TCRG1_MOUSE
ID TCRG1_MOUSE Reviewed; 1100 AA.
AC Q8CGF7; Q61051; Q8C490; Q8CHT8; Q9R0R5;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Transcription elongation regulator 1;
DE AltName: Full=Formin-binding protein 28;
DE Short=FBP 28;
DE AltName: Full=TATA box-binding protein-associated factor 2S;
DE AltName: Full=Transcription factor CA150;
DE AltName: Full=p144;
GN Name=Tcerg1; Synonyms=Taf2s;
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 [MRNA] (ISOFORM 3), AND ALTERNATIVE SPLICING.
RC TISSUE=Liver;
RX PubMed=10578054; DOI=10.1093/oxfordjournals.jbchem.a022547;
RA Simada M., Saito M., Katakai T., Shimizu A., Ichimura T., Omata S.,
RA Horigome T.;
RT "Molecular cloning and splicing isoforms of mouse p144, a homologue of
RT CA150.";
RL J. Biochem. 126:1033-1042(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
RP 184-GLN-ALA-185 DEL.
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 437-462, AND INTERACTION WITH FORMIN.
RC STRAIN=FVB/NJ; TISSUE=Embryo;
RX PubMed=8605874; DOI=10.1002/j.1460-2075.1996.tb00442.x;
RA Chan D.C., Bedford M.T., Leder P.;
RT "Formin binding proteins bear WWP/WW domains that bind proline-rich
RT peptides and functionally resemble SH3 domains.";
RL EMBO J. 15:1045-1054(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 827-1100 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP INTERACTION WITH HTATSF1, AND DOMAIN.
RX PubMed=15485897; DOI=10.1128/mcb.24.21.9274-9285.2004;
RA Smith M.J., Kulkarni S., Pawson T.;
RT "FF domains of CA150 bind transcription and splicing factors through
RT multiple weak interactions.";
RL Mol. Cell. Biol. 24:9274-9285(2004).
RN [6]
RP INTERACTION WITH TREX1.
RX PubMed=17355961; DOI=10.1074/jbc.m700236200;
RA Brucet M., Querol-Audi J., Serra M., Ramirez-Espain X., Bertlik K.,
RA Ruiz L., Lloberas J., Macias M.J., Fita I., Celada A.;
RT "Structure of the dimeric exonuclease TREX1 in complex with DNA displays a
RT proline-rich binding site for WW Domains.";
RL J. Biol. Chem. 282:14547-14557(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 METHYLATION [LARGE SCALE ANALYSIS] AT ARG-28; ARG-30 AND ARG-41, 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).
RN [9]
RP STRUCTURE BY NMR OF 437-462.
RX PubMed=10802733; DOI=10.1038/75144;
RA Macias M.J., Gervais V., Civera C., Oschkinat H.;
RT "Structural analysis of WW domains and design of a WW prototype.";
RL Nat. Struct. Biol. 7:375-379(2000).
CC -!- FUNCTION: Transcription factor that binds RNA polymerase II and
CC inhibits the elongation of transcripts from target promoters. Regulates
CC transcription elongation in a TATA box-dependent manner (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds RNA polymerase II, HD and SF1 (By similarity). Binds
CC formin. Interacts (via the second WW domain) with TREX1 (via proline-
CC rich region). {ECO:0000250, ECO:0000269|PubMed:15485897,
CC ECO:0000269|PubMed:17355961, ECO:0000269|PubMed:8605874}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=CA150a;
CC IsoId=Q8CGF7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CGF7-2; Sequence=VSP_011655;
CC Name=3; Synonyms=CA150b;
CC IsoId=Q8CGF7-3; Sequence=VSP_011656, VSP_011657;
CC -!- DOMAIN: The FF domains preferentially binds peptides with the consensus
CC sequence [DE](2-5)-[FWY]-[DE](2-5) and mediate interaction with HTATSF1
CC and probably bind the phosphorylated C-terminus of the largest subunit
CC of RNA polymerase II. {ECO:0000269|PubMed:15485897}.
CC -!- DOMAIN: The WW domains bind Pro-rich domains.
CC {ECO:0000269|PubMed:15485897}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH39185.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC039185; AAH39185.1; ALT_INIT; mRNA.
DR EMBL; BC040284; AAH40284.1; -; mRNA.
DR EMBL; AB023485; BAA86392.1; -; mRNA.
DR EMBL; U40749; AAC52477.1; -; mRNA.
DR EMBL; AK082750; BAC38600.1; -; mRNA.
DR CCDS; CCDS29214.1; -. [Q8CGF7-1]
DR CCDS; CCDS89230.1; -. [Q8CGF7-2]
DR PIR; S64716; S64716.
DR RefSeq; NP_001034563.1; NM_001039474.1. [Q8CGF7-1]
DR RefSeq; NP_001276455.1; NM_001289526.1.
DR RefSeq; XP_006526178.1; XM_006526115.3.
DR PDB; 1E0L; NMR; -; A=430-466.
DR PDB; 2JUP; NMR; -; W=430-466.
DR PDB; 2RLY; NMR; -; W=430-466.
DR PDB; 2RM0; NMR; -; W=430-466.
DR PDB; 2YSI; NMR; -; A=133-165.
DR PDBsum; 1E0L; -.
DR PDBsum; 2JUP; -.
DR PDBsum; 2RLY; -.
DR PDBsum; 2RM0; -.
DR PDBsum; 2YSI; -.
DR AlphaFoldDB; Q8CGF7; -.
DR SMR; Q8CGF7; -.
DR BioGRID; 207801; 23.
DR IntAct; Q8CGF7; 2.
DR MINT; Q8CGF7; -.
DR STRING; 10090.ENSMUSP00000025375; -.
DR iPTMnet; Q8CGF7; -.
DR PhosphoSitePlus; Q8CGF7; -.
DR EPD; Q8CGF7; -.
DR MaxQB; Q8CGF7; -.
DR PaxDb; Q8CGF7; -.
DR PeptideAtlas; Q8CGF7; -.
DR PRIDE; Q8CGF7; -.
DR ProteomicsDB; 254682; -. [Q8CGF7-1]
DR ProteomicsDB; 254683; -. [Q8CGF7-2]
DR ProteomicsDB; 254684; -. [Q8CGF7-3]
DR Antibodypedia; 15805; 194 antibodies from 27 providers.
DR DNASU; 56070; -.
DR Ensembl; ENSMUST00000025375; ENSMUSP00000025375; ENSMUSG00000024498. [Q8CGF7-2]
DR Ensembl; ENSMUST00000173642; ENSMUSP00000134458; ENSMUSG00000024498. [Q8CGF7-3]
DR Ensembl; ENSMUST00000237602; ENSMUSP00000158288; ENSMUSG00000024498. [Q8CGF7-1]
DR GeneID; 56070; -.
DR KEGG; mmu:56070; -.
DR UCSC; uc008etw.2; mouse. [Q8CGF7-2]
DR UCSC; uc008etx.1; mouse. [Q8CGF7-1]
DR CTD; 10915; -.
DR MGI; MGI:1926421; Tcerg1.
DR VEuPathDB; HostDB:ENSMUSG00000024498; -.
DR eggNOG; KOG0155; Eukaryota.
DR GeneTree; ENSGT00940000157770; -.
DR HOGENOM; CLU_008684_0_0_1; -.
DR InParanoid; Q8CGF7; -.
DR OMA; KPPGYKG; -.
DR OrthoDB; 1388955at2759; -.
DR PhylomeDB; Q8CGF7; -.
DR TreeFam; TF317748; -.
DR BioGRID-ORCS; 56070; 7 hits in 76 CRISPR screens.
DR ChiTaRS; Tcerg1; mouse.
DR EvolutionaryTrace; Q8CGF7; -.
DR PRO; PR:Q8CGF7; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8CGF7; protein.
DR Bgee; ENSMUSG00000024498; Expressed in embryonic post-anal tail and 201 other tissues.
DR ExpressionAtlas; Q8CGF7; baseline and differential.
DR Genevisible; Q8CGF7; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0070064; F:proline-rich region binding; IDA:MGI.
DR GO; GO:0070063; F:RNA polymerase binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; ISO:MGI.
DR GO; GO:0006397; P:mRNA processing; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0008380; P:RNA splicing; ISO:MGI.
DR GO; GO:0006351; P:transcription, DNA-templated; ISS:MGI.
DR CDD; cd00201; WW; 3.
DR Gene3D; 1.10.10.440; -; 6.
DR InterPro; IPR002713; FF_domain.
DR InterPro; IPR036517; FF_domain_sf.
DR InterPro; IPR045148; TCRG1-like.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR15377; PTHR15377; 2.
DR Pfam; PF01846; FF; 6.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00441; FF; 6.
DR SMART; SM00456; WW; 3.
DR SUPFAM; SSF51045; SSF51045; 3.
DR SUPFAM; SSF81698; SSF81698; 5.
DR PROSITE; PS51676; FF; 6.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Isopeptide bond;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1100
FT /note="Transcription elongation regulator 1"
FT /id="PRO_0000076064"
FT DOMAIN 131..164
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 431..464
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 530..563
FT /note="WW 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 661..714
FT /note="FF 1"
FT DOMAIN 727..781
FT /note="FF 2"
FT DOMAIN 793..848
FT /note="FF 3"
FT DOMAIN 898..954
FT /note="FF 4"
FT DOMAIN 956..1012
FT /note="FF 5"
FT DOMAIN 1014..1079
FT /note="FF 6"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 184..254
FT /evidence="ECO:0000255"
FT COILED 607..657
FT /evidence="ECO:0000255"
FT COILED 846..908
FT /evidence="ECO:0000255"
FT MOTIF 628..632
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 36..90
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O14776"
FT MOD_RES 28
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 30
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 41
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 48
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O14776"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14776"
FT MOD_RES 836
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14776"
FT MOD_RES 935
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14776"
FT CROSSLNK 505
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O14776"
FT CROSSLNK 509
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O14776"
FT CROSSLNK 610
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O14776"
FT VAR_SEQ 381..401
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011655"
FT VAR_SEQ 1034
FT /note="R -> S (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10578054"
FT /id="VSP_011656"
FT VAR_SEQ 1035..1100
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10578054"
FT /id="VSP_011657"
FT VARIANT 184..185
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:15489334"
FT CONFLICT 4
FT /note="R -> H (in Ref. 1; BAA86392)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="R -> G (in Ref. 1; BAA86392)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="R -> I (in Ref. 2; AAH39185)"
FT /evidence="ECO:0000305"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:2YSI"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:2YSI"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:2YSI"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:2YSI"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:1E0L"
FT STRAND 438..441
FT /evidence="ECO:0007829|PDB:1E0L"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:2RM0"
FT STRAND 447..451
FT /evidence="ECO:0007829|PDB:1E0L"
FT TURN 452..455
FT /evidence="ECO:0007829|PDB:1E0L"
FT STRAND 456..460
FT /evidence="ECO:0007829|PDB:1E0L"
SQ SEQUENCE 1100 AA; 123788 MW; 54E73FD2381CA38B CRC64;
MAERGGDGGE GERFNPGELR MAQQQALRFR GPAPPPNAVM RGPPPLMRPP PPFGMMRGPP
PPPRPPFGRP PFDPNMPPMP PPGGIPPPMG PPHLQRPPFM PPPMGAMPPP PGMMFPPGMP
PGTAPGAPAL PPTEEIWVEN KTPDGKVYYY NARTRESAWT KPDGVKVIQQ SELTPMLAAQ
AQVQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ
AQAQAQAQAQ AQVQAQAVGA PTPTTSSPAP AVSTSTPTST PSSTTATTTT ATSVAQTVST
PTTQDQTPSS AVSVATPTVS VSAPAPTATP VQTVPQPHPQ TLPPAVPHSV PQPAAAIPAF
PPVMVPPFRV PLPGMPIPLP GVAMMQIVSC PYVKTVATTK TGVLPGMAPP IVPMIHPQVA
IAASPATLAG ATAVSEWTEY KTADGKTYYY NNRTLESTWE KPQELKEKEK LDEKIKEPIK
EASEEPLPME TEEEDPKEEP VKEIKEEPKE EEMTEEEKAA QKAKPVATTP IPGTPWCVVW
TGDERVFFYN PTTRLSMWDR PDDLIGRADV DKIIQEPPHK KGLEDMKKLR HPAPTMLSIQ
KWQFSMSAIK EEQELMEEMN EDEPIKAKKR KRDDNKDIDS EKEAAMEAEI KAARERAIVP
LEARMKQFKD MLLERGVSAF STWEKELHKI VFDPRYLLLN PKERKQVFDQ YVKTRAEEER
REKKNKIMQA KEDFKKMMEE AKFNPRATFS EFAAKHAKDS RFKAIEKMKD REALFNEFVA
AARKKEKEDS KTRGEKIKSD FFELLSNHHL DSQSRWSKVK DKVESDPRYK AVDSSSMRED
LFKQYIEKIA KNLDSEKEKE LERQARIEAS LREREREVQK ARSEQTKEID REREQHKREE
AIQNFKALLS DMVRSSDVSW SDTRRTLRKD HRWESGSLLE REEKEKLFNE HIEALTKKKR
EHFRQLLDET SAITLTSTWK EVKKIIKEDP RCIKFSSSDR KKQREFEEYI RDKYITAKAD
FRTLLKETKF ITYRSKKLIQ ESDQHLKDVE KILQNDKRYL VLDCVPEERR KLIVAYVDDL
DRRGPPPPPT ASEPTRRSTK
