ELYS_DROME
ID ELYS_DROME Reviewed; 2111 AA.
AC Q9VWE6; Q95TR2;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Protein ELYS homolog;
GN Name=Elys {ECO:0000312|FlyBase:FBgn0031052};
GN ORFNames=CG14215 {ECO:0000312|FlyBase:FBgn0031052};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 944-2111.
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200; SER-1274; SER-1522;
RP SER-1525; SER-1551; SER-1692; THR-1695; SER-1831; SER-1834; SER-1863;
RP SER-1870; SER-1880; SER-1886; THR-1888; SER-1934; SER-1939; SER-1950;
RP SER-1953; THR-1956; SER-1957; SER-1958; THR-1962; SER-1975; SER-1982;
RP SER-2025; SER-2062; SER-2065 AND SER-2068, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1840, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=28366641; DOI=10.1016/j.molcel.2017.02.020;
RA Pascual-Garcia P., Debo B., Aleman J.R., Talamas J.A., Lan Y., Nguyen N.H.,
RA Won K.J., Capelson M.;
RT "Metazoan nuclear pores provide a scaffold for poised genes and mediate
RT induced enhancer-promoter contacts.";
RL Mol. Cell 66:63-76(2017).
RN [8]
RP INTERACTION WITH PIWI, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28472469; DOI=10.1093/nar/gkx355;
RA Ilyin A.A., Ryazansky S.S., Doronin S.A., Olenkina O.M., Mikhaleva E.A.,
RA Yakushev E.Y., Abramov Y.A., Belyakin S.N., Ivankin A.V., Pindyurin A.V.,
RA Gvozdev V.A., Klenov M.S., Shevelyov Y.Y.;
RT "Piwi interacts with chromatin at nuclear pores and promiscuously binds
RT nuclear transcripts in Drosophila ovarian somatic cells.";
RL Nucleic Acids Res. 45:7666-7680(2017).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF 367-GLY--HIS-2111 AND 372-VAL--HIS-2111.
RX PubMed=29773558; DOI=10.1534/g3.118.200361;
RA Hirai K., Wang Z., Miura K., Hayashi T., Awasaki T., Wada M., Keira Y.,
RA Ishikawa H.O., Sawamura K.;
RT "Genetic Analyses of Elys Mutations in Drosophila Show Maternal-Effect
RT Lethality and Interactions with Nucleoporin Genes.";
RL G3 (Bethesda) 8:2421-2431(2018).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=31784359; DOI=10.1016/j.molcel.2019.10.017;
RA Gozalo A., Duke A., Lan Y., Pascual-Garcia P., Talamas J.A., Nguyen S.C.,
RA Shah P.P., Jain R., Joyce E.F., Capelson M.;
RT "Core Components of the Nuclear Pore Bind Distinct States of Chromatin and
RT Contribute to Polycomb Repression.";
RL Mol. Cell 0:0-0(2019).
CC -!- FUNCTION: Component of the nuclear pore complex (PubMed:28366641,
CC PubMed:29773558). Binds to transcriptionally active chromatin including
CC regulatory regions (PubMed:28366641, PubMed:31784359).
CC {ECO:0000269|PubMed:28366641, ECO:0000269|PubMed:29773558,
CC ECO:0000269|PubMed:31784359}.
CC -!- SUBUNIT: Interacts with piwi. {ECO:0000269|PubMed:28472469}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:28366641, ECO:0000269|PubMed:28472469}. Chromosome
CC {ECO:0000269|PubMed:28366641, ECO:0000269|PubMed:31784359}.
CC Note=Interacts with chromatin. {ECO:0000269|PubMed:28366641,
CC ECO:0000269|PubMed:31784359}.
CC -!- TISSUE SPECIFICITY: Expressed in ovaries (at protein level).
CC {ECO:0000269|PubMed:28472469}.
CC -!- DEVELOPMENTAL STAGE: Expressed in larval brains (at protein level).
CC {ECO:0000269|PubMed:28366641}.
CC -!- SIMILARITY: Belongs to the ELYS/MEL-28 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL13830.1; Type=Erroneous initiation; 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; AE014298; AAF48996.2; -; Genomic_DNA.
DR EMBL; BT044469; ACH92534.1; -; mRNA.
DR EMBL; AY058601; AAL13830.1; ALT_INIT; mRNA.
DR RefSeq; NP_001285454.1; NM_001298525.1.
DR RefSeq; NP_608340.2; NM_134496.3.
DR AlphaFoldDB; Q9VWE6; -.
DR SMR; Q9VWE6; -.
DR BioGRID; 59267; 10.
DR IntAct; Q9VWE6; 9.
DR MINT; Q9VWE6; -.
DR STRING; 7227.FBpp0074515; -.
DR iPTMnet; Q9VWE6; -.
DR PaxDb; Q9VWE6; -.
DR PRIDE; Q9VWE6; -.
DR DNASU; 32971; -.
DR EnsemblMetazoa; FBtr0074746; FBpp0074515; FBgn0031052.
DR EnsemblMetazoa; FBtr0345016; FBpp0311267; FBgn0031052.
DR GeneID; 32971; -.
DR KEGG; dme:Dmel_CG14215; -.
DR UCSC; CG14215-RA; d. melanogaster.
DR CTD; 32971; -.
DR FlyBase; FBgn0031052; Elys.
DR VEuPathDB; VectorBase:FBgn0031052; -.
DR eggNOG; ENOG502QU0D; Eukaryota.
DR HOGENOM; CLU_232699_0_0_1; -.
DR InParanoid; Q9VWE6; -.
DR OMA; IVISWHS; -.
DR OrthoDB; 121312at2759; -.
DR PhylomeDB; Q9VWE6; -.
DR Reactome; R-DME-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR BioGRID-ORCS; 32971; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 32971; -.
DR PRO; PR:Q9VWE6; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0031052; Expressed in egg cell and 23 other tissues.
DR ExpressionAtlas; Q9VWE6; baseline and differential.
DR Genevisible; Q9VWE6; DM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR025151; ELYS_dom.
DR Pfam; PF13934; ELYS; 1.
PE 1: Evidence at protein level;
KW Chromosome; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Translocation; Transport.
FT CHAIN 1..2111
FT /note="Protein ELYS homolog"
FT /id="PRO_0000372641"
FT REGION 1..490
FT /note="Seven-bladed beta propeller repeats"
FT /evidence="ECO:0000250"
FT REGION 1076..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1201..1229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1274..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1414..1574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1661..1710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1758..2111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1290..1324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1422..1447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1466..1504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1521..1556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1662..1686
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1786..1841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1849..1884
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1892..1916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1921..1939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1940..1987
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2014..2028
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2045..2062
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2063..2097
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1274
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1522
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1525
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1551
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1692
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1695
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1831
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1834
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1840
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 1863
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1870
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1880
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1886
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1888
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1934
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1939
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1950
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1953
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1956
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1957
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1958
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1962
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1975
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1982
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 2025
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 2062
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 2065
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 2068
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 367..2111
FT /note="Missing: Viable, male-fertile, female-sterile.
FT Female embryos lack mitotic progression with terminal
FT arrest at the first cleavage division."
FT /evidence="ECO:0000269|PubMed:29773558"
FT MUTAGEN 372..2111
FT /note="Missing: Viable, male-fertile, female-sterile.
FT Female embryos lack mitotic progression with terminal
FT arrest at the first cleavage division."
FT /evidence="ECO:0000269|PubMed:29773558"
SQ SEQUENCE 2111 AA; 235187 MW; A24392E6A2014616 CRC64;
MEWHEVELDG SRTIAFPERI VPGFGREPSA HLDAAEYLGG IIRDGQWGWV TWRYGSDATL
LVCSMSTGDY LSWHCFWSES DDLGPRKSIR CVEELFPGEH ERPAMLAICL ESWNSGDQRP
IDCPLSTQVL IYAIRNSQVL RRFDLHGITC SALTFLDKRI YGLTRLRRFK GCLAVATEEG
TVLLVDLNSD SLQASTQRRS LCSPSSKDEP SDGNLYFVSS EESKRQLSSK LTHCRSKGAH
LAVRMDVASI GISCLMGISM APGYAAGLED GRILIYDLIN FDVTTDLNSP VKRKGVNRAV
KRMCLIMPPD DPKPCFYICA LYQNIDVLQM MLHSVCYRGS YRDRETHTIR FKDYRSRTVR
NRQILDGGIC SVIGCATAST FSFAGDNGTL LIVISWHSSA DKKNKLVLFD INQWYKDEMP
TSVHKNEVPN YMSGYILSGL QTGLALDLRS TTILHFVSLQ RYDEHFYPNS LTFDCSLLTP
TGKRYYAQDG VQHRFLNALR CDRATLFLRP QIYHEDIVRL RLLPQFCELN PNATFSKIAM
YELILSVALE HNCGALLNDC ARSWMDGSFL CNMIDNTQLS LSTLTNWILK RAGQIKTRCS
ELCHGIFDYG GYPLDQRERR EFQVLSGQLR ELVRLQSYIV EQGRRRLTSS ILDDCRANER
ALKTVLEYQR VLLWFIDHGL LPEGQHMDNL VPGEQAFVRL QHEYSEKRAQ GKILYIDSLG
KRASFPEPYP PDSLHAYIHL MLSPDIELCH KHALILYLLM DLNQQLVGRF QIAFQLDKDL
ATSLRCFWYL DHGDYERGVE ELYKEPAPAK NLKSWQMRLL IDKLLAEGAV KAAKKVVSRP
PGPLSSALHM KVLLANENIT EAFQIARLDD DEDGQPLLER FFRHCIEIRR FKVLAELYLR
EPEERLLYSL LRQCRSRQTD CVQLIMLLQK SKFIEAVSFM DEVAAERERD ESSNTILPAY
SATMGPVTQN IAGTYLRIRD TLEPYQKTGP LEPFSCQLVK QNASGQLGGI FQSSAVSAHW
ATQCESPPKM TPVSIQSKIG YTNVPFLRHA QYGHSELPLP RRIVKPVPHQ VVEKRQRELE
DQRTNLQDQR QLGTERPNKR PCLMVERMVE DVKDYVRSIR EKSSNQMEQE EVKQNEATNL
LQPPNFLQAR QSTTIRQSSS SPQPIPPILK GSGAVDAVKR APPVATFTAL AGPKRFRFVP
PIPLRTDKSD KSTEMGSEGA AEGEEETDEI IVEIESRSEP RSACSYESDE EDEFLSPLVS
ANVSLVDPVP SRNSPHYFAP PAGPQPRNSL LHGGNGSGSK IGTATGSESS SGFGSFSTVQ
PAQTSSHSQF VPTVCSSKMG ETQSQVFSSG SCGIKISERT TICGEMESTD LGAELTAAPS
AQWSLPSARP AIQGHHQMMD TTLGMSTYDV ASLEQQDTQD VENEEELKLG DTKSLEEQQN
PQDEQKPEQE QDQDEDQAQE PLATGGQLAF LSNSEGTAQE PLSSPIYSLS SEDSNVSSAG
IRNPMLPTLH TDDPMYSIVV ESPGSITTSR SVTHTPTSFL PSDTNVSQTS SPQAPHGEDG
DGTPISLYRA NSLETVDDLD TTKGSLEEEE EYDDDDCVIA LDGTEVRGYV ARPQQSAASS
SAELFAFKDE CQEEAAGVPS PFLSLGATVN SDSDVADTIV LDSDEETAKE KDTQPEQRKD
WPMEEETPSN ESVATVEFSE QKQPRADMDI GMEVDAVPDV LEVLEVPEME PLPVLSDVDI
EMAVDEVPNV LEVLEVPELE PLPAGQATQS SGLGEIPEED VDAEAEEQVV VKVEHVADEQ
PKEGDKTESK EASEEETQHN PEPLLPEEED SRHSLKLIFS GDEDEEEQDV PTRAIHTLRP
RRSFTEHQDS PRTLRPRRVS QEHRDSPTPV AGRTMSLRST DAPTLSPASN PPVSTPKRRG
LQHKYLLEVI DEHSPSDLSL PRTRSRTRLS VDSEATSSRP GTPTMTKARG KRATSQAPPT
ASPSVRRSLR GHSEPPAALS AQLVRKPKTA RAGVRSRKTS SGVQSPVAVS PTPIDAPIDV
PDSTAPEEEQ PRLRRTARRR ISELSDQSAN GTGDLRSEAS SSRTGSKSNS AASTQNRELR
PRLRRTSKSE H
