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Transcription initiation factor TFIID subunit 1 (EC 2.7.11.1) (TAFII250) (TBP-associated factor 230 kDa) (p230) (Transcription initiation factor TFIID 230 kDa subunit) (TAFII-230)

 TAF1_DROME              Reviewed;        2129 AA.
P51123; O97068; Q7KSX6; Q7KSX7; Q86LF7; Q9TX96;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
19-JUL-2005, sequence version 3.
30-AUG-2017, entry version 171.
RecName: Full=Transcription initiation factor TFIID subunit 1;
EC=2.7.11.1;
AltName: Full=TAFII250;
AltName: Full=TBP-associated factor 230 kDa;
Short=p230;
AltName: Full=Transcription initiation factor TFIID 230 kDa subunit;
Short=TAFII-230;
Name=Taf1; Synonyms=TAF250; ORFNames=CG17603;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), PROTEIN SEQUENCE OF 63-75 AND
540-546, AND FUNCTION.
PubMed=8504928; DOI=10.1101/gad.7.6.1033;
Kokubo T., Gong D.-W., Yamashita S., Horikoshi M., Roeder R.G.,
Nakatani Y.;
"Drosophila 230-kD TFIID subunit, a functional homolog of the human
cell cycle gene product, negatively regulates DNA binding of the TATA
box-binding subunit of TFIID.";
Genes Dev. 7:1033-1046(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Berkeley;
Celniker S.E., Pfeiffer B., Knafels J., Martin C.H., Mayeda C.A.,
Palazzolo M.J.;
"Complete sequence of the Antennapedia complex of Drosophila.";
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
NUCLEOTIDE SEQUENCE OF 658-2129 (ISOFORM B), AND INTERACTION WITH TBP
AND TAF4.
PubMed=8464492; DOI=10.1038/362511a0;
Weinzierl R.O., Dynlacht B.D., Tjian R.;
"Largest subunit of Drosophila transcription factor IID directs
assembly of a complex containing TBP and a coactivator.";
Nature 362:511-517(1993).
[7]
FUNCTION, AUTOPHOSPHORYLATION, AND ATP-BINDING.
PubMed=8625415; DOI=10.1016/S0092-8674(00)81055-7;
Dikstein R., Ruppert S., Tjian R.;
"TAFII250 is a bipartite protein kinase that phosphorylates the base
transcription factor RAP74.";
Cell 84:781-790(1996).
[8]
INTERACTION WITH TAF6.
STRAIN=Oregon-R;
PubMed=8262073;
Weinzierl R.O., Ruppert S., Dynlacht B.D., Tanese N., Tjian R.;
"Cloning and expression of Drosophila TAFII60 and human TAFII70 reveal
conserved interactions with other subunits of TFIID.";
EMBO J. 12:5303-5309(1993).
[9]
INTERACTION WITH TAF4.
TISSUE=Embryo;
PubMed=8327460; DOI=10.1073/pnas.90.13.5896;
Kokubo T., Gong D.-W., Roeder R.G., Horikoshi M., Nakatani Y.;
"The Drosophila 110-kDa transcription factor TFIID subunit directly
interacts with the N-terminal region of the 230-kDa subunit.";
Proc. Natl. Acad. Sci. U.S.A. 90:5896-5900(1993).
[10]
INTERACTION WITH TAF2.
TISSUE=Embryo;
PubMed=8178153; DOI=10.1126/science.8178153;
Verrijzer C.P., Yokomori K., Chen J.-L., Tjian R.;
"Drosophila TAFII150: similarity to yeast gene TSM-1 and specific
binding to core promoter DNA.";
Science 264:933-941(1994).
[11]
CAUTION.
PubMed=15143281; DOI=10.1126/science.1095001;
Maile T., Kwoczynski S., Katzenberger R.J., Wassarman D.A., Sauer F.;
"TAF1 activates transcription by phosphorylation of serine 33 in
histone H2B.";
Science 304:1010-1014(2004).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286; SER-288; SER-290;
SER-603 AND SER-1740, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
[13]
STRUCTURE BY NMR OF 11-77, AND FUNCTION.
PubMed=9741622; DOI=10.1016/S0092-8674(00)81599-8;
Liu D., Ishima R., Tong K.I., Bagby S., Kokubo T., Muhandiram D.R.,
Kay L.E., Nakatani Y., Ikura M.;
"Solution structure of a TBP-TAF(II)230 complex: protein mimicry of
the minor groove surface of the TATA box unwound by TBP.";
Cell 94:573-583(1998).
-!- FUNCTION: TFIID is a multimeric protein complex that plays a
central role in mediating promoter responses to various activators
and repressors. Largest component and core scaffold of the
complex. Contains N- and C-terminal Ser/Thr kinase domains which
can autophosphorylate or transphosphorylate other transcription
factors. Possesses DNA-binding activity. Essential for progression
of the G1 phase of the cell cycle. Negative regulator of the TATA
box-binding activity of Tbp. {ECO:0000269|PubMed:8504928,
ECO:0000269|PubMed:8625415, ECO:0000269|PubMed:9741622}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ENZYME REGULATION: Autophosphorylates on Ser residues.
-!- SUBUNIT: Belongs to the TFIID complex which is composed of TATA
binding protein (Tbp) and a number of TBP-associated factors
(Tafs). Taf1 is the largest component of the TFIID complex.
Interacts with Tbp, Taf2, Taf4 and Taf6.
{ECO:0000269|PubMed:8178153, ECO:0000269|PubMed:8262073,
ECO:0000269|PubMed:8327460, ECO:0000269|PubMed:8464492}.
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=B;
IsoId=P51123-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=A;
IsoId=P51123-2; Sequence=VSP_014794, VSP_014795;
Name=C;
IsoId=P51123-3; Sequence=VSP_014795;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the TAF1 family. {ECO:0000305}.
-!- CAUTION: The C-terminal Ser/Thr kinase domain was reported to
phosphorylate histone H2B at 'Ser-33' (PubMed:15143281). However,
the paper was retracted because some data, results and conclusions
in the paper are not reliable. {ECO:0000305|PubMed:15143281}.
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EMBL; S61883; AAB26991.2; -; mRNA.
EMBL; AE001572; AAD19815.1; -; Genomic_DNA.
EMBL; AE014297; AAF54102.3; -; Genomic_DNA.
EMBL; AE014297; AAS65116.1; -; Genomic_DNA.
EMBL; AE014297; AAS65117.1; -; Genomic_DNA.
EMBL; BT004888; AAO47866.1; -; mRNA.
PIR; A47371; A47371.
RefSeq; NP_476956.3; NM_057608.5. [P51123-2]
RefSeq; NP_996159.1; NM_206437.2. [P51123-3]
RefSeq; NP_996160.1; NM_206438.2. [P51123-1]
UniGene; Dm.7380; -.
PDB; 1TBA; NMR; -; A=11-77.
PDBsum; 1TBA; -.
DisProt; DP00081; -.
ProteinModelPortal; P51123; -.
SMR; P51123; -.
BioGrid; 66011; 16.
DIP; DIP-228N; -.
IntAct; P51123; 7.
MINT; MINT-788336; -.
STRING; 7227.FBpp0293442; -.
iPTMnet; P51123; -.
PaxDb; P51123; -.
PRIDE; P51123; -.
EnsemblMetazoa; FBtr0081684; FBpp0081184; FBgn0010355. [P51123-2]
EnsemblMetazoa; FBtr0081685; FBpp0089369; FBgn0010355. [P51123-1]
EnsemblMetazoa; FBtr0081686; FBpp0089420; FBgn0010355. [P51123-3]
GeneID; 40813; -.
KEGG; dme:Dmel_CG17603; -.
CTD; 6872; -.
FlyBase; FBgn0010355; Taf1.
eggNOG; KOG0008; Eukaryota.
eggNOG; COG5076; LUCA.
eggNOG; COG5179; LUCA.
GeneTree; ENSGT00390000012659; -.
InParanoid; P51123; -.
KO; K03125; -.
OrthoDB; EOG091G00MO; -.
PhylomeDB; P51123; -.
Reactome; R-DME-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-DME-73776; RNA Polymerase II Promoter Escape.
Reactome; R-DME-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
Reactome; R-DME-75953; RNA Polymerase II Transcription Initiation.
Reactome; R-DME-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
EvolutionaryTrace; P51123; -.
GenomeRNAi; 40813; -.
PRO; PR:P51123; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0010355; -.
ExpressionAtlas; P51123; differential.
Genevisible; P51123; DM.
GO; GO:0005730; C:nucleolus; IDA:FlyBase.
GO; GO:0005654; C:nucleoplasm; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0035102; C:PRC1 complex; TAS:ParkinsonsUK-UCL.
GO; GO:0005669; C:transcription factor TFIID complex; IDA:FlyBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0010485; F:H4 histone acetyltransferase activity; IDA:FlyBase.
GO; GO:0036408; F:histone acetyltransferase activity (H3-K14 specific); IDA:FlyBase.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:FlyBase.
GO; GO:0001129; F:RNA polymerase II transcription factor activity, TBP-class protein binding, involved in preinitiation complex assembly; IPI:FlyBase.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central.
GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0006352; P:DNA-templated transcription, initiation; IDA:BHF-UCL.
GO; GO:0044154; P:histone H3-K14 acetylation; IDA:FlyBase.
GO; GO:0043967; P:histone H4 acetylation; IDA:FlyBase.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:FlyBase.
GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0007221; P:positive regulation of transcription of Notch receptor target; IMP:FlyBase.
GO; GO:0006468; P:protein phosphorylation; ISS:FlyBase.
GO; GO:0046425; P:regulation of JAK-STAT cascade; IMP:FlyBase.
GO; GO:0051123; P:RNA polymerase II transcriptional preinitiation complex assembly; IDA:BHF-UCL.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISS:FlyBase.
Gene3D; 1.10.1100.10; -; 1.
Gene3D; 1.20.920.10; -; 2.
InterPro; IPR017956; AT_hook_DNA-bd_motif.
InterPro; IPR001487; Bromodomain.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR011177; TAF1_animal.
InterPro; IPR009067; TAF_II_230-bd.
InterPro; IPR022591; TFIID_sub1_DUF3591.
Pfam; PF00439; Bromodomain; 2.
Pfam; PF12157; DUF3591; 1.
Pfam; PF09247; TBP-binding; 1.
PIRSF; PIRSF003047; TAF1_animal; 1.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00384; AT_hook; 2.
SMART; SM00297; BROMO; 2.
SUPFAM; SSF47055; SSF47055; 1.
SUPFAM; SSF47370; SSF47370; 2.
PROSITE; PS00633; BROMODOMAIN_1; 2.
PROSITE; PS50014; BROMODOMAIN_2; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Bromodomain;
Cell cycle; Complete proteome; Direct protein sequencing; DNA-binding;
Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Serine/threonine-protein kinase;
Transcription; Transcription regulation; Transferase.
CHAIN 1 2129 Transcription initiation factor TFIID
subunit 1.
/FTId=PRO_0000211216.
DOMAIN 1 423 Protein kinase 1.
DOMAIN 1487 1557 Bromo 1. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
DOMAIN 1515 2065 Protein kinase 2.
DOMAIN 1609 1679 Bromo 2. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
MOTIF 1442 1448 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 2056 2120 Gln-rich.
MOD_RES 286 286 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 288 288 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 290 290 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 315 315 Phosphoserine; by autocatalysis.
{ECO:0000250}.
MOD_RES 603 603 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 1740 1740 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
VAR_SEQ 1805 1837 Missing (in isoform A).
{ECO:0000303|PubMed:12537569,
ECO:0000303|PubMed:8504928}.
/FTId=VSP_014794.
VAR_SEQ 1904 1934 Missing (in isoform A and isoform C).
{ECO:0000303|PubMed:12537569,
ECO:0000303|PubMed:8504928}.
/FTId=VSP_014795.
VARIANT 572 572 P -> S.
CONFLICT 98 98 E -> G (in Ref. 1; AAB26991).
{ECO:0000305}.
CONFLICT 113 113 E -> EERE (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 169 169 E -> D (in Ref. 5; AAO47866).
{ECO:0000305}.
CONFLICT 267 268 KR -> QS (in Ref. 1; AAB26991).
{ECO:0000305}.
CONFLICT 361 361 M -> I (in Ref. 1; AAB26991).
{ECO:0000305}.
CONFLICT 386 386 P -> Q (in Ref. 1; AAB26991).
{ECO:0000305}.
CONFLICT 656 657 KL -> NV (in Ref. 1; AAB26991).
{ECO:0000305}.
CONFLICT 670 671 HG -> QR (in Ref. 6). {ECO:0000305}.
CONFLICT 762 762 F -> Y (in Ref. 1; AAB26991).
{ECO:0000305}.
CONFLICT 932 932 A -> G (in Ref. 6). {ECO:0000305}.
CONFLICT 966 966 L -> M (in Ref. 6). {ECO:0000305}.
CONFLICT 1088 1088 M -> I (in Ref. 5; AAO47866).
{ECO:0000305}.
CONFLICT 1420 1420 D -> G (in Ref. 6). {ECO:0000305}.
CONFLICT 1437 1437 P -> G (in Ref. 6). {ECO:0000305}.
CONFLICT 1462 1462 K -> E (in Ref. 5; AAO47866).
{ECO:0000305}.
CONFLICT 1472 1472 V -> G (in Ref. 6). {ECO:0000305}.
CONFLICT 1487 1487 R -> G (in Ref. 6). {ECO:0000305}.
CONFLICT 1525 1526 RQ -> AKGGTRVARC (in Ref. 6).
{ECO:0000305}.
CONFLICT 1534 1534 M -> N (in Ref. 6). {ECO:0000305}.
CONFLICT 1611 1611 L -> LG (in Ref. 6). {ECO:0000305}.
CONFLICT 1680 1680 K -> E (in Ref. 5; AAO47866).
{ECO:0000305}.
CONFLICT 1685 1685 I -> IRYTKFSKKI (in Ref. 6).
{ECO:0000305}.
CONFLICT 2072 2072 V -> G (in Ref. 6). {ECO:0000305}.
HELIX 23 26 {ECO:0000244|PDB:1TBA}.
TURN 30 32 {ECO:0000244|PDB:1TBA}.
STRAND 42 44 {ECO:0000244|PDB:1TBA}.
TURN 50 52 {ECO:0000244|PDB:1TBA}.
HELIX 53 56 {ECO:0000244|PDB:1TBA}.
TURN 60 62 {ECO:0000244|PDB:1TBA}.
HELIX 64 69 {ECO:0000244|PDB:1TBA}.
SEQUENCE 2129 AA; 239315 MW; 6BF505E5A3EFF160 CRC64;
MEMESDNSDD EGSIGNGLDL TGILFGNIDS EGRLLQDDDG EGRGGTGFDA ELRENIGSLS
KLGLDSMLLE VIDLKEAEPP SDDEEEEDAR PSAVSASEGM SAFDALKAGV KREDGAVKAQ
DDAIDYSDIT ELSEDCPRTP PEETSTYDDL EDAIPASKVE AKLTKDDKEL MPPPSAPMRS
GSGGGIEEPA KSNDASSPSD DSKSTDSKDA DRKLDTPLAD ILPSKYQNVD VRELFPDFRP
QKVLRFSRLF GPGKPTSLPQ IWRHVRKRRR KRNQSRDQKT TNTGGSDSPS DTEEPRKRGF
SLHYAAEPTP AECMSDDEDK LLGDFNSEDV RPEGPDNGEN SDQKPKVADW RFGPAQIWYD
MLEVPDSGEG FNYGFKTKAA STSSQPQLKD ERRVKSPEDD VEDPSIADDA FLMVSQLHWE
DDVVWDGNDI KAKVLQKLNS KTNAAGWLPS SGSRTAGAFS QPGKPSMPVG SGSSKQGSGA
SSKKAQQNAQ AKPAEAPDDT WYSLFPVENE ELIYYKWEDE VIWDAQQVSK VPKPKVLTLD
PNDENIILGI PDDIDPSKIN KSTGPPPKIK IPHPHVKKSK ILLGKAGVIN VLAEDTPPPP
PKSPDRDPFN ISNDTYYTPK TEPTLRLKVG GNLIQHSTPV VELRAPFVPT HMGPMKLRAF
HRPPLKKYSH GPMAQSIPHP VFPLLKTIAK KAKQREVERI ASGGGDVFFM RNPEDLSGRD
GDIVLAEFCE EHPPLINQVG MCSKIKNYYK RKAEKDSGPQ DFVYGEVAFA HTSPFLGILH
PGQCIQAIEN NMYRAPIYPH KMAHNDFLVI RTRNNYWIRS VNSIYTVGQE CPLYEVPGPN
SKRANNFTRD FLQVFIYRLF WKSRDNPRRI RMDDIKQAFP AHSESSIRKR LKQCADFKRT
GMDSNWWVIK PEFRLPSEEE IRAMVSPEQC CAYFSMIAAE QRLKDAGYGE KFLFAPQEDD
DEEAQLKLDD EVKVAPWNTT RAYIQAMRGK CLLQLSGPAD PTGCGEGFSY VRVPNKPTQT
KEEQESQPKR SVTGTDADLR RLPLQRAKEL LRQFKVPEEE IKKLSRWEVI DVVRTLSTEK
AKAGEEGMDK FSRGNRFSIA EHQERYKEEC QRIFDLQNRV LASSEVLSTD EAESSASEES
DLEELGKNLE NMLSNKKTST QLSREREELE RQELLRQLDE EHGGPSGSGG AKGAKGKDDP
GQQMLATNNQ GRILRITRTF RGNDGKEYTR VETVRRQPVI DAYIKIRTTK DEQFIKQFAT
LDEQQKEEMK REKRRIQEQL RRIKRNQERE RLAQLAQNQK LQPGGMPTSL GDPKSSGGHS
HKERDSGYKE VSPSRKKFKL KPDLKLKCGA CGQVGHMRTN KACPLYSGMQ SSLSQSNPSL
ADDFDEQSEK EMTMDDDDLV NVDGTKVTLS SKILKRHGGD DGKRRSGSSS GFTLKVPRDA
MGKKKRRVGG DLHCDYLQRH NKTANRRRTD PVVVLSSILE IIHNELRSMP DVSPFLFPVS
AKKVPDYYRV VTKPMDLQTM REYIRQRRYT SREMFLEDLK QIVDNSLIYN GPQSAYTLAA
QRMFSSCFEL LAEREDKLMR LEKAINPLLD DDDQVALSFI FDKLHSQIKQ LPESWPFLKP
VNKKQVKDYY TVIKRPMDLE TIGKNIEAHR YHSRAEYLAD IELIATNCEQ YNGSDTRYTK
FSKKILEYAQ TQLIEFSEHC GQLENNIAKT QERARENAPE FDEAWGNDDY NFDRGSRASS
PGDDYIDVEG HGGHASSSNS IHRSMGAEAG SSHTAPAVRK PAPPGPGEVK RGRGRPRKQR
DPVEEVKSQN PVKRGRGRPR KDSLASNMSH TQAYFLDEDL QCSTDDEDDD EEEDFQEVSE
DENNAASILD QGERINAPAD AMDGMFDPKN IKTEIDLEAH QMAEEPIGED DSQQVAEAMV
QLSGVGGYYA QQQQDESMDV DPNYDPSDFL AMHKQRQSLG EPSSLQGAFT NFLSHEQDDN
GPYNPAEAST SAASGADLGM DASMAMQMAP EMPVNTMNNG MGIDDDLDIS ESDEEDDGSR
VRIKKEVFDD GDYALQHQQM GQAASQSQIY MVDSSNEPTT LDYQQPPQLD FQQVQEMEQL
QHQVMPPMQS EQLQQQQTPQ GDNDYAWTF


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