EPHA6_HUMAN
ID EPHA6_HUMAN Reviewed; 1036 AA.
AC Q9UF33; D6RAL5;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Ephrin type-A receptor 6;
DE EC=2.7.10.1;
DE AltName: Full=EPH homology kinase 2;
DE Short=EHK-2;
DE AltName: Full=EPH-like kinase 12;
DE Short=EK12;
DE Flags: Precursor;
GN Name=EPHA6; Synonyms=EHK2, HEK12;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=14726470; DOI=10.1373/clinchem.2003.026849;
RA Hafner C., Schmitz G., Meyer S., Bataille F., Hau P., Langmann T.,
RA Dietmaier W., Landthaler M., Vogt T.;
RT "Differential gene expression of Eph receptors and ephrins in benign human
RT tissues and cancers.";
RL Clin. Chem. 50:490-499(2004).
RN [4]
RP VARIANT [LARGE SCALE ANALYSIS] SER-704.
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 tyrosine kinase which binds promiscuously GPI-
CC anchored ephrin-A family ligands residing on adjacent cells, leading to
CC contact-dependent bidirectional signaling into neighboring cells. The
CC signaling pathway downstream of the receptor is referred to as forward
CC signaling while the signaling pathway downstream of the ephrin ligand
CC is referred to as reverse signaling (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 Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBUNIT: Heterotetramer upon binding of the ligand. The heterotetramer
CC is composed of an ephrin dimer and a receptor dimer. Oligomerization is
CC probably required to induce biological responses (By similarity).
CC Interacts (via SAM domain) with ANKS1A (via SAM domain) (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q62413}.
CC -!- INTERACTION:
CC Q9UF33; Q04771: ACVR1; NbExp=2; IntAct=EBI-3950019, EBI-1383616;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UF33-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UF33-2; Sequence=VSP_018473, VSP_018474, VSP_018475,
CC VSP_018476;
CC Name=3;
CC IsoId=Q9UF33-3; Sequence=VSP_018473, VSP_018474, VSP_054716,
CC VSP_054717;
CC -!- TISSUE SPECIFICITY: Expressed in brain and testis.
CC {ECO:0000269|PubMed:14726470}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; AL133666; CAB63775.1; -; mRNA.
DR EMBL; AC109782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC134730; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC135369; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC119745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117470; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC130510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117439; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS54616.1; -. [Q9UF33-2]
DR CCDS; CCDS63697.1; -. [Q9UF33-3]
DR PIR; T43450; T43450.
DR RefSeq; NP_001265229.1; NM_001278300.1. [Q9UF33-3]
DR RefSeq; NP_775926.1; NM_173655.3. [Q9UF33-2]
DR AlphaFoldDB; Q9UF33; -.
DR SMR; Q9UF33; -.
DR BioGRID; 130049; 11.
DR IntAct; Q9UF33; 4.
DR MINT; Q9UF33; -.
DR STRING; 9606.ENSP00000374323; -.
DR BindingDB; Q9UF33; -.
DR ChEMBL; CHEMBL4526; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q9UF33; -.
DR GlyGen; Q9UF33; 3 sites.
DR iPTMnet; Q9UF33; -.
DR PhosphoSitePlus; Q9UF33; -.
DR BioMuta; EPHA6; -.
DR DMDM; 97048747; -.
DR jPOST; Q9UF33; -.
DR MassIVE; Q9UF33; -.
DR MaxQB; Q9UF33; -.
DR PaxDb; Q9UF33; -.
DR PeptideAtlas; Q9UF33; -.
DR PRIDE; Q9UF33; -.
DR ProteomicsDB; 13364; -.
DR ProteomicsDB; 84168; -. [Q9UF33-1]
DR ProteomicsDB; 84169; -. [Q9UF33-2]
DR Antibodypedia; 32095; 411 antibodies from 35 providers.
DR DNASU; 285220; -.
DR Ensembl; ENST00000502694.1; ENSP00000423950.1; ENSG00000080224.18. [Q9UF33-2]
DR Ensembl; ENST00000514100.5; ENSP00000421711.1; ENSG00000080224.18. [Q9UF33-3]
DR GeneID; 285220; -.
DR KEGG; hsa:285220; -.
DR UCSC; uc003drr.6; human. [Q9UF33-1]
DR CTD; 285220; -.
DR DisGeNET; 285220; -.
DR GeneCards; EPHA6; -.
DR HGNC; HGNC:19296; EPHA6.
DR HPA; ENSG00000080224; Tissue enhanced (brain, testis).
DR MIM; 600066; gene.
DR neXtProt; NX_Q9UF33; -.
DR OpenTargets; ENSG00000080224; -.
DR PharmGKB; PA134866684; -.
DR VEuPathDB; HostDB:ENSG00000080224; -.
DR eggNOG; KOG0196; Eukaryota.
DR GeneTree; ENSGT00940000154490; -.
DR HOGENOM; CLU_000288_141_5_1; -.
DR InParanoid; Q9UF33; -.
DR OrthoDB; 933071at2759; -.
DR PathwayCommons; Q9UF33; -.
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; Q9UF33; -.
DR SIGNOR; Q9UF33; -.
DR BioGRID-ORCS; 285220; 7 hits in 1100 CRISPR screens.
DR ChiTaRS; EPHA6; human.
DR GeneWiki; EPHA6; -.
DR GenomeRNAi; 285220; -.
DR Pharos; Q9UF33; Tchem.
DR PRO; PR:Q9UF33; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9UF33; protein.
DR Bgee; ENSG00000080224; Expressed in left testis and 89 other tissues.
DR ExpressionAtlas; Q9UF33; baseline and differential.
DR Genevisible; Q9UF33; HS.
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:0005654; C:nucleoplasm; IDA:HPA.
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; IBA:GO_Central.
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; cd10484; EphR_LBD_A6; 1.
DR CDD; cd00063; FN3; 2.
DR CDD; cd09547; SAM_EPH-A6; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR042746; EPH-A6_SAM.
DR InterPro; IPR027936; Eph_TM.
DR InterPro; IPR034280; EphA6_rcpt_lig-bd.
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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; 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; PF07699; Ephrin_rec_like; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
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 SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS51550; EPH_LBD; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 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; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1036
FT /note="Ephrin type-A receptor 6"
FT /id="PRO_0000235684"
FT TOPO_DOM 23..550
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 551..571
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 572..1036
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..212
FT /note="Eph LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00883"
FT DOMAIN 331..441
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 442..537
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 631..944
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 961..1025
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT MOTIF 1034..1036
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT ACT_SITE 798
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 637..645
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 663
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 606
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000255"
FT MOD_RES 612
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000255"
FT MOD_RES 831
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000255"
FT MOD_RES 978
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..514
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_018473"
FT VAR_SEQ 515..538
FT /note="IRVRTATGYSGYSQKFEFETGDET -> MKDSPFQVTKLYWLNEKWDFIASA
FT (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_018474"
FT VAR_SEQ 835..912
FT /note="GGKIPIRWTAPEAIAYRKFSSASDAWSYGIVMWEVMSYGERPYWEMSNQDVI
FT LSIEEGYRLPAPMGCPASLHQLMLHC -> RPTNHNKEQSELVKEDGLESLCEQCESSS
FT GYGTGLVLMWKRNRRAMGASGQTRKQCDKRDNPPTDLFQTLTLNLCYSA (in
FT isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_054716"
FT VAR_SEQ 835..848
FT /note="GGKIPIRWTAPEAI -> DLFQTLTLNLCYSA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_018475"
FT VAR_SEQ 849..1036
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_018476"
FT VAR_SEQ 913..1036
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_054717"
FT VARIANT 704
FT /note="F -> S"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042149"
FT VARIANT 711
FT /note="A -> V (in dbSNP:rs4857276)"
FT /id="VAR_055991"
SQ SEQUENCE 1036 AA; 116379 MW; 53402C6DCD7CD32C CRC64;
MGGCEVREFL LQFGFFLPLL TAWPGDCSHV SNNQVVLLDT TTVLGELGWK TYPLNGWDAI
TEMDEHNRPI HTYQVCNVME PNQNNWLRTN WISRDAAQKI YVEMKFTLRD CNSIPWVLGT
CKETFNLFYM ESDESHGIKF KPNQYTKIDT IAADESFTQM DLGDRILKLN TEIREVGPIE
RKGFYLAFQD IGACIALVSV RVFYKKCPFT VRNLAMFPDT IPRVDSSSLV EVRGSCVKSA
EERDTPKLYC GADGDWLVPL GRCICSTGYE EIEGSCHACR PGFYKAFAGN TKCSKCPPHS
LTYMEATSVC QCEKGYFRAE KDPPSMACTR PPSAPRNVVF NINETALILE WSPPSDTGGR
KDLTYSVICK KCGLDTSQCE DCGGGLRFIP RHTGLINNSV IVLDFVSHVN YTFEIEAMNG
VSELSFSPKP FTAITVTTDQ DAPSLIGVVR KDWASQNSIA LSWQAPAFSN GAILDYEIKY
YEKEHEQLTY SSTRSKAPSV IITGLKPATK YVFHIRVRTA TGYSGYSQKF EFETGDETSD
MAAEQGQILV IATAAVGGFT LLVILTLFFL ITGRCQWYIK AKMKSEEKRR NHLQNGHLRF
PGIKTYIDPD TYEDPSLAVH EFAKEIDPSR IRIERVIGAG EFGEVCSGRL KTPGKREIPV
AIKTLKGGHM DRQRRDFLRE ASIMGQFDHP NIIRLEGVVT KRSFPAIGVE AFCPSFLRAG
FLNSIQAPHP VPGGGSLPPR IPAGRPVMIV VEYMENGSLD SFLRKHDGHF TVIQLVGMLR
GIASGMKYLS DMGYVHRDLA ARNILVNSNL VCKVSDFGLS RVLEDDPEAA YTTTGGKIPI
RWTAPEAIAY RKFSSASDAW SYGIVMWEVM SYGERPYWEM SNQDVILSIE EGYRLPAPMG
CPASLHQLML HCWQKERNHR PKFTDIVSFL DKLIRNPSAL HTLVEDILVM PESPGEVPEY
PLFVTVGDWL DSIKMGQYKN NFVAAGFTTF DLISRMSIDD IRRIGVILIG HQRRIVSSIQ
TLRLHMMHIQ EKGFHV
