CE290_DROME
ID CE290_DROME Reviewed; 1978 AA.
AC Q9W0M1; Q8T3H8;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Centrosomal protein cep290 {ECO:0000312|FlyBase:FBgn0035168};
GN Name=cep290 {ECO:0000312|FlyBase:FBgn0035168};
GN ORFNames=CG13889 {ECO:0000312|FlyBase:FBgn0035168};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|EMBL:AAM12244.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1045.
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM12244.1};
RC TISSUE=Testis {ECO:0000312|EMBL:AAM12244.1};
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 [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP 1472-LEU--GLU-1978.
RX PubMed=25447994; DOI=10.1016/j.cub.2014.09.047;
RA Basiri M.L., Ha A., Chadha A., Clark N.M., Polyanovsky A., Cook B.,
RA Avidor-Reiss T.;
RT "A migrating ciliary gate compartmentalizes the site of axoneme assembly in
RT Drosophila spermatids.";
RL Curr. Biol. 24:2622-2631(2014).
RN [5] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP 1472-LEU--GLU-1978.
RX PubMed=27646273; DOI=10.1083/jcb.201603086;
RA Vieillard J., Paschaki M., Duteyrat J.L., Augiere C., Cortier E.,
RA Lapart J.A., Thomas J., Durand B.;
RT "Transition zone assembly and its contribution to axoneme formation in
RT Drosophila male germ cells.";
RL J. Cell Biol. 214:875-889(2016).
RN [6] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=27577095; DOI=10.1242/jcs.194621;
RA Pratt M.B., Titlow J.S., Davis I., Barker A.R., Dawe H.R., Raff J.W.,
RA Roque H.;
RT "Drosophila sensory cilia lacking MKS proteins exhibit striking defects in
RT development but only subtle defects in adults.";
RL J. Cell Sci. 129:3732-3743(2016).
RN [7] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF 1472-LEU--GLU-1978.
RX PubMed=30013109; DOI=10.1038/s41556-018-0132-1;
RA Jana S.C., Mendonca S., Machado P., Werner S., Rocha J., Pereira A.,
RA Maiato H., Bettencourt-Dias M.;
RT "Differential regulation of transition zone and centriole proteins
RT contributes to ciliary base diversity.";
RL Nat. Cell Biol. 20:928-941(2018).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31821146; DOI=10.7554/elife.49307;
RA Lapart J.A., Gottardo M., Cortier E., Duteyrat J.L., Augiere C., Mange A.,
RA Jerber J., Solassol J., Gopalakrishnan J., Thomas J., Durand B.;
RT "Dzip1 and Fam92 form a ciliary transition zone complex with cell type
RT specific roles in Drosophila.";
RL Elife 8:0-0(2019).
RN [9]
RP FUNCTION, INTERACTION WITH DZIP1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 1-MET--GLU-650; 1-MET--GLU-1384; 157-LYS--GLU-1978; 651-GLU--GLU-1978;
RP 1385-GLY--GLU-1978 AND 1386-GLU--GLU-1978.
RX PubMed=33370260; DOI=10.1371/journal.pbio.3001034;
RA Wu Z., Pang N., Zhang Y., Chen H., Peng Y., Fu J., Wei Q.;
RT "CEP290 is essential for the initiation of ciliary transition zone
RT assembly.";
RL PLoS Biol. 18:e3001034-e3001034(2020).
CC -!- FUNCTION: Essential for ciliogenesis in sensory neurons and
CC spermatocytes (PubMed:25447994, PubMed:30013109, PubMed:31821146,
CC PubMed:33370260). During neuron and spermatocyte ciliogenesis,
CC essential for initiating transition zone (TZ) assembly and is required
CC for the formation of diverse connections between microtubules and
CC between microtubules and the membrane (PubMed:25447994,
CC PubMed:30013109, PubMed:31821146, PubMed:33370260). Regulates TZ
CC assembly by recruiting DZIP1 to the plasma membrane where it promotes
CC early ciliary membrane formation resulting in the initiation of TZ
CC assembly (PubMed:31821146, PubMed:33370260).
CC {ECO:0000269|PubMed:25447994, ECO:0000269|PubMed:30013109,
CC ECO:0000269|PubMed:31821146, ECO:0000269|PubMed:33370260}.
CC -!- SUBUNIT: Interacts (via N-terminus) with DZIP1.
CC {ECO:0000269|PubMed:33370260}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000269|PubMed:25447994, ECO:0000269|PubMed:27577095,
CC ECO:0000269|PubMed:27646273, ECO:0000269|PubMed:30013109,
CC ECO:0000269|PubMed:33370260}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:25447994}.
CC Note=Localizes at the transition zone (TZ), a region between the basal
CC body and the ciliary axoneme in the olfactory, auditory and
CC spermatocyte system (PubMed:30013109, PubMed:33370260). In sensory
CC neurons, localizes to the transition zone at the tip of the mother
CC centriole (PubMed:25447994). In germ cells, component of the
CC spermatocyte primary cilium and spermatid ciliary cap (PubMed:25447994,
CC PubMed:27646273, PubMed:27577095). {ECO:0000269|PubMed:25447994,
CC ECO:0000269|PubMed:27577095, ECO:0000269|PubMed:27646273,
CC ECO:0000269|PubMed:30013109, ECO:0000269|PubMed:33370260}.
CC -!- TISSUE SPECIFICITY: Expressed in sensory neurons type I and in germ
CC cells (at protein level). {ECO:0000269|PubMed:25447994,
CC ECO:0000269|PubMed:27577095, ECO:0000269|PubMed:27646273,
CC ECO:0000269|PubMed:30013109}.
CC -!- DOMAIN: The C-terminus orients towards the microtubules and the N-
CC terminus orients towards the membrane in a 9-fold symmetric manner.
CC {ECO:0000269|PubMed:30013109}.
CC -!- DISRUPTION PHENOTYPE: Adults are severely uncoordinated and exhibit
CC disorganized spermatid cysts with dispersed nuclei, likely as a
CC consequence of the severe defects in axonemal elongation
CC (PubMed:31821146). RNAi-mediated knockdown in developing sensory
CC neurons results in defective microtubule (MT)-microtubule (MT) and
CC microtubule-membrane connections (Y linkers) ultimately affecting cilia
CC formation leading to olfactory and gravitaxis behavioral defects
CC (PubMed:30013109). RNAi-mediated knockdown in spermatocytes results in
CC defective transition zone assembly including increased distance between
CC microtubules (MT) and MT-membrane causing defective cilia
CC (PubMed:30013109). {ECO:0000269|PubMed:30013109,
CC ECO:0000269|PubMed:31821146}.
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DR EMBL; AE014296; AAF47422.2; -; Genomic_DNA.
DR EMBL; AE014296; AGB93922.1; -; Genomic_DNA.
DR EMBL; AY095510; AAM12244.1; -; mRNA.
DR RefSeq; NP_001261227.1; NM_001274298.1.
DR RefSeq; NP_612064.1; NM_138220.1.
DR AlphaFoldDB; Q9W0M1; -.
DR SMR; Q9W0M1; -.
DR IntAct; Q9W0M1; 5.
DR STRING; 7227.FBpp0304992; -.
DR PaxDb; Q9W0M1; -.
DR EnsemblMetazoa; FBtr0072586; FBpp0072483; FBgn0035168.
DR EnsemblMetazoa; FBtr0332752; FBpp0304992; FBgn0035168.
DR GeneID; 38099; -.
DR KEGG; dme:Dmel_CG13889; -.
DR UCSC; CG13889-RA; d. melanogaster.
DR CTD; 80184; -.
DR FlyBase; FBgn0035168; cep290.
DR VEuPathDB; VectorBase:FBgn0035168; -.
DR eggNOG; ENOG502QPTZ; Eukaryota.
DR HOGENOM; CLU_235006_0_0_1; -.
DR InParanoid; Q9W0M1; -.
DR OMA; FHDDQQR; -.
DR OrthoDB; 27774at2759; -.
DR PhylomeDB; Q9W0M1; -.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR SignaLink; Q9W0M1; -.
DR BioGRID-ORCS; 38099; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 38099; -.
DR PRO; PR:Q9W0M1; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0035168; Expressed in testis and 7 other tissues.
DR GO; GO:0034451; C:centriolar satellite; IBA:GO_Central.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0061822; C:ciliary cap; IDA:FlyBase.
DR GO; GO:0035869; C:ciliary transition zone; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0097711; P:ciliary basal body-plasma membrane docking; IMP:UniProtKB.
DR GO; GO:1905349; P:ciliary transition zone assembly; IMP:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:FlyBase.
DR GO; GO:0061824; P:cytosolic ciliogenesis; IDA:FlyBase.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:FlyBase.
DR InterPro; IPR026201; Cep290.
DR PANTHER; PTHR18879; PTHR18879; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Coiled coil;
KW Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..1978
FT /note="Centrosomal protein cep290"
FT /evidence="ECO:0000305"
FT /id="PRO_0000445799"
FT REGION 1..650
FT /note="Necessary and sufficient for function in
FT ciliogenesis, transition zone (TZ) assembly, and
FT recruitment of DZP1 and Mks1 to the TZ. Also required for
FT subcellular localization to the cilium basal body"
FT /evidence="ECO:0000269|PubMed:33370260"
FT REGION 271..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1313..1397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1684..1714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1859..1884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 76..384
FT /evidence="ECO:0000255"
FT COILED 471..505
FT /evidence="ECO:0000255"
FT COILED 853..887
FT /evidence="ECO:0000255"
FT COILED 922..970
FT /evidence="ECO:0000255"
FT COILED 1192..1233
FT /evidence="ECO:0000255"
FT COILED 1405..1439
FT /evidence="ECO:0000255"
FT COILED 1501..1654
FT /evidence="ECO:0000255"
FT COILED 1726..1935
FT /evidence="ECO:0000255"
FT COMPBIAS 274..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 1..1384
FT /note="Missing: In CEP290-C; no effect on cilium basal body
FT localization."
FT /evidence="ECO:0000269|PubMed:33370260"
FT MUTAGEN 1..650
FT /note="Missing: In CEP290-M; abolishes cilium basal body
FT localization; when associated with 1385-G--E-1978."
FT /evidence="ECO:0000269|PubMed:33370260"
FT MUTAGEN 157..1978
FT /note="Missing: In CEP290-1; in olfactory and auditory
FT neurons, transition zones (TZ) fail to form leading to the
FT disassociation of the basal bodies from plasma membrane at
FT later stages cliliogenesis, abnormal elongation of the
FT axoneme and consequently complete loss of cilia. As a
FT consequence, adults are uncoordinated and have severe
FT defects in touch and hearing. In testes, flagellar axonemes
FT are almost completely lost and sperm cyst elongation is
FT severely defective. As a consequence, mature sperms do not
FT develop and so males are completely infertile."
FT /evidence="ECO:0000269|PubMed:33370260"
FT MUTAGEN 651..1978
FT /note="Missing: In CEP290-N; no effect on cilium basal body
FT localization however expression in more restricted within
FT the transition zone of auditory cilia. When overexpressed
FT in CEP290-1 mutants, rescues defects in ciliogenesis, basal
FT body docking, transition zone (TZ) assembly, and
FT recruitment of DZP1 and Mks1 to the TZ. It does not rescue
FT uncoordination."
FT /evidence="ECO:0000269|PubMed:33370260"
FT MUTAGEN 1385..1978
FT /note="Missing: In CEP290-N+M; no effect on cilium basal
FT body localization. In CEP290-M; abolishes cilium basal body
FT localization; when associated with 1-M--E-650."
FT /evidence="ECO:0000269|PubMed:33370260"
FT MUTAGEN 1386..1978
FT /note="Missing: In olfactory and auditory neurons,
FT transition zones (TZ) fail to form, ciliary axonemes are
FT lost and DZIP1 expression is significantly reduced
FT resulting in uncoordination and severe defects in touch and
FT hearing. No effect on connection between the basal bodies
FT and plasma membrane. Mild defects in spermatid development
FT and male fertility. In spermatocyte cilia there is no
FT significant reduction in DZIP1 expression."
FT /evidence="ECO:0000269|PubMed:33370260"
FT MUTAGEN 1472..1978
FT /note="Missing: Results in motor defects including crossed
FT legs and inability to stand or hold wings erect. In sensory
FT neurons, results in failure to form a transition zone. In
FT cilia, shows severe proprioception defects including
FT defective mechanoreceptor current (MRC) but normal
FT transepithelial potential (TEP). In germ cells, results in
FT defective transition zone assembly and ciliary cap
FT structure; the defects include increased distance between
FT microtubules (MT) and between MT and membrane and it is
FT associated with longer cilium basal body. This leads to
FT ultrastructural axoneme defects without compromising the
FT attachment of spermatocyte centrioles to the membrane."
FT /evidence="ECO:0000269|PubMed:25447994,
FT ECO:0000269|PubMed:30013109"
FT CONFLICT 79
FT /note="L -> M (in Ref. 3; AAM12244)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="A -> V (in Ref. 3; AAM12244)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="A -> G (in Ref. 3; AAM12244)"
FT /evidence="ECO:0000305"
FT CONFLICT 829
FT /note="P -> H (in Ref. 3; AAM12244)"
FT /evidence="ECO:0000305"
FT CONFLICT 942
FT /note="E -> G (in Ref. 3; AAM12244)"
FT /evidence="ECO:0000305"
FT CONFLICT 1035
FT /note="I -> V (in Ref. 3; AAM12244)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1978 AA; 227962 MW; 5FFEEF7F9B22977D CRC64;
MSMDIPETVS LRKFRDFSAR QKQELYETLL ELAESIDELP KKSLRKTLEL TLAVLEYKGE
QVQQLQESAA GGLSSDRRLQ DENEKLKRML QKLEDERDGL KSKAKELGEE IRQLELRLQE
AAQQAEISDK DSSDPLSELD KQEQLLQNID SKNKHIKRLL KEIETLQNQN IAQSKTIVLH
ERELQTIKAN LVQLSQDITK VEQERKSLKQ KEQQQALEIT RLEGNLTFLE VEREKQEVEM
RQFLDKYEAK SLGWRQALDD RDKEVERLKK QLEGKSISSG QTNSSNSQSQ QEEEHAKLRQ
LLESREQRIE KLEEKIKSMA EEMVSSTRAM NQLCQEKERA HDPEQPRACC QMIEERLREA
TARCQQLSEM LEAAEQDNVL KSQQALHAIS ALEAYKRDED GLIPALRRCS GLEQKVAARD
KQLRAYIQEL NSLHEVVQEN ELLRRKLHIP DDVVIMAKNV HSKQRNKDKQ IERLTLKLRT
SEELRLQLKL EKSELRRKLL ELQQDSPQTL NESLQAPSEV GEVPHSVHLE NSPRRGQGDG
AASSEMQNRY DEVLAENETL RSGMYEILEK LREYDATSEH ITIDSDLLRR LIEALPGGTT
TPQRLQGQLL ELKAREEALR QLLEQQNYSD SETGELSSVH SLCEVPEIAE EHPVEEDAVL
NTATRPSSPT EATMGLRRPT VPDPEEKPTN EALAELSILR KHYDELRLHM SADGSDLMNR
NQELHDQMIA LELQLEQQRN SYSYMRRDYD QLLTETRKQE LRFIDDKASL ARQLEHSKSE
LCEAREELEQ VNRRNLYTAE EQQKLEHRNA ILSMQLGQAM EQLLGELKPT EICAEYGIIR
ENYQLDYITA QDFEEQQQEL LTWRSKQAEL QRETKQLEGL LHVANEQIHS QQRLLNEITD
NHINLRHLVA DLQSSSDEKL MLAKVQRDLD SVKAECSRLE TEREKLQLKA DCLQTQLEAS
ELSLKQTQQD FQQERTNSDI KHKFLQHSLF MLKDKYAKFT PLVFLTNFVF AYQKFQRRLE
EEQVQQRHRD HTALIDEVTA VVQAKIGLNE ESSQQLVKLI KSETQTRLLE QRCEILQAKQ
EELVRELGEL RMSQATDTEH WSTIQALFGE GEPRSQLKVD AETNTDAVAP NLAMRRAVQL
IDRESSPIGS PLRKHPHLDT ATQTLEAQVE FSETAVQTNG ILSQQNQAVQ TADAVEDNRR
DSRAELQKMQ ETLQEANQRI EILGKQLEAS RSESRESASP QGGVVEKTIL SFHTLLLEKD
QSIQKYQDLL QTERDQSQQA LSKQVAENES LRATVNNLNF NIKTKDAEIQ GLKEKLRQKP
EVPVERNPST DSRSSSSSDS SVNELTDEKI EELFESSSVE RPPQEELEVP VEAGPENIVT
EEPEGEEEKQ DTEELKEVPT LHKQIKDLKD KLEYSERSLK TREEEVDILK EKLKLCQERE
KSVESTVNPE LDQLRIFLDE KDKHIKDLMD TLKNFHDDQQ RYIKDTSNFS EDQIAKLAAD
LNRTEATNKI YHTQMEALRR QLANVTQREK QARDLSQSLR QQLLKRPVVS IKTELNARVK
NENQLKRIQQ LELDLDEARG QLQRQQTLLE AKRTRSANEV QLWEKQKRYQ QQAEKTKARL
EETELALEKT RALLQAARTT IARLEKDKQI LESKLGRNGP PSNSSGGNNL KCCRTPSCPN
LQHVGVSKFA PSPSESPETY TGPSSECSSP AHHHTQIFDQ SQLDLIEALK SRIELQQRKI
IAMELEGRGS NALTTELEKL QERCQAIEAQ NIRLEARNLQ LQLDSDLLRQ GDSSDRLQKR
IKHLEDYIMA LKEEMARNES RRELGSGLKV STNQGQSAEQ TILSLRNLVE KLRSENKFLK
DGRRSTESRS SMDSTPAEAA RLQQQHAEAL EKISALQQEL QKRTTKCSQC GGRSKDAANE
ELKFIKEQLV KKTQLLQKAK VLLTRAAAKE KVLREQLALW KRKCSELQNV PVIDEISE
