PRC2A_MOUSE
ID PRC2A_MOUSE Reviewed; 2158 AA.
AC Q7TSC1; Q923A9; Q9Z1R1;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Protein PRRC2A;
DE AltName: Full=HLA-B-associated transcript 2;
DE AltName: Full=Proline-rich and coiled-coil-containing protein 2A;
GN Name=Prrc2a; Synonyms=Bat2;
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=129;
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Mammary gland;
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 [3]
RP PROTEIN SEQUENCE OF 82-89, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-995; SER-1087 AND SER-1090,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166 AND THR-609, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-808 AND SER-1217, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-166; SER-378;
RP SER-454; SER-761; THR-807; SER-1087; SER-1090; SER-1217; SER-1302;
RP SER-1306; THR-1319 AND SER-1321, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-35, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [9]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-907 AND ARG-1064, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: May play a role in the regulation of pre-mRNA splicing.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
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DR EMBL; AF109719; AAC82480.1; -; Genomic_DNA.
DR EMBL; BC006664; AAH06664.1; -; mRNA.
DR EMBL; BC053522; AAH53522.1; -; mRNA.
DR CCDS; CCDS37596.1; -.
DR RefSeq; NP_001185973.1; NM_001199044.1.
DR RefSeq; NP_064411.2; NM_020027.3.
DR RefSeq; XP_006524683.1; XM_006524620.3.
DR AlphaFoldDB; Q7TSC1; -.
DR BioGRID; 207439; 32.
DR DIP; DIP-49629N; -.
DR IntAct; Q7TSC1; 7.
DR MINT; Q7TSC1; -.
DR STRING; 10090.ENSMUSP00000025253; -.
DR iPTMnet; Q7TSC1; -.
DR PhosphoSitePlus; Q7TSC1; -.
DR EPD; Q7TSC1; -.
DR jPOST; Q7TSC1; -.
DR MaxQB; Q7TSC1; -.
DR PaxDb; Q7TSC1; -.
DR PeptideAtlas; Q7TSC1; -.
DR PRIDE; Q7TSC1; -.
DR ProteomicsDB; 291551; -.
DR Antibodypedia; 62364; 11 antibodies from 7 providers.
DR DNASU; 53761; -.
DR Ensembl; ENSMUST00000025253; ENSMUSP00000025253; ENSMUSG00000024393.
DR GeneID; 53761; -.
DR KEGG; mmu:53761; -.
DR UCSC; uc008cgj.2; mouse.
DR CTD; 7916; -.
DR MGI; MGI:1915467; Prrc2a.
DR VEuPathDB; HostDB:ENSMUSG00000024393; -.
DR eggNOG; KOG4817; Eukaryota.
DR GeneTree; ENSGT00950000183161; -.
DR HOGENOM; CLU_001247_1_0_1; -.
DR InParanoid; Q7TSC1; -.
DR OMA; QFGTNDK; -.
DR OrthoDB; 17901at2759; -.
DR PhylomeDB; Q7TSC1; -.
DR TreeFam; TF328738; -.
DR BioGRID-ORCS; 53761; 15 hits in 74 CRISPR screens.
DR ChiTaRS; Prrc2a; mouse.
DR PRO; PR:Q7TSC1; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q7TSC1; protein.
DR Bgee; ENSMUSG00000024393; Expressed in embryonic post-anal tail and 243 other tissues.
DR ExpressionAtlas; Q7TSC1; baseline and differential.
DR Genevisible; Q7TSC1; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR InterPro; IPR009738; BAT2_N.
DR InterPro; IPR033184; PRRC2.
DR PANTHER; PTHR14038; PTHR14038; 1.
DR Pfam; PF07001; BAT2_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..2158
FT /note="Protein PRRC2A"
FT /id="PRO_0000064831"
FT REPEAT 41..95
FT /note="1-1"
FT REPEAT 98..154
FT /note="1-2"
FT REPEAT 281..336
FT /note="1-3"
FT REPEAT 337..428
FT /note="2-1"
FT REPEAT 486..559
FT /note="2-2"
FT REPEAT 1756..1811
FT /note="1-4"
FT REPEAT 1917..1966
FT /note="3-1"
FT REPEAT 1983..2032
FT /note="3-2"
FT REPEAT 2058..2107
FT /note="3-3"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..1811
FT /note="4 X 57 AA type A repeats"
FT REGION 49..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..559
FT /note="2 X type B repeats"
FT REGION 737..1769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1802..1883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1917..2107
FT /note="3 X 50 AA type C repeats"
FT REGION 1945..1975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1996..2158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..277
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..419
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..559
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..614
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..714
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..871
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..962
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..988
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1063
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1203
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1230..1265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1441..1456
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1467..1487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1492..1515
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1551..1566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1638..1670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1707..1724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1802..1824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1840..1876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1952..1967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1996..2037
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2067..2111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2133..2149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 27
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 35
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 272
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 296
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 609
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 759
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 761
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 764
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 807
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 808
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 907
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 931
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 995
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 1002
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 1064
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1081
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 1083
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 1087
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1090
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1092
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 1104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 1108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 1118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 1145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 1194
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 1217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1319
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 1343
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 1349
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 1380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 1382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 1401
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6MG48"
FT MOD_RES 1521
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 1757
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6MG48"
FT MOD_RES 2037
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 2077
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT MOD_RES 2114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48634"
FT CONFLICT 1846
FT /note="Missing (in Ref. 1; AAC82480)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2158 AA; 229203 MW; 85A5CBDCDA84A256 CRC64;
MSDRSGPTAK GKDGKKYSSL NLFDTYKGKS LEIQKPAVAP RHGLQSLGKV AIARRMPPPA
NLPSLKAENK GNDPNVSLVP KDGTGWASKQ EQSDPKSSDA STAQPPESQP LPASQTPASN
QPKRPPTAPE NTPSVPSGVK SWAQASVTHG AHGDGGRASN LLSRFSREEF PTLQAAGDQD
KAAKERESAE QSSGPGPSLR PQNSTTWRDG GGRGPDDLEG PDSKLHHGHD PRGGLQPSGP
PQFPPYRGMM PPFMYPPYLP FPPPYGPQGP YRYPTPDGPS RFPRVAGPRG SGPPMRLVEP
VGRPSILKED NLKEFDQLDQ ENDDGWAGAH EEVDYTEKLK FSDEEDGRDS DEEGAEGHKD
SQSAAAEEPE TDGKKGTSPG SELPPPKTAW TENARPSETE PAPPTPKPPP PPPHRGPVGN
WGPPGDYPDR GGPPCKPPAP EDEDEAWRQR RKQSSSEISL AVERARRRRE EEERRMQEER
RAACAEKLKR LDEKFGAPDK RLKAEPAAPP VTPAAPALPP VVPKEIPAAP ALPPTPTPTP
EKEPEEPAQA PPVQAAPSPG VAPVPTLVSG GGCTANSNSS GSFEASPVEP QLPSKEGPEP
PEEVPPPTTP PAPKMEPKGD GVGSTRQPPS QGLGYPKYQK SLPPRFQRQQ QEQLLKQQQQ
QQQWQQQQQG TAPPAPVPPS PPQPVTLGAV PAPQAPPPPP KALYPGALGR PPPMPPMNFD
PRWMMIPPYV DPRLLQGRPP LDFYPPGVHP SGLVPRERSD SGGSSSEPFE RHAPPLLRER
GTPPVDPKLA WVGDVFTTTP TDPRPLTSPL RQAADEEEKS MRSETPPVPP PPPYLANYPG
FPENGTPGPP ISRFPLEESA PPGPRPLPWP PGNDEAAKMQ APPPKKEPSK EEPPQLSGPE
AGRKPARGGQ GPPPPRRENR TETRWGPRPG SCRRGIPPEE PGVPPRRAGP IKKPPPPVKV
EELPPKSLEQ GDETPKVPKP DALKTAKGKV GPKETPPGGN LSPAPRLRRD YSYERVGPTS
CRGRGRGEYF ARGRGFRGTY GGRGRGARSR EFRSYREFRG DDGRGGGSGG TNHPSAPRGR
TASETRSEGS EYEEIPKRRR QRGSETGSET HESDLAPSDK EAPPPKEGVL GQVPLAPPQP
GAPPSPAPAR FSTARGGRVF TPRGVPSRRG RGGGRPPPVC SGWSPPAKSL VPKKPPTGPL
PPSKEPLKEK LISGPLSPMS RAGNMGVGME DGERPRRRRH GRAQQQDKPP RFRRLKQERE
NAARGADGKP PSLTLAASTP GPEETLTAAT VPPPPRRTAA KSPDLSNQNS DQANEEWETA
SESSDFASER RGDKETPPAA LMTSKAVGTP GANAGGAGPG ISAMSRGDLS QRAKDLSKRS
FSSQRPGMDR QNRRPGTGGK TGSGGGSSGG GGAGPGGRTG PGRGDKRSWP SPKNRSRPPE
ERPPGLPLPP PPPSSSAVFR LDQVIHSNPA GIQQALAQLS SRQGNVTAPG GHPRPKPGPP
QAPQGSSPRP PTRYDPPRAS SAISSDPHFE EPGPMVRGVG GTPRDSAGVN PFPPKRRERP
PRKPELLQEE TVPASHSSGF LGSKPEVPGP QEESRDSGTE ALTPHIWNRL HTATSRKSYQ
PGSIEPWMEP LSPFEDVAGT EMSQSDSGVD LSGDSQVSSG PCSQRSSPDG GLKGSAEGPP
KRPGGPSPLN AVPGESASGS EPSEPPRRRP PASHEGERKE LPREQPLPPG PIGTERSQRT
DRGPEPGPLR PAHRPGSQVE FGTTNKDSDL CLVVGDTLKG EKELVASATE AVPISRDWEL
LPSASTSAEP QPKSLGSGQC VPEPSPSGQR PYPEVFYGSP GPPNSQQVSG GAPIDSQLHP
NSGGFRPGTP SLHQYRSQPL YLPPGPAPPS ALLSGVALKG QFLDFSALQA TELGKLPAGG
VLYPPPSFLY SAAFCPSPLP DPPLLQVRQD LPSPSDFYST PLQPGGQSGF LPSGAPAQQM
LLPVVDSQLP VVNFGSLPPA PPPAPPPLSL LPVGPALQPP NLAVRPPPAP AARVLPSPAR
PFAPSLGRAE LHPVELKPFQ DYRKLSSNLG GPGSSRTPPS GRPFSGLNSR LKAPPSTYSG
VFRTQRIDLY QQASPPDALR WMPKPWERAG PPSREGPPRR AEEPGSRGEK EPGLPPPR
