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 24-JAN-2024, entry version 173. 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 INVOLVEMENT IN DFNA88. 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). RN [5] 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 -!- DISEASE: Deafness, autosomal dominant, 88 (DFNA88) [MIM:620283]: A form CC of non-syndromic, sensorineural hearing loss. Sensorineural hearing CC loss results from damage to the neural receptors of the inner ear, the CC nerve pathways to the brain, or the area of the brain that receives CC sound information. DFNA88 is characterized by postlingual, progressive CC and severe hearing loss with tinnitus. {ECO:0000269|PubMed:36048850}. CC Note=The disease may be caused by variants affecting the gene CC represented in this entry. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 85. DR IntAct; Q5JZY3; 84. DR STRING; 9606.ENSP00000362139; -. DR ChEMBL; CHEMBL2363043; -. DR GlyCosmos; Q5JZY3; 2 sites, No reported glycans. 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; 9606-ENSP00000362139; -. DR PeptideAtlas; Q5JZY3; -. DR ProteomicsDB; 63538; -. [Q5JZY3-1] DR ProteomicsDB; 63539; -. [Q5JZY3-2] DR ProteomicsDB; 63540; -. [Q5JZY3-3] DR Antibodypedia; 51311; 307 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 AGR; HGNC:19987; -. DR CTD; 284656; -. DR DisGeNET; 284656; -. DR GeneCards; EPHA10; -. DR HGNC; HGNC:19987; EPHA10. DR HPA; ENSG00000183317; Tissue enhanced (brain, intestine, testis). DR MalaCards; EPHA10; -. DR MIM; 611123; gene. DR MIM; 620283; phenotype. 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 OrthoDB; 1614410at2759; -. 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 1186 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 129 other cell types or tissues. DR ExpressionAtlas; Q5JZY3; baseline and differential. DR GO; GO:0030425; C:dendrite; IBA:GO_Central. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; NAS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005005; F:transmembrane-ephrin receptor activity; IDA:UniProtKB. 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; cd10487; EphR_LBD_A10; 1. DR CDD; cd00063; FN3; 2. DR CDD; cd05064; PTKc_EphR_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; 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; 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. DR Genevisible; Q5JZY3; HS. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Cell membrane; Deafness; Glycoprotein; KW Kinase; Membrane; Non-syndromic deafness; Nucleotide-binding; Receptor; KW Reference proteome; Repeat; Secreted; Signal; Transferase; Transmembrane; KW Transmembrane helix; 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 //