CP250_MOUSE
ID CP250_MOUSE Reviewed; 2414 AA.
AC Q60952; E9QMB2; Q2I8G3; Q3UTR4; Q6PFF6; Q8BLC6;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Centrosome-associated protein CEP250;
DE AltName: Full=250 kDa centrosomal protein;
DE Short=Cep250;
DE AltName: Full=Centrosomal Nek2-associated protein 1;
DE Short=C-Nap1;
DE AltName: Full=Centrosomal protein 2;
DE AltName: Full=Intranuclear matrix protein;
GN Name=Cep250; Synonyms=Cep2, Inmp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND INTERACTION WITH
RP CROCC.
RC STRAIN=C57BL/6 X 129/Sv;
RX PubMed=16339073; DOI=10.1091/mbc.e05-10-0943;
RA Yang J., Adamian M., Li T.;
RT "Rootletin interacts with C-Nap1 and may function as a physical linker
RT between the pair of centrioles/basal bodies in cells.";
RL Mol. Biol. Cell 17:1033-1040(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-686 AND 1966-2414.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Corpora quadrigemina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1806-2414.
RC TISSUE=Macrophage;
RX PubMed=8950169; DOI=10.1016/s0167-4781(96)00132-7;
RA Menz K., Radomski N., Jost E.;
RT "INMP, a novel intranuclear matrix protein related to the family of
RT intermediate filament-like proteins: molecular cloning and sequence
RT analysis.";
RL Biochim. Biophys. Acta 1309:14-20(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1872-2414.
RC STRAIN=C57BL/6J; 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP INTERACTION WITH NIN.
RX PubMed=27565344; DOI=10.1016/j.cell.2016.07.025;
RA Zhang X., Chen M.H., Wu X., Kodani A., Fan J., Doan R., Ozawa M., Ma J.,
RA Yoshida N., Reiter J.F., Black D.L., Kharchenko P.V., Sharp P.A.,
RA Walsh C.A.;
RT "Cell-type-specific alternative splicing governs cell fate in the
RT developing cerebral cortex.";
RL Cell 166:1147-1162(2016).
RN [8]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=28005958; DOI=10.1371/journal.pone.0168966;
RA de Castro-Miro M., Tonda R., Escudero-Ferruz P., Andres R.,
RA Mayor-Lorenzo A., Castro J., Ciccioli M., Hidalgo D.A.,
RA Rodriguez-Ezcurra J.J., Farrando J., Perez-Santonja J.J., Cormand B.,
RA Marfany G., Gonzalez-Duarte R.;
RT "Novel candidate genes and a wide spectrum of structural and point
RT mutations responsible for inherited retinal dystrophies revealed by exome
RT sequencing.";
RL PLoS ONE 11:E0168966-E0168966(2016).
RN [9]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 187-ARG--ARG-2414.
RX PubMed=30998843; DOI=10.1002/humu.23759;
RA Huang X.F., Xiang L., Fang X.L., Liu W.Q., Zhuang Y.Y., Chen Z.J.,
RA Shen R.J., Cheng W., Han R.Y., Zheng S.S., Chen X.J., Liu X., Jin Z.B.;
RT "Functional characterization of CEP250 variant identified in nonsyndromic
RT retinitis pigmentosa.";
RL Hum. Mutat. 40:1039-1045(2019).
CC -!- FUNCTION: May be involved in ciliogenesis. Probably plays an important
CC role in centrosome cohesion during interphase.
CC {ECO:0000250|UniProtKB:Q9BV73}.
CC -!- SUBUNIT: Monomer and homodimer (Probable). Forms a complex in vitro
CC with both NEK2 kinase and the PPP1CC catalytic subunit of protein
CC phosphatase 1 (PP1) (By similarity). Interacts with CEP135 (By
CC similarity). Interacts with CROCC/rootletin (PubMed:16339073).
CC Interacts with CNTLN (By similarity). Interacts with NIN (via C-
CC terminus) (PubMed:27565344). {ECO:0000250|UniProtKB:Q9BV73,
CC ECO:0000269|PubMed:16339073, ECO:0000269|PubMed:27565344, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:16339073}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:16339073}.
CC Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000269|PubMed:16339073, ECO:0000269|PubMed:30998843}. Cell
CC projection, cilium, photoreceptor outer segment
CC {ECO:0000269|PubMed:28005958}. Photoreceptor inner segment
CC {ECO:0000269|PubMed:30998843}. Note=Component of the core centrosome
CC where it is found at the proximal ends of centrioles.
CC -!- TISSUE SPECIFICITY: Expressed in the retina.
CC {ECO:0000269|PubMed:28005958}.
CC -!- PTM: C-terminal part is phosphorylated by NEK2. Dephosphorylated in
CC vitro by the PP1 phosphatase (By similarity). {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB41824.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DQ148475; ABA29340.1; -; mRNA.
DR EMBL; AL833786; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK045557; BAC32417.1; -; mRNA.
DR EMBL; AK139187; BAE23916.1; -; mRNA.
DR EMBL; U33198; AAB41824.1; ALT_FRAME; mRNA.
DR EMBL; BC057582; AAH57582.1; -; mRNA.
DR CCDS; CCDS50771.1; -.
DR RefSeq; NP_001123471.1; NM_001129999.1.
DR RefSeq; NP_032409.3; NM_008383.3.
DR RefSeq; NP_796191.2; NM_177217.3.
DR AlphaFoldDB; Q60952; -.
DR SMR; Q60952; -.
DR BioGRID; 200766; 14.
DR IntAct; Q60952; 8.
DR STRING; 10090.ENSMUSP00000105248; -.
DR iPTMnet; Q60952; -.
DR PhosphoSitePlus; Q60952; -.
DR EPD; Q60952; -.
DR jPOST; Q60952; -.
DR MaxQB; Q60952; -.
DR PaxDb; Q60952; -.
DR PeptideAtlas; Q60952; -.
DR PRIDE; Q60952; -.
DR ProteomicsDB; 283438; -.
DR Antibodypedia; 26072; 85 antibodies from 20 providers.
DR Ensembl; ENSMUST00000094421; ENSMUSP00000091988; ENSMUSG00000038241.
DR GeneID; 16328; -.
DR KEGG; mmu:16328; -.
DR UCSC; uc008nlu.2; mouse.
DR CTD; 11190; -.
DR MGI; MGI:108084; Cep250.
DR VEuPathDB; HostDB:ENSMUSG00000038241; -.
DR eggNOG; ENOG502QTBY; Eukaryota.
DR GeneTree; ENSGT00940000161056; -.
DR InParanoid; Q60952; -.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR BioGRID-ORCS; 16328; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Cep250; mouse.
DR PRO; PR:Q60952; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q60952; protein.
DR Bgee; ENSMUSG00000038241; Expressed in retinal neural layer and 129 other tissues.
DR ExpressionAtlas; Q60952; baseline and differential.
DR Genevisible; Q60952; MM.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0031616; C:spindle pole centrosome; IDA:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0010457; P:centriole-centriole cohesion; ISO:MGI.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IMP:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; ISO:MGI.
DR GO; GO:1905515; P:non-motile cilium assembly; ISO:MGI.
DR GO; GO:1904781; P:positive regulation of protein localization to centrosome; ISO:MGI.
DR GO; GO:0008104; P:protein localization; ISO:MGI.
DR GO; GO:0033365; P:protein localization to organelle; ISO:MGI.
DR GO; GO:0030997; P:regulation of centriole-centriole cohesion; ISO:MGI.
PE 1: Evidence at protein level;
KW Cell cycle; Cell projection; Cilium; Cilium biogenesis/degradation;
KW Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..2414
FT /note="Centrosome-associated protein CEP250"
FT /id="PRO_0000089488"
FT REGION 356..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1269..1303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2050..2071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2194..2238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2275..2317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2390..2414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 91..153
FT /evidence="ECO:0000255"
FT COILED 248..357
FT /evidence="ECO:0000255"
FT COILED 400..1165
FT /evidence="ECO:0000255"
FT COILED 1237..2200
FT /evidence="ECO:0000255"
FT COILED 2231..2290
FT /evidence="ECO:0000255"
FT COILED 2320..2345
FT /evidence="ECO:0000255"
FT COMPBIAS 356..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1269..1287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1288..1303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2194..2226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2275..2290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2294..2317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BV73"
FT MOD_RES 2389
FT /note="Phosphoserine; by NEK2"
FT /evidence="ECO:0000250|UniProtKB:Q9BV73"
FT MOD_RES 2393
FT /note="Phosphoserine; by NEK2"
FT /evidence="ECO:0000250|UniProtKB:Q9BV73"
FT MUTAGEN 187..2414
FT /note="Missing: Knockin mutant mice show retinal
FT morphological anomalies and altered electroretinographic
FT responses to light stimuli."
FT /evidence="ECO:0000269|PubMed:30998843"
FT CONFLICT 91
FT /note="E -> K (in Ref. 3; BAC32417)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="S -> L (in Ref. 1; ABA29340)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="H -> R (in Ref. 1; ABA29340)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="K -> R (in Ref. 1; ABA29340)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="G -> D (in Ref. 1; ABA29340)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="K -> R (in Ref. 1; ABA29340)"
FT /evidence="ECO:0000305"
FT CONFLICT 615
FT /note="E -> G (in Ref. 1; ABA29340)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="Q -> R (in Ref. 1; ABA29340)"
FT /evidence="ECO:0000305"
FT CONFLICT 1837
FT /note="A -> P (in Ref. 4; AAB41824)"
FT /evidence="ECO:0000305"
FT CONFLICT 1864
FT /note="Q -> R (in Ref. 4; AAB41824)"
FT /evidence="ECO:0000305"
FT CONFLICT 1924..1925
FT /note="QA -> RP (in Ref. 4; AAB41824)"
FT /evidence="ECO:0000305"
FT CONFLICT 1966
FT /note="Q -> E (in Ref. 3; BAE23916)"
FT /evidence="ECO:0000305"
FT CONFLICT 1974
FT /note="Q -> H (in Ref. 5; AAH57582)"
FT /evidence="ECO:0000305"
FT CONFLICT 2003
FT /note="S -> R (in Ref. 1; ABA29340 and 4; AAB41824)"
FT /evidence="ECO:0000305"
FT CONFLICT 2040
FT /note="K -> E (in Ref. 1; ABA29340 and 4; AAB41824)"
FT /evidence="ECO:0000305"
FT CONFLICT 2105
FT /note="R -> S (in Ref. 1; ABA29340 and 4; AAB41824)"
FT /evidence="ECO:0000305"
FT CONFLICT 2192
FT /note="R -> S (in Ref. 4; AAB41824)"
FT /evidence="ECO:0000305"
FT CONFLICT 2218
FT /note="G -> E (in Ref. 4; AAB41824)"
FT /evidence="ECO:0000305"
FT CONFLICT 2221
FT /note="S -> P (in Ref. 1; ABA29340 and 4; AAB41824)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2414 AA; 276814 MW; 7B76E9E781D731CC CRC64;
METGSPGLNM KPQSLQLVLE GQVLALQQQM AENQAASWRK LKNSQEAQKR QATLVRKLQA
KVLQYRSWCQ DLEKRLEATG GLIPQRWESV EEPNLEQLLI RLEEEQQRCE SLVEVNTELR
LHMEKADVVN KALQEDVEKL TVDWSRARDE LVRKESQWRM EQEFFKGYLR GEHGRLLNLW
REVVTFRRHF LKMKSATDRD LTELKAEHAR LSGSLLTCCL RLTLRAQSRE SSGSGRTEES
EPARLLLLVA KTQALEKEAH EKSQELMQLK SHGDLEKAEL QDRVTELSAL LTQSQKQNED
YEKMVKALRE TMEILETNHA ELMEHEASLS RNAQEEKLSL QQVIKAITQA LASVEEEDTV
TQSSGHEDSL QSDCNGLSQF DPQDPDRALT LVQSVLTRRQ QAVQDLRQQL SGCQEAMSFL
QQQHDQWEEE GRALREKLQK LTGERDALAG QTVGLQGEVD SLSRERELLQ KARGELQQQL
EVLEQEAWRL RRMNMELQLQ GDSAQGEKLE QQEELHLAVR ERERLQETLV GLEAKQSESL
SELLTLREAL ESSRLEGELL KQERVEVAAA LARAEQSIVE LSGSENSLKA EVADLRAAAV
KLGALNEALA LDKVELNQQL LQLEQENQSL CSRVEAAEQL RSALQVDLAE AERRREALWE
KKTQLETQLQ KAEEAGAELQ AELRGTREEK EELKDKLSEA HHQQETATAH LEQLHQDAER
QEETLARAVQ EKEALVRERA ALEVRLQAVE RDRQDLTEHV LGLRSAKEQL ESNLFEAQQQ
NSVIQVTKGQ LEVQIQTIIQ AKEVIQGEVK CLKLELDAER TRAEQEWDAV ARQLAQAEQE
GQASLERQKV AHEEEVNRLQ EKWEKERSWL QQELDKTLET LERERAELET KLREQQTEME
AIRAQREEER SQADSALYQM QLETEKERVS LLETLLRTQK ELADASQQLE RLRQDMKIQK
LKEQETTGML QAQLQETQQE LKEAAQQHRD DLAAFQKDKL DLQKQVEDLM SQLVAHDDSQ
RLVKEEIEEK VKVAQECSRI QKELEKENAS LALSLVEKEK RLLILQEADS VRQQELSSLR
QDIQEAQEGQ RELGVQVELL RQEVKEKEAD FVAREAQLLE ELEASRVAEQ QLRASLWAQE
AKATQLQLQL RSTESQLEAL VAEQQPENQA QAQLASLCSV LQQALGSACE SRPELRGGGD
SAPTLWGPDP DQNGASRLFK RWSLPTALSP EAVALALQKL HQDVWKARQA RDDLRDQVQK
LVQRLTDTEA QKSQVHSELQ DLQRQLSQSQ EEKSKWEGRQ NSLESELRDL HETAASLQSR
LRQAELQKME AQNDRELLQA SKEKLSAQVE HLQACVAEAQ AQADAAAVLE EDLRTARSAL
KLKNEELESE RERAQALQEQ GELKVAQGKA LQENLALLAQ TLSNREREVE TLQAEVQELE
KQREMQKAAL ELLSLDLKKR SREVDLQQEQ IQELEQCRSV LEHLPMAVQE REQKLSVQRD
QIRELENDRE AQRSVLEHQL LDLEQKAQVI ESQRGQIQDL KKQLGTLECL ALELEESHHK
VESQQKMITE LEGQREMQRV ALTHLTLDLE ERSQELQAQS SQLHELENHS THLAKELQER
DQEVTSQRQQ IDELQKQQEQ LAQALERKGQ ELVLQKERIQ VLEDQRTLQT KILEEDLEQI
KHSLRERSQE LASQWQLVHE RADDGKSPSK GQRGSLEHLK LILRDKEKEV ECQQERIQEL
QGHMGQLEQQ LQGLHRKVGE TSLLLTHREQ ETATLQQHLQ EAKEQGELRE QVLQGQLEEA
QRDLAQRDHE LETLRQEKQQ TQDQEESMKL KTSALQAALE QAHATLKERQ GELEEHREQV
RRLQEELEVE GRQVRALEEV LGDLRAESRE HEKAVLALQQ RCAEQAQEHE AEARTLQDSW
LQAQATLTEQ EQELAALRAE NQYSRRQEEA AVSQAEALQE ALSKAQAALQ EKEQSLLEQA
ELSHTLEAST AALQATLDTC QASARQLEEA LRIREGEIQA QALQHHEVTQ HLQQELCQKK
EELRQLLEKA GARRSQENGI QEKQSLEQER QEETRRLLES LKELQLTVAQ REEEILMLRE
ASSPRHRALP AEKPALQPLP AQQELERLQT ALRQTEAREI EWREKAQDLA LSLAQSKASI
SSLQEITMFL QASVLERESE QQRLQEELVL SRQALEEQQS GGPHSTSRAD QGPKVGQGSQ
SGEVETEPSP GVEEKERLTQ RLERLQQAVA ELEVDRSKLQ CHNAQLRTAL EQVERERRKL
KRDSVRASRA GSLEARETMT SSPTQQDGRG SQRGSSDSVL VVELQREVAL LRAQLALERK
QRQDYIARSV QTSRELAGLH HSLSHSLLTV AQAPEATVLE AETRKLDESL NQSLTSPGPC
LLHPSLDTTQ NTHR
