EVI5_HUMAN
ID EVI5_HUMAN Reviewed; 810 AA.
AC O60447; A6NKX8; B9A6J0; Q9H1Y9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Ecotropic viral integration site 5 protein homolog;
DE Short=EVI-5;
DE AltName: Full=Neuroblastoma stage 4S gene protein;
GN Name=EVI5; Synonyms=NB4S;
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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DISEASE,
RP CHROMOSOMAL TRANSLOCATION WITH TRNG10, AND VARIANTS VAL-82 AND VAL-336.
RC TISSUE=Brain;
RX PubMed=9618176; DOI=10.1093/hmg/7.7.1169;
RA Roberts T., Chernova O., Cowell J.K.;
RT "NB4S, a member of the TBC1 domain family of genes, is truncated as a
RT result of a constitutional t(1;10)(p22;q21) chromosome translocation in a
RT patient with stage 4S neuroblastoma.";
RL Hum. Mol. Genet. 7:1169-1178(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS VAL-82 AND VAL-336.
RX PubMed=19077034; DOI=10.1111/j.1365-2443.2008.01251.x;
RA Ishibashi K., Kanno E., Itoh T., Fukuda M.;
RT "Identification and characterization of a novel Tre-2/Bub2/Cdc16 (TBC)
RT protein that possesses Rab3A-GAP activity.";
RL Genes Cells 14:41-52(2009).
RN [3]
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 [4]
RP TISSUE SPECIFICITY, OLIGOMERIZATION, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH ALPHA-TUBULIN AND GAMMA-TUBULIN.
RX PubMed=16033705; DOI=10.1016/j.ygeno.2005.06.002;
RA Faitar S.L., Dabbeekeh J.T.S., Ranalli T.A., Cowell J.K.;
RT "EVI5 is a novel centrosomal protein that binds to alpha- and gamma-
RT tubulin.";
RL Genomics 86:594-605(2005).
RN [5]
RP FUNCTION, INTERACTION WITH FBXO5, INDUCTION, UBIQUITINATION, SUBCELLULAR
RP LOCATION, AND PHOSPHORYLATION BY PLK1.
RX PubMed=16439210; DOI=10.1016/j.cell.2005.10.038;
RA Eldridge A.G., Loktev A.V., Hansen D.V., Verschuren E.W., Reimann J.D.R.,
RA Jackson P.K.;
RT "The evi5 oncogene regulates cyclin accumulation by stabilizing the
RT anaphase-promoting complex inhibitor emi1.";
RL Cell 124:367-380(2006).
RN [6]
RP INTERACTION WITH AURKB; BIRC5 AND INCENP, AND SUBCELLULAR LOCATION.
RX PubMed=16764853; DOI=10.1016/j.yexcr.2006.03.032;
RA Faitar S.L., Sossey-Alaoui K., Ranalli T.A., Cowell J.K.;
RT "EVI5 protein associates with the INCENP-aurora B kinase-survivin
RT chromosomal passenger complex and is involved in the completion of
RT cytokinesis.";
RL Exp. Cell Res. 312:2325-2335(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-776, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-689, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Functions as a regulator of cell cycle progression by
CC stabilizing the FBXO5 protein and promoting cyclin-A accumulation
CC during interphase. May play a role in cytokinesis.
CC {ECO:0000269|PubMed:16439210}.
CC -!- SUBUNIT: Dimeric and monomeric. Interacts with alpha- and gamma-
CC tubulin. Interacts with FBXO5. Interacts with the chromosome passenger
CC complex (CPC) which is at least composed of AURKB/aurora-B,
CC BIRC5/survivin, CDCA8/borealin and INCENP.
CC {ECO:0000269|PubMed:16033705, ECO:0000269|PubMed:16439210,
CC ECO:0000269|PubMed:16764853}.
CC -!- INTERACTION:
CC O60447; P40617: ARL4A; NbExp=3; IntAct=EBI-852291, EBI-2875746;
CC O60447; Q8N715: CCDC185; NbExp=3; IntAct=EBI-852291, EBI-740814;
CC O60447; Q96LK0: CEP19; NbExp=3; IntAct=EBI-852291, EBI-741885;
CC O60447; P48730: CSNK1D; NbExp=3; IntAct=EBI-852291, EBI-751621;
CC O60447; Q12959: DLG1; NbExp=2; IntAct=EBI-852291, EBI-357481;
CC O60447; Q14241: ELOA; NbExp=3; IntAct=EBI-852291, EBI-742350;
CC O60447; Q3B820: FAM161A; NbExp=3; IntAct=EBI-852291, EBI-719941;
CC O60447; Q9UKT4: FBXO5; NbExp=6; IntAct=EBI-852291, EBI-852298;
CC O60447; Q9NV31: IMP3; NbExp=3; IntAct=EBI-852291, EBI-747481;
CC O60447; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-852291, EBI-726510;
CC O60447; P25800: LMO1; NbExp=3; IntAct=EBI-852291, EBI-8639312;
CC O60447; Q8IYB1: MB21D2; NbExp=3; IntAct=EBI-852291, EBI-11323212;
CC O60447; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-852291, EBI-348259;
CC O60447; Q15014: MORF4L2; NbExp=3; IntAct=EBI-852291, EBI-399257;
CC O60447; P53350: PLK1; NbExp=3; IntAct=EBI-852291, EBI-476768;
CC O60447; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-852291, EBI-1567797;
CC O60447; P62491: RAB11A; NbExp=6; IntAct=EBI-852291, EBI-745098;
CC O60447; Q6BDI9: REP15; NbExp=3; IntAct=EBI-852291, EBI-12048237;
CC O60447; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-852291, EBI-11955057;
CC O60447; Q8WVP5: TNFAIP8L1; NbExp=3; IntAct=EBI-852291, EBI-752102;
CC O60447; Q9NWS9-2: ZNF446; NbExp=3; IntAct=EBI-852291, EBI-740232;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Cytoplasm, cytoskeleton, spindle.
CC Note=Associates with the mitotic spindle through anaphase and remains
CC within the midzone and midbody until completion of cytokinesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O60447-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60447-2; Sequence=VSP_056828;
CC -!- TISSUE SPECIFICITY: Expressed in various cell lines (at protein level).
CC Expressed in a wide range of tissues including brain and adrenal.
CC {ECO:0000269|PubMed:16033705, ECO:0000269|PubMed:9618176}.
CC -!- INDUCTION: Down-regulated during mitosis through proteasomal
CC degradation. {ECO:0000269|PubMed:16439210}.
CC -!- PTM: Probably phosphorylated by PLK1; may be required for degradation
CC during mitosis. {ECO:0000269|PubMed:16439210}.
CC -!- PTM: Ubiquitinated. Degradation during prophase is ubiquitin-dependent.
CC {ECO:0000269|PubMed:16439210}.
CC -!- DISEASE: Note=A chromosomal aberration involving EVI5 is found is a
CC patient with stage 4S neuroblastoma. Translocation t(1;10)(p22;q21)
CC that forms a EVI5-TRNG10 fusion protein. TRNG10 is a probable
CC structural transcript which is normally not translated.
CC {ECO:0000269|PubMed:9618176}.
CC -!- MISCELLANEOUS: Depletion of EVI5 by RNAi causes cell cycle arrest and
CC mitotic abnormalities.
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DR EMBL; AF008915; AAC16031.1; -; mRNA.
DR EMBL; AB449875; BAH16618.1; -; mRNA.
DR EMBL; AC104332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104456; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS30774.1; -. [O60447-1]
DR CCDS; CCDS76179.1; -. [O60447-2]
DR RefSeq; NP_001295177.1; NM_001308248.1. [O60447-2]
DR RefSeq; NP_005656.4; NM_005665.5. [O60447-1]
DR AlphaFoldDB; O60447; -.
DR SMR; O60447; -.
DR BioGRID; 113584; 65.
DR CORUM; O60447; -.
DR DIP; DIP-38024N; -.
DR IntAct; O60447; 40.
DR STRING; 9606.ENSP00000359356; -.
DR iPTMnet; O60447; -.
DR PhosphoSitePlus; O60447; -.
DR BioMuta; EVI5; -.
DR EPD; O60447; -.
DR jPOST; O60447; -.
DR MassIVE; O60447; -.
DR MaxQB; O60447; -.
DR PaxDb; O60447; -.
DR PeptideAtlas; O60447; -.
DR PRIDE; O60447; -.
DR ProteomicsDB; 49405; -. [O60447-1]
DR Antibodypedia; 19897; 89 antibodies from 20 providers.
DR DNASU; 7813; -.
DR Ensembl; ENST00000370331.5; ENSP00000359356.1; ENSG00000067208.16. [O60447-1]
DR Ensembl; ENST00000540033.2; ENSP00000440826.2; ENSG00000067208.16. [O60447-2]
DR GeneID; 7813; -.
DR KEGG; hsa:7813; -.
DR UCSC; uc001dox.3; human. [O60447-1]
DR CTD; 7813; -.
DR DisGeNET; 7813; -.
DR GeneCards; EVI5; -.
DR HGNC; HGNC:3501; EVI5.
DR HPA; ENSG00000067208; Low tissue specificity.
DR MIM; 602942; gene.
DR neXtProt; NX_O60447; -.
DR OpenTargets; ENSG00000067208; -.
DR PharmGKB; PA27915; -.
DR VEuPathDB; HostDB:ENSG00000067208; -.
DR eggNOG; KOG4436; Eukaryota.
DR GeneTree; ENSGT00940000153846; -.
DR HOGENOM; CLU_005350_6_0_1; -.
DR InParanoid; O60447; -.
DR OMA; NSKKMKX; -.
DR OrthoDB; 191811at2759; -.
DR PhylomeDB; O60447; -.
DR TreeFam; TF317184; -.
DR PathwayCommons; O60447; -.
DR SignaLink; O60447; -.
DR SIGNOR; O60447; -.
DR BioGRID-ORCS; 7813; 7 hits in 1081 CRISPR screens.
DR ChiTaRS; EVI5; human.
DR GeneWiki; EVI5; -.
DR GenomeRNAi; 7813; -.
DR Pharos; O60447; Tbio.
DR PRO; PR:O60447; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O60447; protein.
DR Bgee; ENSG00000067208; Expressed in calcaneal tendon and 194 other tissues.
DR ExpressionAtlas; O60447; baseline and differential.
DR Genevisible; O60447; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
DR InterPro; IPR031214; Evi5.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR PANTHER; PTHR22957:SF254; PTHR22957:SF254; 2.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Chromosomal rearrangement;
KW Coiled coil; Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..810
FT /note="Ecotropic viral integration site 5 protein homolog"
FT /id="PRO_0000256241"
FT DOMAIN 163..348
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..483
FT /note="Interaction with alpha-tubulin, gamma-tubulin, BIRC5
FT and FBXO5"
FT /evidence="ECO:0000269|PubMed:16439210,
FT ECO:0000269|PubMed:16764853"
FT REGION 49..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..693
FT /note="Dimerization"
FT REGION 377..810
FT /note="Targeting to the centrosomes"
FT REGION 487..810
FT /note="Interaction with AURKB and INCENP"
FT /evidence="ECO:0000269|PubMed:16764853"
FT REGION 756..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 406..716
FT /evidence="ECO:0000255"
FT COMPBIAS 99..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 594
FT /note="Breakpoint for translocation to form EVI5-TRNG10
FT fusion protein"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97366"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 776
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97366"
FT VAR_SEQ 448
FT /note="K -> KESASLADRLIQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19077034"
FT /id="VSP_056828"
FT VARIANT 82
FT /note="D -> V (in dbSNP:rs1064580)"
FT /evidence="ECO:0000269|PubMed:19077034,
FT ECO:0000269|PubMed:9618176"
FT /id="VAR_047753"
FT VARIANT 336
FT /note="I -> V (in dbSNP:rs2391199)"
FT /evidence="ECO:0000269|PubMed:19077034,
FT ECO:0000269|PubMed:9618176"
FT /id="VAR_028890"
FT VARIANT 612
FT /note="Q -> H (in dbSNP:rs11808092)"
FT /id="VAR_028891"
FT CONFLICT 94
FT /note="R -> I (in Ref. 1; AAC16031 and 2; BAH16618)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="K -> Q (in Ref. 1; AAC16031)"
FT /evidence="ECO:0000305"
FT CONFLICT 714
FT /note="R -> K (in Ref. 1; AAC16031)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 810 AA; 92949 MW; 4A2CC99A9192F632 CRC64;
MVTNKMTAAF RNPSGKQVAT DKVAEKLSST LSWVKNTVSH TVSQMASQVA SPSTSLHTTS
SSTTLSTPAL SPSSPSQLSP DDLELLAKLE EQNRLLETDS KSLRSVNGSR RNSGSSLVSS
SSASSNLSHL EEDSWILWGR IVNEWEDVRK KKEKQVKELV HKGIPHHFRA IVWQLLCSAQ
SMPIKDQYSE LLKMTSPCEK LIRRDIARTY PEHNFFKEKD SLGQEVLFNV MKAYSLVDRE
VGYCQGSAFI VGLLLMQMPE EEAFCVFVKL MQDYRLRELF KPSMAELGLC MYQFECMIQE
HLPELFVHFQ SQSFHTSMYA SSWFLTIFLT TFPLPIATRI FDIFMSEGLE IVFRVGLALL
QMNQAELMQL DMEGMLQHFQ KVIPHQFDGV PDKLIQAAYQ VKYNSKKMKK LEKEYTTIKT
KEMEEQVEIK RLRTENRLLK QRIETLEKHK CSSNYNEDFV LQLEKELVQA RLSEAESQCA
LKEMQDKVLD IEKRNNSLPD ENNIARLQEE LIAVKLREAE AIMGLKELRQ QVKDLEEHWQ
RHLARTTGRW KDPPKKNAMN ELQDELMTIR LREAETQAEI REIKQRMMEM ETQNQINSNH
LRRAEQEVIS LQEKVQYLSA QNKGLLTQLS EAKRKQAEIE CKNKEEVMAV RLREADSIAA
VAELRQHIAE LEIQKEEGKL QGQLNKSDSN QYIGELKDQI AELNHELRCL KGQRGFSGQP
PFDGIHIVNH LIGDDESFHS SDEDFIDNSL QETGVGFPLH GKSGSMSLDP AVADGSESET
EDSVLETRES NQVVQKERPP RRRESYSTTV
