EPHAA_MOUSE
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 03-AUG-2022, entry version 149.
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).
CC -!- FUNCTION: Receptor for members of the ephrin-A family. Binds to EFNA3,
CC EFNA4 and EFNA5 (By similarity). {ECO:0000250}.
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 -!- 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 GlyGen; Q8BYG9; 2 sites.
DR iPTMnet; Q8BYG9; -.
DR PhosphoSitePlus; Q8BYG9; -.
DR jPOST; Q8BYG9; -.
DR MaxQB; Q8BYG9; -.
DR PeptideAtlas; Q8BYG9; -.
DR PRIDE; Q8BYG9; -.
DR ProteomicsDB; 277886; -. [Q8BYG9-1]
DR ProteomicsDB; 277887; -. [Q8BYG9-2]
DR Antibodypedia; 51311; 280 antibodies from 31 providers.
DR DNASU; 230735; -.
DR Ensembl; ENSMUST00000059343; ENSMUSP00000050810; ENSMUSG00000028876. [Q8BYG9-2]
DR GeneID; 230735; -.
DR KEGG; mmu:230735; -.
DR UCSC; uc008urh.2; mouse. [Q8BYG9-2]
DR UCSC; uc008uri.2; mouse. [Q8BYG9-1]
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; 933071at2759; -.
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; 1 hit in 41 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 tissues.
DR ExpressionAtlas; Q8BYG9; baseline and differential.
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: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; ISO:MGI.
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; PF07647; SAM_2; 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 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
