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Mediator of RNA polymerase II transcription subunit 15 (Autonomous replication regulatory protein 3) (Basal expression activator protein 1) (Defective silencing suppressor protein 4) (Mediator complex subunit 15) (Transcription regulatory protein GAL11) (Ty insertion suppressor protein 13)

 MED15_YEAST             Reviewed;        1081 AA.
P19659; D6W217; Q08221;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 3.
25-OCT-2017, entry version 165.
RecName: Full=Mediator of RNA polymerase II transcription subunit 15;
AltName: Full=Autonomous replication regulatory protein 3;
AltName: Full=Basal expression activator protein 1;
AltName: Full=Defective silencing suppressor protein 4;
AltName: Full=Mediator complex subunit 15;
AltName: Full=Transcription regulatory protein GAL11;
AltName: Full=Ty insertion suppressor protein 13;
Name=GAL11; Synonyms=ABE1, MED15, RAR3, SDS4, SPT13;
OrderedLocusNames=YOL051W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=3062377; DOI=10.1128/MCB.8.11.4991;
Suzuki Y., Nogi Y., Abe A., Fukasawa T.;
"GAL11 protein, an auxiliary transcription activator for genes
encoding galactose-metabolizing enzymes in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 8:4991-4999(1988).
[2]
ERRATUM, AND SEQUENCE REVISION.
PubMed=1406662; DOI=10.1128/MCB.12.10.4806;
Suzuki Y., Nogi Y., Abe A., Fukasawa T.;
Mol. Cell. Biol. 12:4806-4806(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-352.
STRAIN=ATCC 90843 / S288c / FY73;
PubMed=8789261;
DOI=10.1002/(SICI)1097-0061(199601)12:1<67::AID-YEA884>3.0.CO;2-F;
Mannhaupt G., Vetter I., Schwarzlose C., Mitzel S., Feldmann H.;
"Analysis of a 26 kb region on the left arm of yeast chromosome XV.";
Yeast 12:67-76(1996).
[6]
CHARACTERIZATION.
PubMed=2005915; DOI=10.1128/MCB.11.4.2311;
Long R.M., Mylin L.M., Hopper J.E.;
"GAL11 (SPT13), a transcriptional regulator of diverse yeast genes,
affects the phosphorylation state of GAL4, a highly specific
transcriptional activator.";
Mol. Cell. Biol. 11:2311-2314(1991).
[7]
COMPONENT OF MEDIATOR COMPLEX.
PubMed=8187178; DOI=10.1016/0092-8674(94)90221-6;
Kim Y.-J., Bjoerklund S., Li Y., Sayre M.H., Kornberg R.D.;
"A multiprotein mediator of transcriptional activation and its
interaction with the C-terminal repeat domain of RNA polymerase II.";
Cell 77:599-608(1994).
[8]
INTERACTION WITH GAL4.
PubMed=11478912; DOI=10.1021/bi010011k;
Jeong C.-J., Yang S.-H., Xie Y., Zhang L., Johnston S.A., Kodadek T.;
"Evidence that Gal11 protein is a target of the Gal4 activation domain
in the mediator.";
Biochemistry 40:9421-9427(2001).
[9]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[10]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[11]
NOMENCLATURE.
PubMed=15175151; DOI=10.1016/j.molcel.2004.05.011;
Bourbon H.-M., Aguilera A., Ansari A.Z., Asturias F.J., Berk A.J.,
Bjoerklund S., Blackwell T.K., Borggrefe T., Carey M., Carlson M.,
Conaway J.W., Conaway R.C., Emmons S.W., Fondell J.D., Freedman L.P.,
Fukasawa T., Gustafsson C.M., Han M., He X., Herman P.K.,
Hinnebusch A.G., Holmberg S., Holstege F.C.P., Jaehning J.A.,
Kim Y.-J., Kuras L., Leutz A., Lis J.T., Meisterernest M.,
Naeaer A.M., Nasmyth K., Parvin J.D., Ptashne M., Reinberg D.,
Ronne H., Sadowski I., Sakurai H., Sipiczki M., Sternberg P.W.,
Stillman D.J., Strich R., Struhl K., Svejstrup J.Q., Tuck S.,
Winston F., Roeder R.G., Kornberg R.D.;
"A unified nomenclature for protein subunits of mediator complexes
linking transcriptional regulators to RNA polymerase II.";
Mol. Cell 14:553-557(2004).
[12]
TOPOLOGY OF THE MEDIATOR COMPLEX.
PubMed=15477388; DOI=10.1093/nar/gkh878;
Guglielmi B., van Berkum N.L., Klapholz B., Bijma T., Boube M.,
Boschiero C., Bourbon H.-M., Holstege F.C.P., Werner M.;
"A high resolution protein interaction map of the yeast Mediator
complex.";
Nucleic Acids Res. 32:5379-5391(2004).
[13]
FUNCTION OF THE MEDIATOR COMPLEX.
PubMed=16076843; DOI=10.1074/jbc.M506067200;
Nair D., Kim Y., Myers L.C.;
"Mediator and TFIIH govern carboxyl-terminal domain-dependent
transcription in yeast extracts.";
J. Biol. Chem. 280:33739-33748(2005).
[14]
FUNCTION.
PubMed=16109375; DOI=10.1016/j.molcel.2005.06.033;
van de Peppel J., Kettelarij N., van Bakel H., Kockelkorn T.T.J.P.,
van Leenen D., Holstege F.C.P.;
"Mediator expression profiling epistasis reveals a signal transduction
pathway with antagonistic submodules and highly specific downstream
targets.";
Mol. Cell 19:511-522(2005).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone
signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[16]
FUNCTION OF THE MEDIATOR COMPLEX.
PubMed=16263706; DOI=10.1074/jbc.M508253200;
Takagi Y., Kornberg R.D.;
"Mediator as a general transcription factor.";
J. Biol. Chem. 281:80-89(2006).
[17]
SUBCELLULAR LOCATION.
PubMed=16630888; DOI=10.1016/j.molcel.2006.03.023;
Andrau J.-C., van de Pasch L., Lijnzaad P., Bijma T., Koerkamp M.G.,
van de Peppel J., Werner M., Holstege F.C.P.;
"Genome-wide location of the coactivator mediator: binding without
activation and transient Cdk8 interaction on DNA.";
Mol. Cell 22:179-192(2006).
[18]
ASSOCIATION WITH PROMOTER REGIONS.
PubMed=16429153; DOI=10.1038/nsmb1049;
Fan X., Chou D.M., Struhl K.;
"Activator-specific recruitment of Mediator in vivo.";
Nat. Struct. Mol. Biol. 13:117-120(2006).
[19]
CHARACTERIZATION OF THE MEDIATOR COMPLEX, AND INTERACTION OF THE
MEDIATOR COMPLEX WITH RNA POLYMERASE II.
PubMed=17192271; DOI=10.1074/jbc.M609484200;
Baidoobonso S.M., Guidi B.W., Myers L.C.;
"Med19(Rox3) regulates intermodule interactions in the Saccharomyces
cerevisiae mediator complex.";
J. Biol. Chem. 282:5551-5559(2007).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1034, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1034, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335; SER-736; SER-752;
THR-793; SER-1003; SER-1018 AND SER-1034, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783; SER-785; SER-789;
THR-793; SER-831; SER-1003; SER-1008; SER-1018 AND SER-1034, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[25]
ELECTRON MICROSCOPY OF MEDIATOR COMPLEX IN COMPLEX WITH RNA POLYMERASE
II.
PubMed=12191485; DOI=10.1016/S1097-2765(02)00598-1;
Davis J.A., Takagi Y., Kornberg R.D., Asturias F.J.;
"Structure of the yeast RNA polymerase II holoenzyme: mediator
conformation and polymerase interaction.";
Mol. Cell 10:409-415(2002).
-!- FUNCTION: Component of the Mediator complex, a coactivator
involved in the regulated transcription of nearly all RNA
polymerase II-dependent genes. Mediator functions as a bridge to
convey information from gene-specific regulatory proteins to the
basal RNA polymerase II transcription machinery. The Mediator
complex, having a compact conformation in its free form, is
recruited to promoters by direct interactions with regulatory
proteins and serves for the assembly of a functional preinitiation
complex with RNA polymerase II and the general transcription
factors. The Mediator complex unfolds to an extended conformation
and partially surrounds RNA polymerase II, specifically
interacting with the unphosphorylated form of the C-terminal
domain (CTD) of RNA polymerase II. The Mediator complex
dissociates from the RNA polymerase II holoenzyme and stays at the
promoter when transcriptional elongation begins. It has an
important role in the negative regulation of Ty transcription.
{ECO:0000269|PubMed:16076843, ECO:0000269|PubMed:16109375,
ECO:0000269|PubMed:16263706}.
-!- SUBUNIT: Component of the Mediator complex, which is composed of
at least 21 subunits that form three structurally distinct
submodules. The Mediator head module contains MED6, MED8, MED11,
SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the
middle module contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9,
NUT2/MED10, SRB7/MED21 and SOH1/MED31, and the tail module
contains MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16.
The head and the middle modules interact directly with RNA
polymerase II, whereas the elongated tail module interacts with
gene-specific regulatory proteins. GAL11/MED15 interacts directly
with the activator GAL4. {ECO:0000269|PubMed:11478912,
ECO:0000269|PubMed:17192271}.
-!- INTERACTION:
P12383:PDR1; NbExp=5; IntAct=EBI-7305, EBI-13019;
P36956-1:SREBF1 (xeno); NbExp=3; IntAct=EBI-7305, EBI-948328;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
ECO:0000269|PubMed:16630888}.
-!- MISCELLANEOUS: Present with 606 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the Mediator complex subunit 15 family.
{ECO:0000305}.
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EMBL; M22481; AAA34622.1; -; Genomic_DNA.
EMBL; Z74793; CAA99056.1; -; Genomic_DNA.
EMBL; X91067; CAA62537.1; -; Genomic_DNA.
EMBL; BK006948; DAA10733.1; -; Genomic_DNA.
PIR; S66736; S66736.
RefSeq; NP_014591.1; NM_001183305.1.
PDB; 2K0N; NMR; -; A=6-90.
PDB; 2LPB; NMR; -; A=158-238.
PDBsum; 2K0N; -.
PDBsum; 2LPB; -.
ProteinModelPortal; P19659; -.
SMR; P19659; -.
BioGrid; 34353; 158.
DIP; DIP-2334N; -.
IntAct; P19659; 20.
MINT; MINT-635654; -.
STRING; 4932.YOL051W; -.
iPTMnet; P19659; -.
MaxQB; P19659; -.
PRIDE; P19659; -.
EnsemblFungi; YOL051W; YOL051W; YOL051W.
GeneID; 854106; -.
KEGG; sce:YOL051W; -.
EuPathDB; FungiDB:YOL051W; -.
SGD; S000005411; GAL11.
HOGENOM; HOG000113522; -.
InParanoid; P19659; -.
KO; K15158; -.
OMA; RFKHRQE; -.
OrthoDB; EOG092C0QLI; -.
BioCyc; YEAST:G3O-33462-MONOMER; -.
EvolutionaryTrace; P19659; -.
PRO; PR:P19659; -.
Proteomes; UP000002311; Chromosome XV.
GO; GO:0070847; C:core mediator complex; IDA:SGD.
GO; GO:0016592; C:mediator complex; IEA:InterPro.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IDA:SGD.
GO; GO:0001128; F:RNA polymerase II transcription coactivator activity involved in preinitiation complex assembly; IDA:SGD.
GO; GO:0001095; F:TFIIE-class transcription factor binding; IDA:SGD.
GO; GO:0001097; F:TFIIH-class transcription factor binding; IDA:SGD.
GO; GO:0001135; F:transcription factor activity, RNA polymerase II transcription factor recruiting; IMP:SGD.
GO; GO:0001088; F:transcription factor activity, TFIIE-class binding; IDA:SGD.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:SGD.
GO; GO:2000219; P:positive regulation of invasive growth in response to glucose limitation; IMP:SGD.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:SGD.
GO; GO:0070202; P:regulation of establishment of protein localization to chromosome; IMP:SGD.
GO; GO:0051123; P:RNA polymerase II transcriptional preinitiation complex assembly; IDA:SGD.
CDD; cd12191; gal11_coact; 1.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR033789; Gal11_coact.
InterPro; IPR008626; Mediator_Med15_fun.
Pfam; PF05397; Med15_fungi; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Complete proteome; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Transcription;
Transcription regulation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 1081 Mediator of RNA polymerase II
transcription subunit 15.
/FTId=PRO_0000096363.
REPEAT 422 423 1.
REPEAT 424 425 2.
REPEAT 426 427 3.
REPEAT 428 429 4.
REPEAT 430 431 5.
REPEAT 432 433 6.
REPEAT 434 435 7.
REPEAT 436 437 8.
REPEAT 438 439 9.
REPEAT 440 441 10.
REPEAT 442 443 11.
REPEAT 444 445 12; approximate.
REPEAT 446 447 13; approximate.
REPEAT 448 449 14.
REPEAT 450 451 15.
REPEAT 452 453 16.
REPEAT 454 455 17.
REPEAT 456 457 18.
REPEAT 458 459 19.
REPEAT 460 461 20.
REPEAT 462 463 21.
REPEAT 464 465 22.
REPEAT 466 467 23.
REPEAT 468 469 24.
REPEAT 470 471 25.
REPEAT 472 473 26.
REPEAT 474 475 27.
REPEAT 476 477 28.
REPEAT 478 479 29.
REPEAT 480 481 30.
REGION 422 481 30 X 2 AA approximate tandem repeats of
Q-A.
COMPBIAS 147 158 Poly-Gln.
COMPBIAS 674 696 Poly-Gln.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 335 335 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 736 736 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 752 752 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 783 783 Phosphoserine.
{ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:19779198}.
MOD_RES 785 785 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 789 789 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 793 793 Phosphothreonine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 831 831 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 1003 1003 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 1008 1008 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 1018 1018 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 1034 1034 Phosphoserine.
{ECO:0000244|PubMed:17287358,
ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
CONFLICT 171 171 N -> T (in Ref. 1; AAA34622).
{ECO:0000305}.
CONFLICT 302 302 P -> Q (in Ref. 1; AAA34622).
{ECO:0000305}.
CONFLICT 499 499 N -> T (in Ref. 1; AAA34622).
{ECO:0000305}.
CONFLICT 751 751 P -> Q (in Ref. 1; AAA34622).
{ECO:0000305}.
STRAND 8 11 {ECO:0000244|PDB:2K0N}.
HELIX 14 35 {ECO:0000244|PDB:2K0N}.
HELIX 41 58 {ECO:0000244|PDB:2K0N}.
HELIX 63 89 {ECO:0000244|PDB:2K0N}.
HELIX 164 170 {ECO:0000244|PDB:2LPB}.
HELIX 172 174 {ECO:0000244|PDB:2LPB}.
HELIX 180 183 {ECO:0000244|PDB:2LPB}.
HELIX 196 199 {ECO:0000244|PDB:2LPB}.
HELIX 201 204 {ECO:0000244|PDB:2LPB}.
HELIX 210 232 {ECO:0000244|PDB:2LPB}.
SEQUENCE 1081 AA; 120309 MW; 275C78721B5415C7 CRC64;
MSAAPVQDKD TLSNAERAKN VNGLLQVLMD INTLNGGSSD TADKIRIHAK NFEAALFAKS
SSKKEYMDSM NEKVAVMRNT YNTRKNAVTA AAANNNIKPV EQHHINNLKN SGNSANNMNV
NMNLNPQMFL NQQAQARQQV AQQLRNQQQQ QQQQQQQQRR QLTPQQQQLV NQMKVAPIPK
QLLQRIPNIP PNINTWQQVT ALAQQKLLTP QDMEAAKEVY KIHQQLLFKA RLQQQQAQAQ
AQANNNNNGL PQNGNINNNI NIPQQQQMQP PNSSANNNPL QQQSSQNTVP NVLNQINQIF
SPEEQRSLLQ EAIETCKNFE KTQLGSTMTE PVKQSFIRKY INQKALRKIQ ALRDVKNNNN
ANNNGSNLQR AQNVPMNIIQ QQQQQNTNNN DTIATSATPN AAAFSQQQNA SSKLYQMQQQ
QQAQAQAQAQ AQAQAQAQAQ AQAAQAAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ
AHAQHQPSQQ PQQAQQQPNP LHGLTPTAKD VEVIKQLSLD ASKTNLRLTD VTNSLSNEEK
EKIKMKLKQG QKLFVQVSNF APQVYIITKN ENFLKEVFQL RIFVKEILEK CAEGIFVVKL
DTVDRLIIKY QKYWESMRIQ ILRRQAILRQ QQQMANNNGN PGTTSTGNNN NIATQQNMQQ
SLQQMQHLQQ LKMQQQQQQQ QQQQQQQQQQ QQQQQQHIYP SSTPGVANYS AMANAPGNNI
PYMNHKNTSS MDFLNSMENT PKVPVSAAAT PSLNKTINGK VNGRTKSNTI PVTSIPSTNK
KLSISNAASQ QPTPRSASNT AKSTPNTNPS PLKTQTKNGT PNPNNMKTVQ SPMGAQPSYN
SAIIENAFRK EELLLKDLEI RKLEISSRFK HRQEIFKDSP MDLFMSTLGD CLGIKDEEML
TSCTIPKAVV DHINGSGKRK PTKAAQRARD QDSIDISIKD NKLVMKSKFN KSNRSYSIAL
SNVAAIFKGI GGNFKDLSTL VHSSSPSTSS NMDVGNPRKR KASVLEISPQ DSIASVLSPD
SNIMSDSKKI KVDSPDDPFM TKSGATTSEK QEVTNEAPFL TSGTSSEQFN VWDWNNWTSA
T


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