CE295_MOUSE
ID CE295_MOUSE Reviewed; 2412 AA.
AC Q8BQ48; Q0VF60; Q3UYP6; Q571B9; Q8CCJ2; Q8CDA9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 3.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Centrosomal protein of 295 kDa {ECO:0000305};
GN Name=Cep295 {ECO:0000250|UniProtKB:Q9C0D2};
GN Synonyms=Kiaa1731 {ECO:0000250|UniProtKB:Q9C0D2};
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-114 AND 1173-2412 (ISOFORM 2),
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1296-2412 (ISOFORM 6), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2006-2412 (ISOFORM 5).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, Spinal ganglion, and Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 317-2412 (ISOFORM 4).
RC TISSUE=Pancreatic islet;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1251-2412 (ISOFORM 3).
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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).
CC -!- FUNCTION: Centriole-enriched microtubule-binding protein involved in
CC centriole biogenesis. Essential for the generation of the distal
CC portion of new-born centrioles in a CENPJ- and CEP120-mediated
CC elongation dependent manner during the cell cycle S/G2 phase after
CC formation of the initiating cartwheel structure. Required for the
CC recruitment of centriolar proteins, such as POC1B, POC5 and CEP135,
CC into the distal portion of centrioles. Also required for centriole-to-
CC centrosome conversion during mitotic progression, but is dispensable
CC for cartwheel removal or centriole disengagement. Binds to and
CC stabilizes centriolar microtubule. {ECO:0000250|UniProtKB:Q9C0D2}.
CC -!- SUBUNIT: Interacts (via ALMS motif) with microtubules; this interaction
CC is direct. {ECO:0000250|UniProtKB:Q9C0D2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250|UniProtKB:Q9C0D2}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q9C0D2}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q9C0D2}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9C0D2}. Note=Associates with both of the
CC converted centrioles during G1 but becomes more enriched at the newly
CC formed daughter (or unconverted) centrioles during S, G2, and early M
CC phases. In early S phase, localized at the procentriolar microtubule
CC wall and enriched at the proximal ends of the centrioles in CENPJ- and
CC CEP135-dependent manner. Colocalizes with SASS6 and CEP250 proteins.
CC Colocalizes with CEP135 and CEP192 at the centrosomes. Associates with
CC interphase microtubules and mitotic spindles. Colocalizes with
CC centriolar acetylated tubulin. {ECO:0000250|UniProtKB:Q9C0D2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q8BQ48-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BQ48-2; Sequence=VSP_032298;
CC Name=3;
CC IsoId=Q8BQ48-3; Sequence=VSP_032294;
CC Name=4;
CC IsoId=Q8BQ48-4; Sequence=VSP_032292, VSP_032293, VSP_032294;
CC Name=5;
CC IsoId=Q8BQ48-5; Sequence=VSP_032295, VSP_032296, VSP_032297;
CC Name=6;
CC IsoId=Q8BQ48-6; Sequence=VSP_032294, VSP_032296, VSP_032297;
CC -!- DOMAIN: The N-terminal and the ALMS motif-containing C-terminal regions
CC are essential for CEP295-mediated centriole elongation.
CC {ECO:0000250|UniProtKB:Q9C0D2}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI18969.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC27153.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD90195.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC154296; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK030838; BAC27153.1; ALT_INIT; mRNA.
DR EMBL; AK032664; BAC27977.1; -; mRNA.
DR EMBL; AK051561; BAC34674.2; -; mRNA.
DR EMBL; AK134513; BAE22166.1; -; mRNA.
DR EMBL; AK220270; BAD90195.1; ALT_INIT; mRNA.
DR EMBL; BC118968; AAI18969.1; ALT_INIT; mRNA.
DR CCDS; CCDS52727.1; -. [Q8BQ48-3]
DR RefSeq; NP_795950.2; NM_176976.4. [Q8BQ48-3]
DR AlphaFoldDB; Q8BQ48; -.
DR SMR; Q8BQ48; -.
DR BioGRID; 235442; 6.
DR STRING; 10090.ENSMUSP00000123788; -.
DR iPTMnet; Q8BQ48; -.
DR PhosphoSitePlus; Q8BQ48; -.
DR EPD; Q8BQ48; -.
DR PaxDb; Q8BQ48; -.
DR PRIDE; Q8BQ48; -.
DR ProteomicsDB; 281161; -. [Q8BQ48-1]
DR ProteomicsDB; 281162; -. [Q8BQ48-2]
DR ProteomicsDB; 281163; -. [Q8BQ48-3]
DR ProteomicsDB; 281164; -. [Q8BQ48-4]
DR ProteomicsDB; 281165; -. [Q8BQ48-5]
DR ProteomicsDB; 281166; -. [Q8BQ48-6]
DR Ensembl; ENSMUST00000098979; ENSMUSP00000096578; ENSMUSG00000046111. [Q8BQ48-3]
DR Ensembl; ENSMUST00000161132; ENSMUSP00000123788; ENSMUSG00000046111. [Q8BQ48-1]
DR GeneID; 319675; -.
DR KEGG; mmu:319675; -.
DR UCSC; uc009ofv.2; mouse. [Q8BQ48-4]
DR UCSC; uc009ofw.3; mouse. [Q8BQ48-1]
DR UCSC; uc009ofy.2; mouse. [Q8BQ48-6]
DR CTD; 85459; -.
DR MGI; MGI:2442521; Cep295.
DR eggNOG; ENOG502QSZR; Eukaryota.
DR GeneTree; ENSGT00940000153123; -.
DR HOGENOM; CLU_001093_0_0_1; -.
DR InParanoid; Q8BQ48; -.
DR OrthoDB; 97863at2759; -.
DR PhylomeDB; Q8BQ48; -.
DR TreeFam; TF331536; -.
DR BioGRID-ORCS; 319675; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Cep295; mouse.
DR PRO; PR:Q8BQ48; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BQ48; protein.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:1990498; C:mitotic spindle microtubule; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0007099; P:centriole replication; ISS:UniProtKB.
DR GO; GO:1903724; P:positive regulation of centriole elongation; ISS:UniProtKB.
DR GO; GO:0010825; P:positive regulation of centrosome duplication; ISS:UniProtKB.
DR GO; GO:1904951; P:positive regulation of establishment of protein localization; ISS:UniProtKB.
DR GO; GO:1901985; P:positive regulation of protein acetylation; ISS:UniProtKB.
DR GO; GO:0046599; P:regulation of centriole replication; IBA:GO_Central.
DR InterPro; IPR029560; CEP295.
DR PANTHER; PTHR21553:SF25; PTHR21553:SF25; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..2412
FT /note="Centrosomal protein of 295 kDa"
FT /id="PRO_0000324596"
FT REGION 1..540
FT /note="Necessary for centriole targeting and microtubule
FT association"
FT /evidence="ECO:0000250|UniProtKB:Q9C0D2"
FT REGION 600..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1158..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1216..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1820..1895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1916..1937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2028..2048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2089..2111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2367..2412
FT /note="ALMS motif"
FT COILED 63..84
FT /evidence="ECO:0000255"
FT COILED 114..134
FT /evidence="ECO:0000255"
FT COILED 209..273
FT /evidence="ECO:0000255"
FT COILED 489..535
FT /evidence="ECO:0000255"
FT COILED 563..592
FT /evidence="ECO:0000255"
FT COILED 811..841
FT /evidence="ECO:0000255"
FT COILED 1300..1327
FT /evidence="ECO:0000255"
FT COILED 1448..1493
FT /evidence="ECO:0000255"
FT COMPBIAS 739..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1158..1177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1834..1862
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1919..1933
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2029..2048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0D2"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0D2"
FT MOD_RES 1573
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0D2"
FT VAR_SEQ 655..1237
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_032292"
FT VAR_SEQ 1341..1692
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_032293"
FT VAR_SEQ 1916..1995
FT /note="Missing (in isoform 3, isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.3"
FT /id="VSP_032294"
FT VAR_SEQ 2042
FT /note="Y -> YQ (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032295"
FT VAR_SEQ 2286..2287
FT /note="ET -> VS (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032296"
FT VAR_SEQ 2288..2412
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032297"
FT VAR_SEQ 2363..2412
FT /note="ATSGSLQEAFMTRQTLTERSYQRQREIWNKTRLPQTKVSKEKLPTGCTGS
FT -> GKPLISLRTLSTHVGMKATHNFSQIL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032298"
FT CONFLICT 1344
FT /note="P -> T (in Ref. 2; BAC27977)"
FT /evidence="ECO:0000305"
FT CONFLICT 1872
FT /note="L -> M (in Ref. 2; BAC27977)"
FT /evidence="ECO:0000305"
FT CONFLICT 1924
FT /note="H -> R (in Ref. 2; BAC27153)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2412 AA; 272779 MW; 58D8E5F8DF469D7D CRC64;
MKRKGMNTKL RLSPSEEAFI LKEDYERRRK LRLLQVREQE RGIAFQIREG IKQRRSQQVS
HLAEELRAKW EEAQSQKIQN LEKLYLASLR HMGDGHRQAK ENEPDLDALS RRAAERKRKA
EVRHKEALKV QKNQKEMLMK QKTRHIKARK EAVLVEKQRS AKMARLPPPV PSPFENIDVN
RIPSLKTNSS TYHHISTFVS RQMGTKQPDA HLAAEEEARR VERLRKQAAQ ERVKQFERAH
VRGSQAMKKI HLAQNQERLM EELKQLQKED LARRRQTVAQ MPPQMLELPY RRSEMKEDRQ
RELEFAFEDM YNADRKVKGN LILHLKPEPL PTISDQLQDE ELDLSMEQEN QVPLAAKIQQ
IPSRILFKRL LNKIRSQKSL WTIKSVSEDE GEVTSSIIEI ESKVPSVDSG AIITEERTAA
SFEQEQVTDS DRLTIESGPL SSEDKPLYYK AGTGREQAMA VSPPATAVAQ SSVLLHPQEE
AVRIRMSLRR KQIMEIEEQK QKQLELLEQI EQQKLRLETD CFRAQLEEQR KQADQPEVCC
APMSHAMISD EDSHRQMIRN YQHQLLQQNR LHKETVETAR KRLLEYQTVL KERSPSLSAS
ALVPDSVVSG PPQQSYKPAA ASDSWDPSQR LKLSPSKYQP VQPSQIPALE QSHIQVPRHG
HITQRQGKMA VSEMLGKQPV ESQERQWQFS QVETHQGDYE FVLKDSHSLS RTLSYVRPQT
LQDAREVSKP PRVIICQSLD SQQISSEDSE NISSKPSEPS PFLPLVPERP FTSLPVKFHS
GTIHKPFTTI NQSVISQMHD QPLSSSETIT AQQGDLRFLQ EQLELQKKVL QARQEAREKL
LLCTQKELGQ QTGLPVFLPS PAGNIFSSLP SASAESGNFQ TSSTKSDATV SSDNMDRLWD
SSQPISSQQT HLEFLQEQSS VETDNLQARR EAQEVLFAHT QNTLEKIVRS EQAGSSLPHQ
VAQQSFSSLT LADTQSKKIQ KQPLPANKKG LLPSQSEVSK AQDGSSGFLQ QTLPLQNTLK
LLQEQLTRQR SMIPPRRDGQ ETLLLYKESC SEDSEAGPVE SLSSVVVQHA DASRAVSEVP
KRLQDVYSSE EENRVLSSHL ITHGFPQHSL QRQEHFTPLQ EETHIQRLIL GARKNNEEFA
PKQNELEKGL CSQQTDALSS PSQVTDWGTS RGSVSVRSDR TDPLRHFKIP AFRERLVRVS
QHTFPLQDNL QEHQEWVDTE KESFQSSPLT PENPSSQQTG FSSFKASLRL PSCVSLPSAD
SGITQHPLST ESDSKVKSSH LQIPELQHRL SKISQLIPPQ QDSLKALQEQ LATQREAIIH
SRQEAHEETL REWKEKIFPE QVGPFSPLIP QHSLASFPVS DTERAQELCS TNSDTISSGY
PEMLELPDRT LGLSHTALPQ QNNLTAHPEH LHAQTNFFHS TEKAQEGLVF PRPCQFEEMS
AEHFIQPQHD DLKALQQQLD MQREAIRSGQ EMQEKMLLQR LNKLEQRISS KQISSSLFSS
QVALPIANSD GTLQSFPTKS NETELLGSQD EYLSFSQPRL PLQNNMTEQL DLEKVFHKEL
LLHKQKSQNK SESSEHSLPP LFLSKEIEHP FISLPFAESK SKSICELYLS DKKHAAPNDA
VIPRLQDRLL SCSQPVLTQQ DNMSLQKQLN LQRETLHSRQ KAQEELLVQR QTSLQQQIQR
HRETLKNFFN VSQARNPTDE NDLEMQKREQ LGGWFPHTQG LTWGDAGQGS ANGEQPRADV
HAEHNGESLA KELSGRASKP PVSKVKCVLD LNQHELSTIQ EVESPASGRI SMPGKAEFYQ
DRDPLRVSVS REQSFLESPL AHDPFGCHQP PAQENSKSHD DNAEAVKVKK SDVEDHAVLS
HAVSKEEACT NLGPLGKPDD EAETQEISQE PLSSVTVSTG SFLSYEITDL SLTDPESFSE
QTEHLEQEST NKQEETDPLS IAVPSVIYQQ QHSLGAHNSL LPMEEESTSD HTHVQQIMDN
DVNEANLIPD KRDFQVPAVD LDFRELEHIF PHLHRQLFKP LEPHLDFDLS SPGTSQEDSD
FYQSSESSSE KHVKALSTGT ICFPALTAKS HSPNPRLNQL DINLAHATTE GSEQSFQQLR
PEFSSQESQH ADLPSIYSIE ARGPSQRMEN QNYSEMLQNK KKSLSLQPST EDLTPACSSS
DTALFDQLHL QHSTPCASVS SECSVKLLES REEVLGFEEL SRRAVTMSQR LTEDENVVLP
INPHVGRVEK EASVQGSNPL SIQNEKPIQN FIETDTTEAV GNVCQLAQAE HILKSCPFRS
PIPIWETDTG YGIMEEPDLT LVSNSDISIT ETDLANLTLE DREDNEAQFF QAGVVLPTSS
METSVCGAVS EPYVDQPTVA PSATSGSLQE AFMTRQTLTE RSYQRQREIW NKTRLPQTKV
SKEKLPTGCT GS
