MED12_MOUSE
ID MED12_MOUSE Reviewed; 2190 AA.
AC A2AGH6; A2AGH7; O88542; Q571H3; Q6PGB4; Q6PGD8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 12;
DE AltName: Full=Mediator complex subunit 12;
DE AltName: Full=OPA-containing protein;
DE AltName: Full=Thyroid hormone receptor-associated protein complex 230 kDa component;
DE Short=Trap230;
DE AltName: Full=Trinucleotide repeat-containing gene 11 protein;
GN Name=Med12; Synonyms=Kiaa0192, Mopa, Tnrc11, Trap230;
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] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 33-2190 (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-2190 (ISOFORM 2).
RX PubMed=9702738; DOI=10.1038/sj.mp.4000442;
RA Philibert R.A., King B.H., Cook E.H., Lee Y.-H., Stubblefield B.,
RA Damschroder-Williams P., Dea C., Palotie A., Tengstrom C., Martin B.M.,
RA Ginns E.I.;
RT "Association of an X-chromosome dodecamer insertional variant allele with
RT mental retardation.";
RL Mol. Psychiatry 3:303-309(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1045-2190 (ISOFORM 1).
RC TISSUE=Spleen;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-636, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, 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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-80 AND LYS-1800, AND
RP IDENTIFICATION BY MASS 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 [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1901 AND ARG-1912, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: Component of the Mediator complex, a coactivator involved in
CC the regulated transcription of nearly all RNA polymerase II-dependent
CC genes. Mediator functions as a bridge to convey information from gene-
CC specific regulatory proteins to the basal RNA polymerase II
CC transcription machinery. Mediator is recruited to promoters by direct
CC interactions with regulatory proteins and serves as a scaffold for the
CC assembly of a functional preinitiation complex with RNA polymerase II
CC and the general transcription factors. This subunit may specifically
CC regulate transcription of targets of the Wnt signaling pathway and SHH
CC signaling pathway (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the Mediator complex, which is composed of MED1,
CC MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L,
CC MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23,
CC MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and
CC CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct
CC module termed the CDK8 module. Mediator containing the CDK8 module is
CC less active than Mediator lacking this module in supporting
CC transcriptional activation. Individual preparations of the Mediator
CC complex lacking one or more distinct subunits have been variously
CC termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. Also interacts with CTNNB1
CC and GLI3 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC A2AGH6; Q8R3L8: Cdk8; NbExp=3; IntAct=EBI-5744969, EBI-5745402;
CC A2AGH6; P37173: TGFBR2; Xeno; NbExp=3; IntAct=EBI-5744969, EBI-296151;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A2AGH6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AGH6-2; Sequence=VSP_029978, VSP_029979, VSP_029980;
CC Name=3;
CC IsoId=A2AGH6-3; Sequence=VSP_029977, VSP_029978;
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 12 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC83164.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL683892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057085; AAH57085.1; -; mRNA.
DR EMBL; BC057119; AAH57119.1; -; mRNA.
DR EMBL; AF071310; AAC83164.1; ALT_INIT; mRNA.
DR EMBL; AK220216; BAD90141.1; -; mRNA.
DR CCDS; CCDS41078.1; -. [A2AGH6-1]
DR RefSeq; NP_067496.2; NM_021521.2. [A2AGH6-1]
DR AlphaFoldDB; A2AGH6; -.
DR BioGRID; 208491; 5.
DR ComplexPortal; CPX-3266; CKM complex variant 1.
DR ComplexPortal; CPX-3267; CKM complex variant 2.
DR CORUM; A2AGH6; -.
DR DIP; DIP-59233N; -.
DR IntAct; A2AGH6; 10.
DR MINT; A2AGH6; -.
DR STRING; 10090.ENSMUSP00000085260; -.
DR iPTMnet; A2AGH6; -.
DR PhosphoSitePlus; A2AGH6; -.
DR EPD; A2AGH6; -.
DR MaxQB; A2AGH6; -.
DR PaxDb; A2AGH6; -.
DR PeptideAtlas; A2AGH6; -.
DR PRIDE; A2AGH6; -.
DR ProteomicsDB; 295847; -. [A2AGH6-1]
DR ProteomicsDB; 295848; -. [A2AGH6-2]
DR ProteomicsDB; 295849; -. [A2AGH6-3]
DR Antibodypedia; 562; 242 antibodies from 32 providers.
DR DNASU; 59024; -.
DR Ensembl; ENSMUST00000087948; ENSMUSP00000085260; ENSMUSG00000079487. [A2AGH6-1]
DR Ensembl; ENSMUST00000087956; ENSMUSP00000085269; ENSMUSG00000079487. [A2AGH6-2]
DR GeneID; 59024; -.
DR KEGG; mmu:59024; -.
DR UCSC; uc009txe.1; mouse. [A2AGH6-1]
DR UCSC; uc009txf.1; mouse. [A2AGH6-2]
DR CTD; 9968; -.
DR MGI; MGI:1926212; Med12.
DR VEuPathDB; HostDB:ENSMUSG00000079487; -.
DR eggNOG; KOG3598; Eukaryota.
DR GeneTree; ENSGT00440000037505; -.
DR HOGENOM; CLU_000904_1_0_1; -.
DR InParanoid; A2AGH6; -.
DR OMA; YQQSHDK; -.
DR PhylomeDB; A2AGH6; -.
DR TreeFam; TF324178; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 59024; 33 hits in 77 CRISPR screens.
DR ChiTaRS; Med12; mouse.
DR PRO; PR:A2AGH6; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; A2AGH6; protein.
DR Bgee; ENSMUSG00000079487; Expressed in bone marrow and 60 other tissues.
DR ExpressionAtlas; A2AGH6; baseline and differential.
DR Genevisible; A2AGH6; MM.
DR GO; GO:0016592; C:mediator complex; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0008013; F:beta-catenin binding; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; ISO: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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IGI:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0090245; P:axis elongation involved in somitogenesis; IMP:MGI.
DR GO; GO:1990403; P:embryonic brain development; IMP:MGI.
DR GO; GO:0048702; P:embryonic neurocranium morphogenesis; IMP:MGI.
DR GO; GO:0048568; P:embryonic organ development; IMP:MGI.
DR GO; GO:0007492; P:endoderm development; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:0021915; P:neural tube development; IMP:MGI.
DR GO; GO:0014003; P:oligodendrocyte development; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0036342; P:post-anal tail morphogenesis; IMP:MGI.
DR GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
DR GO; GO:0014044; P:Schwann cell development; IMP:MGI.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
DR GO; GO:0001756; P:somitogenesis; IMP:MGI.
DR GO; GO:0021510; P:spinal cord development; IMP:MGI.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IMP:MGI.
DR InterPro; IPR019035; Mediator_Med12.
DR InterPro; IPR021989; Mediator_Med12_catenin-bd.
DR InterPro; IPR021990; Mediator_Med12_LCEWAV.
DR Pfam; PF09497; Med12; 1.
DR Pfam; PF12145; Med12-LCEWAV; 1.
DR Pfam; PF12144; Med12-PQL; 1.
DR SMART; SM01281; Med12; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..2190
FT /note="Mediator of RNA polymerase II transcription subunit
FT 12"
FT /id="PRO_0000312957"
FT REGION 324..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1395..1416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1451..1475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1617..2063
FT /note="Interaction with CTNNB1 and GLI3"
FT /evidence="ECO:0000250"
FT REGION 1740..1833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1961..2003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2126..2162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2171..2190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1451..1472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1740..1762
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2126..2140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2147..2162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 80
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 166
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q93074"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93074"
FT MOD_RES 699
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93074"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93074"
FT MOD_RES 1259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93074"
FT MOD_RES 1270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93074"
FT MOD_RES 1800
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1901
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1901
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1912
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1999
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q93074"
FT MOD_RES 2020
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q93074"
FT VAR_SEQ 1..1321
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029977"
FT VAR_SEQ 1919..1921
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9702738"
FT /id="VSP_029978"
FT VAR_SEQ 1946
FT /note="S -> SQLSSPSL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9702738"
FT /id="VSP_029979"
FT VAR_SEQ 1966..1990
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9702738"
FT /id="VSP_029980"
FT CONFLICT 674
FT /note="S -> T (in Ref. 2; AAC83164)"
FT /evidence="ECO:0000305"
FT CONFLICT 1597
FT /note="A -> T (in Ref. 4; BAD90141)"
FT /evidence="ECO:0000305"
FT CONFLICT 2171
FT /note="L -> I (in Ref. 2; AAC83164)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2190 AA; 244561 MW; 146E05DCCFF38DB4 CRC64;
MAAFGILSYE HRPLKRLRLG PPDVYPQDPK QKEDELTALN VKQGFNNQPA VSGDEHGSAK
NVNFNPAKIS SNFSSIIAEK LRCNTLSDTG RRKSLMNQKD NFWLVTARSQ SAINTWFTDL
AGTKPLTHLA KKVPIFSKKE EVFGYLAKYT VPVMRAAWLI KMTCAYYAAM SETKVKKKNT
ADPFTEWTQI ITKYLWEQLQ KMAEYYRPGP AGSGGCGSTI GPLPHDVEMA IRQWDYNEKL
ALFMFQDGML DRHEFLTWVL ECFEKIRPGE DELLKLLLPL LLRYSGEFVQ SAYLSRRLAY
FCTRRLALQL DGVSSHSSHV IAAQSTSSLP TTPAPQPPTS STPSTPFSDL LMCPQHRPLV
FGLSCILQTI LLCCPSALVW HYSLTDSRIK TGSPLDHLPI APSNLPMPEG NSAFTQQVRA
KLREIEQQIK ERGQAVEVRW SFDKCQEATA GFTIGRVLHT LEVLDSHSFE RSDFSNSLDS
LCNRIFGLGP SKDGHEISSD DDAVVSLLCE WAVSCKRSGR HRAMVVAKLL EKRQAEIEAE
RCGESEAADE KGSVASGSLS APSAPIFQDV LLQFLDTQAP MLTDPRSESE RVEFFNLVLL
FCELIRHDVF SHNMYTCTLI SRGDLAFGAP GPRPPSPFDD PTDDPERKEA EGSSSSKLED
PGLSESMDID PSSSVLFEDM EKPDFSLFSP TMPCEGKGSP SPEKPDVEKE VKPPAKEKIE
GTLGILYDQP RHVQYATHFP IPQEESCSHE CNQRLVVLFG VGKQRDDARH AIKKITKDIL
KVLNRKGTAE TDQLAPIVPL NPGDLTFLGG EDGQKRRRNR PEAFPTAEDI FAKFQHLSHY
DQHQVTAQVS RNVLEQITSF ALGMSYHLPL VQHVQFIFDL MEYSLSISGL IDFAIQLLNE
LSVVEAELLL KSSDLVGSYT TSLCLCIVAV LRHYHACLIL NQDQMAQVFE GLCGVVKHGM
NRSDGSSAER CILAYLYDLY TSCSHLKSKF GELFSDFCSK VKNTIYCNVE PSESNMRWAP
EFMIDTLENP AAHTFTYTGL GKSLSENPAN RYSFVCNALM HVCVGHHDPD RVNDIAILCA
ELTGYCKSLS AEWLGVLKAL CCSSNNGTCG FNDLLCNVDV SDLSFHDSLA TFVAILIARQ
CLLLEDLIRC AAIPSLLNAA CSEQDSEPGA RLTCRILLHL FKTPQLNPCQ SDGNKPTVGI
RSSCDRHLLA ASQNRIVDGA VFAVLKAVFV LGDAELKGSG FTVPGGTEEL PEEEGGGGSS
GRRQGGRNIS VETASLDVYA KYVLRSICQQ EWVGERCLKS LCEDSNDLQD PVLSSAQAQR
LMQLICYPHR LLDNEDGENP QRQRIKRILK NLDQWTMRQS SLELQLMIKQ TPNTEMNSLL
ENIAKATIEV FQQSAETGSS SGSTASNMPS SSKTKPVLSS LERSGVWLVA PLIAKLPTSV
QGHVLKAAGE ELEKGQHLGS SSRKERDRQK QKSMSLLSQQ PFLSLVLTCL KGQDEQREGL
LASLHSQVHQ IVINWRENQY LDDCKPKQLM HEALKLRLNL VGGMFDTVQR STQQTTEWAQ
LLLEIIISGT VDMQSNNELF TTVLDMLSVL INGTLAADMS SISQGSMEEN KRAYMNLVKK
LQKDLGERQS DSLEKVHQLL PLPKQNRDVI TCEPQGSLID TKGNKIAGFD SIFKKEGLQV
STKQKISPWE LFEGLKPSTA PLSWAWFGTV RVDRRVARGE EQQRLLLYHT HLRPRPRAYY
LEPLPLPPED EEPPAPALLE PEKKAPEPPK TDKPGAAPPS TEERKKKSTK GKKRSQPATK
NEDYGMGPGR SGPYGVTVPP DLLHHANPGS ISHLSYRQSS MGLYTQNQPL PAGGPRVDPY
RPVRLPMQKL PTRPTYPGVL PTTMSTVMGL EPSSYKTSVY RQQQPTVPQG QRLRQQLQAK
IQSQGMLGQS SVHQMTPSSS YGLQTSQGYT SYVSHVGLQQ HTGPAGTMVP PSYSSQPYQS
THPSTNPTLV DPTRHLQQRP SGYVHQQAPT YGHGLTSTQR FSHQTLQQTP MMGTMTPLSA
QGVQAGVRST SILPEQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQYH IRQQQQQQQM
LRQQQQQQQQ QQQQQQQQQQ QQQQQQQQQP HQQQQQAAPP QPQPQSQPQF QRQGLQQTQQ
QQQTAALVRQ LQQQLSNTQP QPSTNIFGRY
