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   24-JAN-2024, entry version 120.
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 10090-ENSMUSP00000085260; -.
DR   PeptideAtlas; A2AGH6; -.
DR   ProteomicsDB; 295847; -. [A2AGH6-1]
DR   ProteomicsDB; 295848; -. [A2AGH6-2]
DR   ProteomicsDB; 295849; -. [A2AGH6-3]
DR   Pumba; A2AGH6; -.
DR   Antibodypedia; 562; 280 antibodies from 32 providers.
DR   DNASU; 59024; -.
DR   Ensembl; ENSMUST00000087948.11; ENSMUSP00000085260.5; ENSMUSG00000079487.12. [A2AGH6-1]
DR   Ensembl; ENSMUST00000087956.6; ENSMUSP00000085269.6; ENSMUSG00000079487.12. [A2AGH6-2]
DR   GeneID; 59024; -.
DR   KEGG; mmu:59024; -.
DR   UCSC; uc009txe.1; mouse. [A2AGH6-1]
DR   UCSC; uc009txf.1; mouse. [A2AGH6-2]
DR   AGR; MGI:1926212; -.
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   OrthoDB; 470522at2759; -.
DR   PhylomeDB; A2AGH6; -.
DR   TreeFam; TF324178; -.
DR   BioGRID-ORCS; 59024; 33 hits in 82 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 63 other cell types or tissues.
DR   ExpressionAtlas; A2AGH6; baseline and differential.
DR   GO; GO:1990508; C:CKM complex; ISO:MGI.
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: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; IEA:Ensembl.
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:0045893; P:positive regulation of DNA-templated transcription; ISO: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 by RNA polymerase II; 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   PANTHER; PTHR46007; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 12; 1.
DR   PANTHER; PTHR46007:SF2; MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT 12; 1.
DR   Pfam; PF09497; Med12; 1.
DR   Pfam; PF12145; Med12-LCEWAV; 1.
DR   Pfam; PF12144; Med12-PQL; 1.
DR   SMART; SM01281; Med12; 1.
DR   Genevisible; A2AGH6; MM.
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
//