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Centrosomal protein of 152 kDa (Cep152)

 CE152_HUMAN             Reviewed;        1710 AA.
O94986; E7ER66; Q17RV1; Q6NTA0;
29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
26-JUN-2013, sequence version 4.
30-AUG-2017, entry version 136.
RecName: Full=Centrosomal protein of 152 kDa;
Short=Cep152;
Name=CEP152; Synonyms=KIAA0912;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10048485; DOI=10.1093/dnares/5.6.355;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 5:355-364(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Heart, Lung, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PLK4.
PubMed=21059844; DOI=10.1083/jcb.201007107;
Cizmecioglu O., Arnold M., Bahtz R., Settele F., Ehret L.,
Haselmann-Weiss U., Antony C., Hoffmann I.;
"Cep152 acts as a scaffold for recruitment of Plk4 and CPAP to the
centrosome.";
J. Cell Biol. 191:731-739(2010).
[6]
FUNCTION, AND INTERACTION WITH PLK4 AND CENPJ.
PubMed=20852615; DOI=10.1038/nature09445;
Dzhindzhev N.S., Yu Q.D., Weiskopf K., Tzolovsky G.,
Cunha-Ferreira I., Riparbelli M., Rodrigues-Martins A.,
Bettencourt-Dias M., Callaini G., Glover D.M.;
"Asterless is a scaffold for the onset of centriole assembly.";
Nature 467:714-718(2010).
[7]
SUBCELLULAR LOCATION.
PubMed=22020124; DOI=10.1038/emboj.2011.378;
Tang C.J., Lin S.Y., Hsu W.B., Lin Y.N., Wu C.T., Lin Y.C.,
Chang C.W., Wu K.S., Tang T.K.;
"The human microcephaly protein STIL interacts with CPAP and is
required for procentriole formation.";
EMBO J. 30:4790-4804(2011).
[8]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CINP, AND VARIANT
SCKL5 ARG-667.
PubMed=21131973; DOI=10.1038/ng.725;
Kalay E., Yigit G., Aslan Y., Brown K.E., Pohl E., Bicknell L.S.,
Kayserili H., Li Y., Tuysuz B., Nurnberg G., Kiess W., Koegl M.,
Baessmann I., Buruk K., Toraman B., Kayipmaz S., Kul S., Ikbal M.,
Turner D.J., Taylor M.S., Aerts J., Scott C., Milstein K., Dollfus H.,
Wieczorek D., Brunner H.G., Hurles M., Jackson A.P., Rauch A.,
Nurnberg P., Karaguzel A., Wollnik B.;
"CEP152 is a genome maintenance protein disrupted in Seckel
syndrome.";
Nat. Genet. 43:23-26(2011).
[9]
INTERACTION WITH CEP63, AND SUBCELLULAR LOCATION.
PubMed=21983783; DOI=10.1038/ng.971;
Sir J.H., Barr A.R., Nicholas A.K., Carvalho O.P., Khurshid M.,
Sossick A., Reichelt S., D'Santos C., Woods C.G., Gergely F.;
"A primary microcephaly protein complex forms a ring around parental
centrioles.";
Nat. Genet. 43:1147-1153(2011).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1241, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[11]
INTERACTION WITH CDK5RAP2.
PubMed=24613305; DOI=10.1016/j.cub.2014.01.067;
Firat-Karalar E.N., Rauniyar N., Yates J.R. III, Stearns T.;
"Proximity interactions among centrosome components identify
regulators of centriole duplication.";
Curr. Biol. 24:664-670(2014).
[12]
FUNCTION, INTERACTION WITH CDK5RAP2; WDR62; CEP63 AND CEP131, AND
SUBCELLULAR LOCATION.
PubMed=26297806; DOI=10.7554/eLife.07519;
Kodani A., Yu T.W., Johnson J.R., Jayaraman D., Johnson T.L.,
Al-Gazali L., Sztriha L., Partlow J.N., Kim H., Krup A.L.,
Dammermann A., Krogan N., Walsh C.A., Reiter J.F.;
"Centriolar satellites assemble centrosomal microcephaly proteins to
recruit CDK2 and promote centriole duplication.";
Elife 4:0-0(2015).
[13]
SUBCELLULAR LOCATION.
PubMed=26337392; DOI=10.1091/mbc.E15-04-0235;
Van de Mark D., Kong D., Loncarek J., Stearns T.;
"MDM1 is a microtubule-binding protein that negatively regulates
centriole duplication.";
Mol. Biol. Cell 26:3788-3802(2015).
[14]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-60 IN COMPLEX WITH PLK4,
FUNCTION, AND MUTAGENESIS OF GLU-21.
PubMed=24997597; DOI=10.1038/nsmb.2846;
Park S.Y., Park J.E., Kim T.S., Kim J.H., Kwak M.J., Ku B., Tian L.,
Murugan R.N., Ahn M., Komiya S., Hojo H., Kim N.H., Kim B.Y.,
Bang J.K., Erikson R.L., Lee K.W., Kim S.J., Oh B.H., Yang W.,
Lee K.S.;
"Molecular basis for unidirectional scaffold switching of human Plk4
in centriole biogenesis.";
Nat. Struct. Mol. Biol. 21:696-703(2014).
[15]
VARIANT MCPH9 PRO-265, AND SUBCELLULAR LOCATION.
PubMed=20598275; DOI=10.1016/j.ajhg.2010.06.003;
Guernsey D.L., Jiang H., Hussin J., Arnold M., Bouyakdan K., Perry S.,
Babineau-Sturk T., Beis J., Dumas N., Evans S.C., Ferguson M.,
Matsuoka M., Macgillivray C., Nightingale M., Patry L., Rideout A.L.,
Thomas A., Orr A., Hoffmann I., Michaud J.L., Awadalla P., Meek D.C.,
Ludman M., Samuels M.E.;
"Mutations in centrosomal protein CEP152 in primary microcephaly
families linked to MCPH4.";
Am. J. Hum. Genet. 87:40-51(2010).
[16]
VARIANT ILE-793.
PubMed=20547088; DOI=10.1016/j.legalmed.2010.04.001;
Yuasa I., Umetsu K., Matsusue A., Nishimukai H., Harihara S.,
Fukumori Y., Saitou N., Jin F., Chattopadhyay P.K., Henke L.,
Henke J.;
"A Japanese-specific allele in the GALNT11 gene.";
Leg. Med. 12:208-211(2010).
-!- FUNCTION: Necessary for centrosome duplication; the function seems
also to involve CEP63, CDK5RAP2 and WDR62 through a stepwise
assembled complex at the centrosome that recruits CDK2 required
for centriole duplication (PubMed:26297806). Acts as a molecular
scaffold facilitating the interaction of PLK4 and CENPJ, 2
molecules involved in centriole formation (PubMed:21059844,
PubMed:20852615). Proposed to snatch PLK4 away from PLK4:CEP92
complexes in early G1 daughter centriole and to reposition PLK4 at
the outer boundary of a newly forming CEP152 ring structure
(PubMed:24997597). Also plays a key role in deuterosome-mediated
centriole amplification in multiciliated that can generate more
than 100 centrioles (By similarity). Overexpression of CEP152 can
drive amplification of centrioles (PubMed:20852615).
{ECO:0000250|UniProtKB:A2AUM9, ECO:0000250|UniProtKB:Q498G2,
ECO:0000269|PubMed:20852615, ECO:0000269|PubMed:21059844,
ECO:0000269|PubMed:21131973}.
-!- SUBUNIT: Interacts (via N-terminus) with PLK4; the interaction is
mutally exclusive with a PLK4:CEP192 interaction (PubMed:21059844,
PubMed:20852615, PubMed:24997597). Interacts (via C-terminus) with
CENPJ (via-N-terminus) (PubMed:20852615). Interacts with CINP
(PubMed:21131973). Interacts with CDK5RAP2, WDR62, CEP63 and
CEP131 (PubMed:21983783, PubMed:24613305, PubMed:26297806). CEP63,
CDK5RAP2, CEP152, WDR62 are proposed to form a stepwise assembled
complex at the centrosome forming a ring near parental centrioles
(PubMed:26297806). Interacts with DEUP1; this interaction recruits
CEP152 to the deuterosome. The interactions with CEP63 and DEUP1
are mutually exclusive (By similarity).
{ECO:0000250|UniProtKB:A2AUM9, ECO:0000269|PubMed:20852615,
ECO:0000269|PubMed:21059844, ECO:0000269|PubMed:21131973,
ECO:0000269|PubMed:21983783, ECO:0000269|PubMed:24613305,
ECO:0000269|PubMed:26297806}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:20598275,
ECO:0000269|PubMed:21059844, ECO:0000269|PubMed:21131973,
ECO:0000269|PubMed:21983783, ECO:0000269|PubMed:26297806}.
Cytoplasm, cytoskeleton, microtubule organizing center,
centrosome, centriole {ECO:0000269|PubMed:21983783,
ECO:0000269|PubMed:22020124, ECO:0000269|PubMed:26297806,
ECO:0000269|PubMed:26337392}. Note=Colocalizes with CDK5RAP2,
WDR62 and CEP63 in a discrete ring around the proximal end of the
parental centriole. At this site, a cohesive structure is
predicted to engage parental centrioles and procentrioles
(PubMed:21983783, PubMed:26297806). Localizes to the deuterosome
(By similarity). Localizes to pericentriolar material (PCM)
(PubMed:26337392). {ECO:0000250|UniProtKB:Q498G2,
ECO:0000269|PubMed:21983783, ECO:0000269|PubMed:26297806,
ECO:0000269|PubMed:26337392}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=4;
IsoId=O94986-4; Sequence=Displayed;
Note=Gene prediction based on EST data.;
Name=1;
IsoId=O94986-1; Sequence=VSP_035981, VSP_035983, VSP_035984;
Name=2;
IsoId=O94986-2; Sequence=VSP_035983, VSP_035984;
Name=3;
IsoId=O94986-3; Sequence=VSP_047002;
Note=No experimental confirmation available.;
-!- DISEASE: Microcephaly 9, primary, autosomal recessive (MCPH9)
[MIM:614852]: A disease defined as a head circumference more than
3 standard deviations below the age-related mean. Brain weight is
markedly reduced and the cerebral cortex is disproportionately
small. Despite this marked reduction in size, the gyral pattern is
relatively well preserved, with no major abnormality in cortical
architecture. Affected individuals are mentally retarded. Primary
microcephaly is further defined by the absence of other syndromic
features or significant neurological deficits due to degenerative
brain disorder. {ECO:0000269|PubMed:20598275}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Seckel syndrome 5 (SCKL5) [MIM:613823]: A rare autosomal
recessive disorder characterized by proportionate dwarfism of
prenatal onset associated with low birth weight, growth
retardation, severe microcephaly with a bird-headed like
appearance, and mental retardation. {ECO:0000269|PubMed:21131973}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the CEP152 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH69186.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAA74935.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AB020719; BAA74935.1; ALT_INIT; mRNA.
EMBL; AC012379; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC022084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC084757; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC069186; AAH69186.1; ALT_SEQ; mRNA.
EMBL; BC117182; AAI17183.1; -; mRNA.
CCDS; CCDS42033.1; -. [O94986-3]
CCDS; CCDS58361.1; -. [O94986-4]
RefSeq; NP_001181927.1; NM_001194998.1. [O94986-4]
RefSeq; NP_055800.2; NM_014985.3. [O94986-3]
RefSeq; XP_006720500.1; XM_006720437.3. [O94986-4]
UniGene; Hs.443005; -.
UniGene; Hs.597323; -.
PDB; 4N7V; X-ray; 2.76 A; C=1-60.
PDBsum; 4N7V; -.
ProteinModelPortal; O94986; -.
SMR; O94986; -.
BioGrid; 116642; 111.
DIP; DIP-31701N; -.
IntAct; O94986; 98.
MINT; MINT-7034544; -.
STRING; 9606.ENSP00000382271; -.
iPTMnet; O94986; -.
PhosphoSitePlus; O94986; -.
BioMuta; CEP152; -.
EPD; O94986; -.
PaxDb; O94986; -.
PeptideAtlas; O94986; -.
PRIDE; O94986; -.
Ensembl; ENST00000325747; ENSP00000321000; ENSG00000103995. [O94986-1]
Ensembl; ENST00000380950; ENSP00000370337; ENSG00000103995. [O94986-4]
Ensembl; ENST00000399334; ENSP00000382271; ENSG00000103995. [O94986-3]
GeneID; 22995; -.
KEGG; hsa:22995; -.
UCSC; uc001zwy.4; human. [O94986-4]
CTD; 22995; -.
DisGeNET; 22995; -.
GeneCards; CEP152; -.
GeneReviews; CEP152; -.
HGNC; HGNC:29298; CEP152.
HPA; HPA039408; -.
MalaCards; CEP152; -.
MIM; 613529; gene.
MIM; 613823; phenotype.
MIM; 614852; phenotype.
neXtProt; NX_O94986; -.
OpenTargets; ENSG00000103995; -.
Orphanet; 2512; Autosomal recessive primary microcephaly.
Orphanet; 808; Seckel syndrome.
PharmGKB; PA142672126; -.
eggNOG; ENOG410IGHC; Eukaryota.
eggNOG; ENOG410XQAW; LUCA.
GeneTree; ENSGT00630000089915; -.
HOGENOM; HOG000111522; -.
HOVERGEN; HBG096403; -.
InParanoid; O94986; -.
KO; K16728; -.
OMA; DDHRNKI; -.
OrthoDB; EOG091G0PGF; -.
TreeFam; TF332017; -.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
ChiTaRS; CEP152; human.
GeneWiki; CEP152; -.
GenomeRNAi; 22995; -.
PRO; PR:O94986; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000103995; -.
CleanEx; HS_CEP152; -.
ExpressionAtlas; O94986; baseline and differential.
Genevisible; O94986; HS.
GO; GO:0005814; C:centriole; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0098536; C:deuterosome; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0000242; C:pericentriolar material; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0007099; P:centriole replication; ISS:UniProtKB.
GO; GO:0051298; P:centrosome duplication; IMP:UniProtKB.
GO; GO:0097711; P:ciliary basal body docking; TAS:Reactome.
GO; GO:0098535; P:de novo centriole assembly involved in multi-ciliated epithelial cell differentiation; ISS:UniProtKB.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
InterPro; IPR029598; Cep152.
PANTHER; PTHR10337:SF15; PTHR10337:SF15; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cilium biogenesis/degradation;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
Disease mutation; Dwarfism; Mental retardation; Phosphoprotein;
Polymorphism; Primary microcephaly; Reference proteome.
CHAIN 1 1710 Centrosomal protein of 152 kDa.
/FTId=PRO_0000089462.
REGION 1 60 Interaction with PLK4.
{ECO:0000269|PubMed:24997597}.
COILED 234 490 {ECO:0000255}.
COILED 615 664 {ECO:0000255}.
COILED 700 772 {ECO:0000255}.
COILED 902 993 {ECO:0000255}.
COILED 1170 1241 {ECO:0000255}.
MOD_RES 1241 1241 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 89 181 Missing (in isoform 1).
{ECO:0000303|PubMed:10048485}.
/FTId=VSP_035981.
VAR_SEQ 1156 1211 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_047002.
VAR_SEQ 1365 1368 ALPL -> GMSK (in isoform 1 and isoform
2). {ECO:0000303|PubMed:10048485}.
/FTId=VSP_035983.
VAR_SEQ 1369 1710 Missing (in isoform 1 and isoform 2).
{ECO:0000303|PubMed:10048485}.
/FTId=VSP_035984.
VARIANT 54 54 S -> L (in dbSNP:rs2289181).
/FTId=VAR_047932.
VARIANT 265 265 Q -> P (in MCPH9; dbSNP:rs267606717).
{ECO:0000269|PubMed:20598275}.
/FTId=VAR_063813.
VARIANT 667 667 K -> R (in SCKL5; dbSNP:rs200879436).
{ECO:0000269|PubMed:21131973}.
/FTId=VAR_065258.
VARIANT 793 793 S -> I (in dbSNP:rs2289178).
{ECO:0000269|PubMed:20547088}.
/FTId=VAR_050779.
VARIANT 914 914 L -> V (in dbSNP:rs16961560).
/FTId=VAR_050780.
VARIANT 1106 1106 V -> A (in dbSNP:rs16961557).
/FTId=VAR_050781.
MUTAGEN 21 21 E->K: Impairs interaction with PLK4;
impaired procentriole assembly and
chromosome segregation.
{ECO:0000269|PubMed:24997597}.
CONFLICT 558 558 S -> P (in Ref. 3; AAH69186).
{ECO:0000305}.
HELIX 21 35 {ECO:0000244|PDB:4N7V}.
SEQUENCE 1710 AA; 195626 MW; 1727BDA921E1F6BD CRC64;
MSLDFGSVAL PVQNEDEEYD EEDYEREKEL QQLLTDLPHD MLDDDLSSPE LQYSDCSEDG
TDGQPHHPEQ LEMSWNEQML PKSQSVNGYN EIQSLYAGEK CGNVWEENRS KTEDRHPVYH
PEEGGDEGGS GYSPPSKCEQ TDLYHLPENF RPYTNGQKQE FNNQATNVIK FSDPQWNHFQ
GPSCQGLEPY NKVTYKPYQS SAQNNGSPAQ EITGSDTFEG LQQQFLGANE NSAENMQIIQ
LQVLNKAKER QLENLIEKLN ESERQIRYLN HQLVIIKDEK DGLTLSLRES QKLFQNGKER
EIQLEAQIKA LETQIQALKV NEEQMIKKSR TTEMALESLK QQLVDLHHSE SLQRAREQHE
SIVMGLTKKY EEQVLSLQKN LDATVTALKE QEDICSRLKD HVKQLERNQE AIKLEKTEII
NKLTRSLEES QKQCAHLLQS GSVQEVAQLQ FQLQQAQKAH AMSANMNKAL QEELTELKDE
ISLYESAAKL GIHPSDSEGE LNIELTESYV DLGIKKVNWK KSKVTSIVQE EDPNEELSKD
EFILKLKAEV QRLLGSNSMK RHLVSQLQND LKDCHKKIED LHQVKKDEKS IEVETKTDTS
EKPKNQLWPE SSTSDVVRDD ILLLKNEIQV LQQQNQELKE TEGKLRNTNQ DLCNQMRQMV
QDFDHDKQEA VDRCERTYQQ HHEAMKTQIR ESLLAKHALE KQQLFEAYER THLQLRSELD
KLNKEVTAVQ ECYLEVCREK DNLELTLRKT TEKEQQTQEK IKEKLIQQLE KEWQSKLDQT
IKAMKKKTLD CGSQTDQVTT SDVISKKEMA IMIEEQKCTI QQNLEQEKDI AIKGAMKKLE
IELELKHCEN ITKQVEIAVQ NAHQRWLGEL PELAEYQALV KAEQKKWEEQ HEVSVNKRIS
FAVSEAKEKW KSELENMRKN ILPGKELEEK IHSLQKELEL KNEEVPVVIR AELAKARSEW
NKEKQEEIHR IQEQNEQDYR QFLDDHRNKI NEVLAAAKED FMKQKTELLL QKETELQTCL
DQSRREWTMQ EAKRIQLEIY QYEEDILTVL GVLLSDTQKE HISDSEDKQL LEIMSTCSSK
WMSVQYFEKL KGCIQKAFQD TLPLLVENAD PEWKKRNMAE LSKDSASQGT GQGDPGPAAG
HHAQPLALQA TEAEADKKKV LEIKDLCCGH CFQELEKAKQ ECQDLKGKLE KCCRHLQHLE
RKHKAVVEKI GEENNKVVEE LIEENNDMKN KLEELQTLCK TPPRSLSAGA IENACLPCSG
GALEELRGQY IKAVKKIKCD MLRYIQESKE RAAEMVKAEV LRERQETARK MRKYYLICLQ
QILQDDGKEG AEKKIMNAAS KLATMAKLLE TPISSKSQSK TTQSALPLTS EMLIAVKKSK
RNDVNQKIPC CIESKSNSVN TITRTLCEQA PKRRAACNLQ RLLENSEHQS IKHVGSKETH
LEFQFGDGSC KHLNSLPRNV SPEFVPCEGE GGFGLHKKKD LLSDNGSESL PHSAAYPFLG
TLGNKPSPRC TPGPSESGCM HITFRDSNER LGLKVYKCNP LMESENAASE KSQGLDVQEP
PVKDGGDLSD CLGWPSSSAT LSFDSREASF VHGRPQGTLE IPSESVKSKQ FSPSGYLSDT
EESNMICQTM KCQRYQTPYL SEETTYLEPG KISVNCGHPS RHKADRLKSD FKKLSSTLPS
SVCQQPSRKL IVPLSSQQDS GFDSPFVNLD


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