; Expressed in piriform cortex and 71 other cell types or tissues.
DR   ExpressionAtlas; Q8BYG9; baseline and differential.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005005; F:transmembrane-ephrin receptor activity; ISO:MGI.
DR   GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR   GO; GO:0048013; P:ephrin receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 2.
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; 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; 2.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF07647; SAM_2; 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; 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   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cell membrane; Glycoprotein; Kinase;
KW   Membrane; Nucleotide-binding; Receptor; Reference proteome; Repeat; Signal;
KW   Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..1007
FT                   /note="Ephrin type-A receptor 10"
FT                   /id="PRO_0000280444"
FT   TOPO_DOM        23..565
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        566..586
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        587..1007
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          644..899
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          932..996
FT                   /note="SAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   REGION          323..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          467..486
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..292
FT                   /note="ACPPGFYKV -> GIQGPRGMG (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_023676"
FT   VAR_SEQ         293..1007
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_023677"
FT   CONFLICT        156
FT                   /note="A -> S (in Ref. 1; BAC30423)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        657
FT                   /note="T -> D (in Ref. 2; CAM16104)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        980
FT                   /note="T -> A (in Ref. 2; CAM16104)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        985
FT                   /note="S -> A (in Ref. 2; CAM16104)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1007 AA;  109100 MW;  157A0E17CDCB9ED9 CRC64;
     METGAGPHPL RLFVCLIPLC LALLLGPGRP GTAEEVILLD SKASQAELGW TALPSTGWEE
     ISGVDEHDRP IRTYQVCNVL EPNQDNWLQT GWISRGRGQR IFVELQFTLR DCSSIPGATG
     TCKETFNAYY LETETDLGRG RPRLGGNRPR KIDTIAADES FTQGDLGERK MKLNTEVREI
     GPLSRQGFHL AFQDVGACVA LVSVRVYYKQ CRATVRGLAA FPATAAESAF STLVEVAGTC
     VAHSEGEPSS PPRMHCGADG EWLVPVGRCS CSAGFQEHGD ICEACPPGFY KVSPRRPLCS
     PCPEHSLALE NASTFCVCQD TYARSPTDPP SASCTRPPSA PRDLQYSLSR SPLALRLRWL
     PPADSGGRSD VTYSLLCLRC GRDGPAGACQ PCGPRVAFVP RQAGLRERAA TLLHLRPGAR
     YTVRVAALNG VSGPAAAAGA TYAQVTVSTG PGAPWEEDEI RRDRVEPQSV SLSWREPVPA
     GAPGTNSTEY EIRYYEKGQS EQTYSTVKTG APAVTVTNLK PATRYVFQIR AASPGPLWEA
     QSFSPSIEVQ TPGEVAPGSR DQSPAVVVTV VTISALLVLG SVMSVLAIWR RPCDGKGSGN
     AHDEEELYFH FKVPTRRTFL DPQSCGDPLQ AVHLFAKELD AKSVTLEKSL GAGRFGTLCC
     GCLQLPGRQE LPVAVHTLRD GCSDSQRLSF LAEALTLGQF DHSHIVRLEG VVTRGNPLMI
     VTEYMNLGAL DDFLRHHEGE LVAAQLMGLL PGLASAMKYL SEMGYVHRGL AARRVLVSSG
     LLCKISGFGR GPRDRAEAVY TTMSGRSPAL WAAPETLQFG HFSSASDVWS FGIVMWEVMA
     FGERPYWDMS GQDVIKAVED GFRLPPPRNC PSQLHRLMLE CWQKDPSERP RFSQIHSILS
     KMGQEPEPSK CASTTCLRPP TPLADRAFST FPSFGSVGAW LEALDLCRYK DNFSAAGYGS
     LEAVAEMTAQ DLGSLGISST EHRESLLSGI SALQTRVLQL QGQGVQV
//
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