BICRA_HUMAN
ID BICRA_HUMAN Reviewed; 1560 AA.
AC Q9NZM4; A8MW01;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=BRD4-interacting chromatin-remodeling complex-associated protein {ECO:0000305};
DE AltName: Full=Glioma tumor suppressor candidate region gene 1 protein {ECO:0000312|HGNC:HGNC:4332};
GN Name=BICRA {ECO:0000312|HGNC:HGNC:4332};
GN Synonyms=GLTSCR1 {ECO:0000312|HGNC:HGNC:4332};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=10708517; DOI=10.1006/geno.1999.6101;
RA Smith J.S., Tachibana I., Pohl U., Lee H.K., Thanarajasingam U.,
RA Portier B.P., Ueki K., Billings S., Ramaswamy S., Mohrenweiser H.W.,
RA Scheithauer B.W., Louis D.N., Jenkins R.B.;
RT "A transcript map of the chromosome 19q-Arm glioma tumor suppressor
RT region.";
RL Genomics 64:44-50(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-500 (ISOFORM 1).
RC 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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1057, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [6]
RP FUNCTION, INTERACTION WITH BRD4, AND SUBCELLULAR LOCATION.
RX PubMed=21555454; DOI=10.1128/mcb.01341-10;
RA Rahman S., Sowa M.E., Ottinger M., Smith J.A., Shi Y., Harper J.W.,
RA Howley P.M.;
RT "The Brd4 extraterminal domain confers transcription activation independent
RT of pTEFb by recruiting multiple proteins, including NSD3.";
RL Mol. Cell. Biol. 31:2641-2652(2011).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-921 AND SER-1413, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-919, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1313, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [10]
RP FUNCTION, IDENTIFICATION IN THE GBAF COMPLEX, AND INTERACTION WITH BRD4.
RX PubMed=29374058; DOI=10.1074/jbc.ra117.001065;
RA Alpsoy A., Dykhuizen E.C.;
RT "Glioma tumor suppressor candidate region gene 1 (GLTSCR1) and its paralog
RT GLTSCR1-like form SWI/SNF chromatin remodeling subcomplexes.";
RL J. Biol. Chem. 293:3892-3903(2018).
RN [11]
RP INVOLVEMENT IN CSS12, AND VARIANTS CSS12 ASP-64; 665-GLN--ARG-1560 DEL;
RP LYS-1423 AND 1457-GLN--ARG-1560 DEL.
RX PubMed=33232675; DOI=10.1016/j.ajhg.2020.11.003;
RG Undiagnosed Diseases Network;
RA Barish S., Barakat T.S., Michel B.C., Mashtalir N., Phillips J.B.,
RA Valencia A.M., Ugur B., Wegner J., Scott T.M., Bostwick B., Murdock D.R.,
RA Dai H., Perenthaler E., Nikoncuk A., van Slegtenhorst M., Brooks A.S.,
RA Keren B., Nava C., Mignot C., Douglas J., Rodan L., Nowak C., Ellard S.,
RA Stals K., Lynch S.A., Faoucher M., Lesca G., Edery P., Engleman K.L.,
RA Zhou D., Thiffault I., Herriges J., Gass J., Louie R.J., Stolerman E.,
RA Washington C., Vetrini F., Otsubo A., Pratt V.M., Conboy E., Treat K.,
RA Shannon N., Camacho J., Wakeling E., Yuan B., Chen C.A., Rosenfeld J.A.,
RA Westerfield M., Wangler M., Yamamoto S., Kadoch C., Scott D.A.,
RA Bellen H.J.;
RT "BICRA, a SWI/SNF Complex Member, Is Associated with BAF-Disorder Related
RT Phenotypes in Humans and Model Organisms.";
RL Am. J. Hum. Genet. 107:1096-1112(2020).
CC -!- FUNCTION: Component of SWI/SNF chromatin remodeling subcomplex GBAF
CC that carries out key enzymatic activities, changing chromatin structure
CC by altering DNA-histone contacts within a nucleosome in an ATP-
CC dependent manner (PubMed:29374058). May play a role in BRD4-mediated
CC gene transcription (PubMed:21555454). {ECO:0000269|PubMed:21555454,
CC ECO:0000269|PubMed:29374058}.
CC -!- SUBUNIT: Component of the multiprotein chromatin-remodeling complexes
CC SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The
CC canonical complex contains a catalytic subunit (either
CC SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1,
CC ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47.
CC Other subunits specific to each of the complexes may also be present
CC permitting several possible combinations developmentally and tissue
CC specific. Component of the SWI/SNF (GBAF) subcomplex, which includes at
CC least BICRA or BICRAL (mutually exclusive), BRD9, SS18, the core BAF
CC subunits, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53,
CC SMARCC1/BAF155, and SMARCD1/BAF60A (PubMed:29374058). Interacts with
CC BRD4; the interaction bridges BRD4 to the GBAF complex
CC (PubMed:29374058, PubMed:21555454). {ECO:0000269|PubMed:21555454,
CC ECO:0000269|PubMed:29374058}.
CC -!- INTERACTION:
CC Q9NZM4; P46108: CRK; NbExp=3; IntAct=EBI-1754943, EBI-886;
CC Q9NZM4; P16333: NCK1; NbExp=3; IntAct=EBI-1754943, EBI-389883;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21555454}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NZM4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NZM4-2; Sequence=VSP_035776;
CC -!- TISSUE SPECIFICITY: Expressed at moderate levels in heart, brain,
CC placenta, skeletal muscle, and pancreas, and at lower levels in lung,
CC liver and kidney. {ECO:0000269|PubMed:10708517}.
CC -!- DISEASE: Coffin-Siris syndrome 12 (CSS12) [MIM:619325]: A form of
CC Coffin-Siris syndrome, a congenital multiple malformation syndrome with
CC broad phenotypic and genetic variability. Cardinal features are
CC intellectual disability, coarse facial features, hypertrichosis, and
CC hypoplastic or absent fifth digit nails or phalanges. Additional
CC features include malformations of the cardiac, gastrointestinal,
CC genitourinary, and/or central nervous systems. Sucking/feeding
CC difficulties, poor growth, ophthalmologic abnormalities, hearing
CC impairment, and spinal anomalies are common findings. CSS12 is an
CC autosomal dominant form characterized by global developmental delay
CC with variably impaired intellectual development, speech and language
CC delay, and behavioral abnormalities, such as autism or hyperactivity.
CC Most CSS12 patients do not have the classic hypoplastic fifth
CC digit/nail abnormalities that are often observed in other forms the
CC disease. {ECO:0000269|PubMed:33232675}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF62874.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF182077; AAF62874.1; ALT_INIT; mRNA.
DR EMBL; AC008985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471126; EAW57504.1; -; Genomic_DNA.
DR EMBL; BC032065; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS46134.1; -. [Q9NZM4-1]
DR RefSeq; NP_056526.3; NM_015711.3. [Q9NZM4-1]
DR RefSeq; XP_005258890.1; XM_005258833.4. [Q9NZM4-1]
DR AlphaFoldDB; Q9NZM4; -.
DR BioGRID; 119022; 59.
DR ComplexPortal; CPX-4084; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4206; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4223; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4225; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA4 variant.
DR IntAct; Q9NZM4; 27.
DR MINT; Q9NZM4; -.
DR STRING; 9606.ENSP00000379946; -.
DR GlyGen; Q9NZM4; 3 sites, 2 O-linked glycans (3 sites).
DR iPTMnet; Q9NZM4; -.
DR PhosphoSitePlus; Q9NZM4; -.
DR BioMuta; BICRA; -.
DR DMDM; 215273990; -.
DR EPD; Q9NZM4; -.
DR jPOST; Q9NZM4; -.
DR MassIVE; Q9NZM4; -.
DR MaxQB; Q9NZM4; -.
DR PaxDb; Q9NZM4; -.
DR PeptideAtlas; Q9NZM4; -.
DR PRIDE; Q9NZM4; -.
DR ProteomicsDB; 83449; -. [Q9NZM4-1]
DR ProteomicsDB; 83450; -. [Q9NZM4-2]
DR Antibodypedia; 65070; 78 antibodies from 18 providers.
DR DNASU; 29998; -.
DR Ensembl; ENST00000396720.7; ENSP00000379946.2; ENSG00000063169.12. [Q9NZM4-1]
DR Ensembl; ENST00000594866.3; ENSP00000469738.2; ENSG00000063169.12. [Q9NZM4-1]
DR Ensembl; ENST00000614245.2; ENSP00000480219.2; ENSG00000063169.12. [Q9NZM4-2]
DR GeneID; 29998; -.
DR KEGG; hsa:29998; -.
DR MANE-Select; ENST00000594866.3; ENSP00000469738.2; NM_001394372.1; NP_001381301.1.
DR UCSC; uc002phh.4; human. [Q9NZM4-1]
DR CTD; 29998; -.
DR DisGeNET; 29998; -.
DR GeneCards; BICRA; -.
DR HGNC; HGNC:4332; BICRA.
DR HPA; ENSG00000063169; Low tissue specificity.
DR MalaCards; BICRA; -.
DR MIM; 605690; gene.
DR MIM; 619325; phenotype.
DR neXtProt; NX_Q9NZM4; -.
DR OpenTargets; ENSG00000063169; -.
DR PharmGKB; PA28735; -.
DR VEuPathDB; HostDB:ENSG00000063169; -.
DR eggNOG; ENOG502QU2K; Eukaryota.
DR GeneTree; ENSGT00940000159112; -.
DR HOGENOM; CLU_002283_0_0_1; -.
DR InParanoid; Q9NZM4; -.
DR OMA; WVGQSHS; -.
DR OrthoDB; 352636at2759; -.
DR PhylomeDB; Q9NZM4; -.
DR TreeFam; TF335495; -.
DR PathwayCommons; Q9NZM4; -.
DR SignaLink; Q9NZM4; -.
DR BioGRID-ORCS; 29998; 28 hits in 1086 CRISPR screens.
DR ChiTaRS; BICRA; human.
DR GenomeRNAi; 29998; -.
DR Pharos; Q9NZM4; Tbio.
DR PRO; PR:Q9NZM4; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9NZM4; protein.
DR Bgee; ENSG00000063169; Expressed in oocyte and 196 other tissues.
DR ExpressionAtlas; Q9NZM4; baseline and differential.
DR Genevisible; Q9NZM4; HS.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0140288; C:GBAF complex; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IMP:UniProtKB.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
DR GO; GO:0140537; F:transcription regulator activator activity; IMP:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IC:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR InterPro; IPR038842; BICRA.
DR InterPro; IPR015671; GSCR1_dom.
DR PANTHER; PTHR15572:SF1; PTHR15572:SF1; 1.
DR Pfam; PF15249; GLTSCR1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Disease variant;
KW Intellectual disability; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..1560
FT /note="BRD4-interacting chromatin-remodeling complex-
FT associated protein"
FT /id="PRO_0000083864"
FT REGION 53..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1049..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1215..1300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1324..1424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1440..1560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..665
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..767
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..831
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..881
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..945
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1026
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1259..1281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1361
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1482..1517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 919
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 921
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1057
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 1313
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..242
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10708517"
FT /id="VSP_035776"
FT VARIANT 64
FT /note="E -> D (in CSS12; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33232675"
FT /id="VAR_085989"
FT VARIANT 665..1560
FT /note="Missing (in CSS12)"
FT /evidence="ECO:0000269|PubMed:33232675"
FT /id="VAR_085990"
FT VARIANT 683
FT /note="P -> S (in dbSNP:rs3745762)"
FT /id="VAR_061663"
FT VARIANT 1044
FT /note="T -> A (in dbSNP:rs13346368)"
FT /id="VAR_059665"
FT VARIANT 1423
FT /note="E -> K (in CSS12; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33232675"
FT /id="VAR_085991"
FT VARIANT 1457..1560
FT /note="Missing (in CSS12)"
FT /evidence="ECO:0000269|PubMed:33232675"
FT /id="VAR_085992"
SQ SEQUENCE 1560 AA; 158490 MW; 32453B35C9219462 CRC64;
MDDEDGRCLL DVICDPQALN DFLHGSEKLD SDDLLDNPGE AQSAFYEGPG LHVQEASGNH
LNPEPNQPAP SVDLDFLEDD ILGSPATGGG GGGSGGADQP CDILQQSLQE ANITEQTLEA
EAELDLGPFQ LPTLQPADGG AGPTGAGGAA AVAAGPQALF PGSTDLLGLQ GPPTVLTHQA
LVPPQDVVNK ALSVQPFLQP VGLGNVTLQP IPGLQGLPNG SPGGATAATL GLAPIQVVGQ
PVMALNTPTS QLLAKQVPVS GYLASAAGPS EPVTLASAGV SPQGAGLVIQ KNLSAAVATT
LNGNSVFGGA GAASAPTGTP SGQPLAVAPG LGSSPLVPAP NVILHRTPTP IQPKPAGVLP
PKLYQLTPKP FAPAGATLTI QGEPGALPQQ PKAPQNLTFM AAGKAGQNVV LSGFPAPALQ
ANVFKQPPAT TTGAAPPQPP GALSKPMSVH LLNQGSSIVI PAQHMLPGQN QFLLPGAPAV
QLPQQLSALP ANVGGQILAA AAPHTGGQLI ANPILTNQNL AGPLSLGPVL APHSGAHSAH
ILSAAPIQVG QPALFQMPVS LAAGSLPTQS QPAPAGPAAT TVLQGVTLPP SAVAMLNTPD
GLVQPATPAA ATGEAAPVLT VQPAPQAPPA VSTPLPLGLQ QPQAQQPPQA PTPQAAAPPQ
ATTPQPSPGL ASSPEKIVLG QPPSATPTAI LTQDSLQMFL PQERSQQPLS AEGPHLSVPA
SVIVSAPPPA QDPAPATPVA KGAGLGPQAP DSQASPAPAP QIPAAAPLKG PGPSSSPSLP
HQAPLGDSPH LPSPHPTRPP SRPPSRPQSV SRPPSEPPLH PCPPPQAPPT LPGIFVIQNQ
LGVPPPASNP APTAPGPPQP PLRPQSQPPE GPLPPAPHLP PSSTSSAVAS SSETSSRLPA
PTPSDFQLQF PPSQGPHKSP TPPPTLHLVP EPAAPPPPPP RTFQMVTTPF PALPQPKALL
ERFHQVPSGI ILQNKAGGAP AAPQTSTSLG PLTSPAASVL VSGQAPSGTP TAPSHAPAPA
PMAATGLPPL LPAENKAFAS NLPTLNVAKA ASSGPGKPSG LQYESKLSGL KKPPTLQPSK
EACFLEHLHK HQGSVLHPDY KTAFPSFEDA LHRLLPYHVY QGALPSPSDY HKVDEEFETV
STQLLKRTQA MLNKYRLLLL EESRRVSPSA EMVMIDRMFI QEEKTTLALD KQLAKEKPDE
YVSSSRSLGL PIAASSEGHR LPGHGPLSSS APGASTQPPP HLPTKLVIRH GGAGGSPSVT
WARASSSLSS SSSSSSAASS LDADEDGPMP SRNRPPIKTY EARSRIGLKL KIKQEAGLSK
VVHNTALDPV HQPPPPPATL KVAEPPPRPP PPPPPTGQMN GTVDHPPPAA PERKPLGTAP
HCPRLPLRKT YRENVGGPGA PEGTPAGRAR GGSPAPLPAK VDEATSGLIR ELAAVEDELY
QRMLKGPPPE PAASAAQGTG DPDWEAPGLP PAKRRKSESP DVDQASFSSD SPQDDTLTEH
LQSAIDSILN LQQAPGRTPA PSYPHAASAG TPASPPPLHR PEAYPPSSHN GGLGARTLTR
