MED17_YEAST
ID MED17_YEAST Reviewed; 687 AA.
AC P32569; D3DLS1; Q06790; Q6B1B4;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 17;
DE AltName: Full=Mediator complex subunit 17;
DE AltName: Full=Suppressor of RNA polymerase B 4;
GN Name=SRB4; Synonyms=MED17; OrderedLocusNames=YER022W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLY-353.
RC STRAIN=Z28;
RX PubMed=8324825; DOI=10.1016/0092-8674(93)90362-t;
RA Thompson C.M., Koleske A.J., Chao D.M., Young R.A.;
RT "A multisubunit complex associated with the RNA polymerase II CTD and TATA-
RT binding protein in yeast.";
RL Cell 73:1361-1375(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 430-687.
RC STRAIN=ATCC 44827 / SKQ2N;
RX PubMed=1508147; DOI=10.1007/bf00283839;
RA Neuville P., Aigle M.;
RT "ore2, a mutation affecting proline biosynthesis in the yeast Saccharomyces
RT cerevisiae, leads to a cdc phenotype.";
RL Mol. Gen. Genet. 234:193-200(1992).
RN [6]
RP COMPONENT OF MEDIATOR COMPLEX.
RX PubMed=8187178; DOI=10.1016/0092-8674(94)90221-6;
RA Kim Y.-J., Bjoerklund S., Li Y., Sayre M.H., Kornberg R.D.;
RT "A multiprotein mediator of transcriptional activation and its interaction
RT with the C-terminal repeat domain of RNA polymerase II.";
RL Cell 77:599-608(1994).
RN [7]
RP FUNCTION.
RX PubMed=9845373; DOI=10.1016/s0092-8674(00)81641-4;
RA Holstege F.C.P., Jennings E.G., Wyrick J.J., Lee T.I., Hengartner C.J.,
RA Green M.R., Golub T.R., Lander E.S., Young R.A.;
RT "Dissecting the regulatory circuitry of a eukaryotic genome.";
RL Cell 95:717-728(1998).
RN [8]
RP INTERACTION WITH GAL4; SRB2 AND SRB6.
RX PubMed=9660972; DOI=10.1016/s1097-2765(00)80088-x;
RA Koh S.S., Ansari A.Z., Ptashne M., Young R.A.;
RT "An activator target in the RNA polymerase II holoenzyme.";
RL Mol. Cell 1:895-904(1998).
RN [9]
RP INTERACTION WITH MED6 AND SRB6.
RX PubMed=9671455; DOI=10.1128/mcb.18.8.4455;
RA Lee T.I., Wyrick J.J., Koh S.S., Jennings E.G., Gadbois E.L., Young R.A.;
RT "Interplay of positive and negative regulators in transcription initiation
RT by RNA polymerase II holoenzyme.";
RL Mol. Cell. Biol. 18:4455-4462(1998).
RN [10]
RP INTERACTION WITH MED11 AND ROX3, FUNCTION OF THE MEDIATOR COMPLEX, AND
RP INTERACTION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
RX PubMed=11555651; DOI=10.1074/jbc.m105961200;
RA Kang J.S., Kim S.H., Hwang M.S., Han S.J., Lee Y.C., Kim Y.-J.;
RT "The structural and functional organization of the yeast mediator
RT complex.";
RL J. Biol. Chem. 276:42003-42010(2001).
RN [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [12]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [13]
RP NOMENCLATURE.
RX PubMed=15175151; DOI=10.1016/j.molcel.2004.05.011;
RA Bourbon H.-M., Aguilera A., Ansari A.Z., Asturias F.J., Berk A.J.,
RA Bjoerklund S., Blackwell T.K., Borggrefe T., Carey M., Carlson M.,
RA Conaway J.W., Conaway R.C., Emmons S.W., Fondell J.D., Freedman L.P.,
RA Fukasawa T., Gustafsson C.M., Han M., He X., Herman P.K., Hinnebusch A.G.,
RA Holmberg S., Holstege F.C.P., Jaehning J.A., Kim Y.-J., Kuras L., Leutz A.,
RA Lis J.T., Meisterernest M., Naeaer A.M., Nasmyth K., Parvin J.D.,
RA Ptashne M., Reinberg D., Ronne H., Sadowski I., Sakurai H., Sipiczki M.,
RA Sternberg P.W., Stillman D.J., Strich R., Struhl K., Svejstrup J.Q.,
RA Tuck S., Winston F., Roeder R.G., Kornberg R.D.;
RT "A unified nomenclature for protein subunits of mediator complexes linking
RT transcriptional regulators to RNA polymerase II.";
RL Mol. Cell 14:553-557(2004).
RN [14]
RP TOPOLOGY OF THE MEDIATOR COMPLEX.
RX PubMed=15477388; DOI=10.1093/nar/gkh878;
RA Guglielmi B., van Berkum N.L., Klapholz B., Bijma T., Boube M.,
RA Boschiero C., Bourbon H.-M., Holstege F.C.P., Werner M.;
RT "A high resolution protein interaction map of the yeast Mediator complex.";
RL Nucleic Acids Res. 32:5379-5391(2004).
RN [15]
RP INTERACTION WITH MED6.
RX PubMed=15710619; DOI=10.1074/jbc.m413466200;
RA Baumli S., Hoeppner S., Cramer P.;
RT "A conserved mediator hinge revealed in the structure of the MED7-MED21
RT (Med7-Srb7) heterodimer.";
RL J. Biol. Chem. 280:18171-18178(2005).
RN [16]
RP CHARACTERIZATION OF THE MEDIATOR COMPLEX.
RX PubMed=16002404; DOI=10.1074/jbc.c500150200;
RA Takagi Y., Chadick J.Z., Davis J.A., Asturias F.J.;
RT "Preponderance of free mediator in the yeast Saccharomyces cerevisiae.";
RL J. Biol. Chem. 280:31200-31207(2005).
RN [17]
RP FUNCTION OF THE MEDIATOR COMPLEX.
RX PubMed=16076843; DOI=10.1074/jbc.m506067200;
RA Nair D., Kim Y., Myers L.C.;
RT "Mediator and TFIIH govern carboxyl-terminal domain-dependent transcription
RT in yeast extracts.";
RL J. Biol. Chem. 280:33739-33748(2005).
RN [18]
RP FUNCTION OF THE MEDIATOR COMPLEX.
RX PubMed=16263706; DOI=10.1074/jbc.m508253200;
RA Takagi Y., Kornberg R.D.;
RT "Mediator as a general transcription factor.";
RL J. Biol. Chem. 281:80-89(2006).
RN [19]
RP SUBCELLULAR LOCATION.
RX PubMed=16630888; DOI=10.1016/j.molcel.2006.03.023;
RA Andrau J.-C., van de Pasch L., Lijnzaad P., Bijma T., Koerkamp M.G.,
RA van de Peppel J., Werner M., Holstege F.C.P.;
RT "Genome-wide location of the coactivator mediator: binding without
RT activation and transient Cdk8 interaction on DNA.";
RL Mol. Cell 22:179-192(2006).
RN [20]
RP ASSOCIATION WITH PROMOTER REGIONS.
RX PubMed=16429153; DOI=10.1038/nsmb1049;
RA Fan X., Chou D.M., Struhl K.;
RT "Activator-specific recruitment of Mediator in vivo.";
RL Nat. Struct. Mol. Biol. 13:117-120(2006).
RN [21]
RP CHARACTERIZATION OF THE MEDIATOR COMPLEX, AND INTERACTION OF THE MEDIATOR
RP COMPLEX WITH RNA POLYMERASE II.
RX PubMed=17192271; DOI=10.1074/jbc.m609484200;
RA Baidoobonso S.M., Guidi B.W., Myers L.C.;
RT "Med19(Rox3) regulates intermodule interactions in the Saccharomyces
RT cerevisiae mediator complex.";
RL J. Biol. Chem. 282:5551-5559(2007).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [24]
RP ELECTRON MICROSCOPY OF MEDIATOR COMPLEX IN COMPLEX WITH RNA POLYMERASE II.
RX PubMed=12191485; DOI=10.1016/s1097-2765(02)00598-1;
RA Davis J.A., Takagi Y., Kornberg R.D., Asturias F.J.;
RT "Structure of the yeast RNA polymerase II holoenzyme: mediator conformation
RT and polymerase interaction.";
RL Mol. Cell 10:409-415(2002).
RN [25]
RP ELECTRON MICROSCOPY OF THE MEDIATOR COMPLEX HEAD MODULE, FUNCTION OF THE
RP MEDIATOR COMPLEX HEAD MODULE, INTERACTION OF THE MEDIATOR COMPLEX HEAD
RP MODULE WITH RNA POLYMERASE II AND TFIIF, AND INTERACTION WITH MED6; MED8;
RP MED11; SRB2; SRB5 AND SRB6.
RX PubMed=16885025; DOI=10.1016/j.molcel.2006.06.007;
RA Takagi Y., Calero G., Komori H., Brown J.A., Ehrensberger A.H., Hudmon A.,
RA Asturias F.J., Kornberg R.D.;
RT "Head module control of mediator interactions.";
RL Mol. Cell 23:355-364(2006).
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. The Mediator complex, having a compact
CC conformation in its free form, is recruited to promoters by direct
CC interactions with regulatory proteins and serves for the assembly of a
CC functional preinitiation complex with RNA polymerase II and the general
CC transcription factors. The Mediator complex unfolds to an extended
CC conformation and partially surrounds RNA polymerase II, specifically
CC interacting with the unphosphorylated form of the C-terminal domain
CC (CTD) of RNA polymerase II. The Mediator complex dissociates from the
CC RNA polymerase II holoenzyme and stays at the promoter when
CC transcriptional elongation begins. {ECO:0000269|PubMed:11555651,
CC ECO:0000269|PubMed:16076843, ECO:0000269|PubMed:16263706,
CC ECO:0000269|PubMed:16885025, ECO:0000269|PubMed:9845373}.
CC -!- SUBUNIT: Component of the Mediator complex, which is composed of at
CC least 21 subunits that form three structurally distinct submodules. The
CC Mediator head module contains MED6, MED8, MED11, SRB4/MED17,
CC SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the middle module
CC contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21
CC and SOH1/MED31, and the tail module contains MED2, PGD1/MED3,
CC RGR1/MED14, GAL11/MED15 and SIN4/MED16. The head and the middle modules
CC interact directly with RNA polymerase II, whereas the elongated tail
CC module interacts with gene-specific regulatory proteins. The head
CC module may also interact with the TFIIF complex. SRB4/MED17 interacts
CC directly with MED6, MED11, ROX3/MED19, SRB2/MED20 and SRB6/MED22.
CC Interacts directly with the activator GAL4.
CC {ECO:0000269|PubMed:11555651, ECO:0000269|PubMed:15710619,
CC ECO:0000269|PubMed:16885025, ECO:0000269|PubMed:17192271,
CC ECO:0000269|PubMed:9660972, ECO:0000269|PubMed:9671455}.
CC -!- INTERACTION:
CC P32569; Q99278: MED11; NbExp=21; IntAct=EBI-18025, EBI-27213;
CC P32569; P38782: MED6; NbExp=7; IntAct=EBI-18025, EBI-10667;
CC P32569; P38304: MED8; NbExp=9; IntAct=EBI-18025, EBI-20932;
CC P32569; P38633: SOH1; NbExp=4; IntAct=EBI-18025, EBI-17658;
CC P32569; P32570: SRB6; NbExp=11; IntAct=EBI-18025, EBI-18039;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16630888}.
CC -!- MISCELLANEOUS: Present with 1720 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 17 family.
CC {ECO:0000305}.
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DR EMBL; L12026; AAA02632.1; -; Unassigned_DNA.
DR EMBL; U18778; AAB64555.1; -; Genomic_DNA.
DR EMBL; AY693166; AAT93185.1; -; Genomic_DNA.
DR EMBL; X57338; CAA40613.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07675.1; -; Genomic_DNA.
DR PIR; A40711; A40711.
DR RefSeq; NP_010939.1; NM_001178913.1.
DR PDB; 3J1O; EM; 16.00 A; I=197-616, I=669-687.
DR PDB; 3RJ1; X-ray; 4.30 A; B/I/P=109-616, B/I/P=669-687.
DR PDB; 4GWP; X-ray; 4.20 A; B=1-687.
DR PDB; 4GWQ; X-ray; 4.50 A; B=1-687.
DR PDB; 4H62; X-ray; 3.00 A; Q=377-687.
DR PDB; 4V1O; EM; 9.70 A; W=2-687.
DR PDB; 5OQM; EM; 5.80 A; d=1-687.
DR PDB; 5SVA; EM; 15.30 A; P=1-687.
DR PDBsum; 3J1O; -.
DR PDBsum; 3RJ1; -.
DR PDBsum; 4GWP; -.
DR PDBsum; 4GWQ; -.
DR PDBsum; 4H62; -.
DR PDBsum; 4V1O; -.
DR PDBsum; 5OQM; -.
DR PDBsum; 5SVA; -.
DR AlphaFoldDB; P32569; -.
DR SMR; P32569; -.
DR BioGRID; 36756; 186.
DR ComplexPortal; CPX-3226; Core mediator complex.
DR DIP; DIP-152N; -.
DR IntAct; P32569; 27.
DR MINT; P32569; -.
DR STRING; 4932.YER022W; -.
DR iPTMnet; P32569; -.
DR MaxQB; P32569; -.
DR PaxDb; P32569; -.
DR PRIDE; P32569; -.
DR EnsemblFungi; YER022W_mRNA; YER022W; YER022W.
DR GeneID; 856743; -.
DR KEGG; sce:YER022W; -.
DR SGD; S000000824; SRB4.
DR VEuPathDB; FungiDB:YER022W; -.
DR eggNOG; ENOG502QS9H; Eukaryota.
DR HOGENOM; CLU_023188_0_0_1; -.
DR InParanoid; P32569; -.
DR OMA; PKINDKR; -.
DR BioCyc; YEAST:G3O-30206-MON; -.
DR PRO; PR:P32569; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P32569; protein.
DR GO; GO:0070847; C:core mediator complex; IDA:SGD.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IDA:SGD.
DR GO; GO:0001139; F:RNA polymerase II complex recruiting activity; IMP:SGD.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IDA:ComplexPortal.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IMP:SGD.
DR InterPro; IPR019313; Mediator_Med17.
DR PANTHER; PTHR13114; PTHR13114; 1.
DR Pfam; PF10156; Med17; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..687
FT /note="Mediator of RNA polymerase II transcription subunit
FT 17"
FT /id="PRO_0000096366"
FT REGION 30..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 353
FT /note="G->C: In SRB4-1; suppresses the phenotypic defects
FT of an RNA polymerase II CTD truncation."
FT /evidence="ECO:0000269|PubMed:8324825"
FT CONFLICT 430..431
FT /note="QL -> PI (in Ref. 5; CAA40613)"
FT /evidence="ECO:0000305"
FT CONFLICT 647
FT /note="I -> T (in Ref. 4; AAT93185)"
FT /evidence="ECO:0000305"
FT STRAND 388..396
FT /evidence="ECO:0007829|PDB:4H62"
FT STRAND 403..408
FT /evidence="ECO:0007829|PDB:4H62"
FT HELIX 425..449
FT /evidence="ECO:0007829|PDB:4H62"
FT HELIX 450..455
FT /evidence="ECO:0007829|PDB:4H62"
FT STRAND 457..461
FT /evidence="ECO:0007829|PDB:4H62"
FT STRAND 464..468
FT /evidence="ECO:0007829|PDB:4H62"
FT STRAND 470..479
FT /evidence="ECO:0007829|PDB:4H62"
FT HELIX 498..524
FT /evidence="ECO:0007829|PDB:4H62"
FT TURN 525..527
FT /evidence="ECO:0007829|PDB:4H62"
FT HELIX 535..538
FT /evidence="ECO:0007829|PDB:4H62"
FT HELIX 542..565
FT /evidence="ECO:0007829|PDB:4H62"
FT TURN 566..569
FT /evidence="ECO:0007829|PDB:4H62"
FT STRAND 574..579
FT /evidence="ECO:0007829|PDB:4H62"
FT HELIX 597..604
FT /evidence="ECO:0007829|PDB:4H62"
FT HELIX 607..610
FT /evidence="ECO:0007829|PDB:4H62"
FT STRAND 614..620
FT /evidence="ECO:0007829|PDB:4H62"
FT STRAND 630..636
FT /evidence="ECO:0007829|PDB:4H62"
FT STRAND 640..642
FT /evidence="ECO:0007829|PDB:4H62"
FT STRAND 644..650
FT /evidence="ECO:0007829|PDB:4H62"
FT TURN 654..656
FT /evidence="ECO:0007829|PDB:4H62"
FT STRAND 660..665
FT /evidence="ECO:0007829|PDB:4H62"
FT HELIX 667..680
FT /evidence="ECO:0007829|PDB:4H62"
SQ SEQUENCE 687 AA; 78476 MW; D25B2993A1BADFD6 CRC64;
MTTEDPDSNH LSSETGIKLA LDPNLITLAL SSNPNSSLHS PTSDEPVPES AGKADTSIRL
EGDELENKTK KDNDKNLKFL KNKDSLVSNP HEIYGSMPLE QLIPIILRQR GPGFKFVDLN
EKELQNEIKQ LGSDSSDGHN SEKKDTDGAD ENVQIGEDFM EVDYEDKDNP VDSRNETDHK
TNENGETDDN IETVMTQEQF VKRRRDMLEH INLAMNESSL ALEFVSLLLS SVKESTGMSS
MSPFLRKVVK PSSLNSDKIP YVAPTKKEYI ELDILNKGWK LQSLNESKDL LRASFNKLSS
ILQNEHDYWN KIMQSISNKD VIFKIRDRTS GQKLLAIKYG YEDSGSTYKH DRGIANIRNN
IESQNLDLIP HSSSVFKGTD FVHSVKKFLR VRIFTKIESE DDYILSGESV MDRDSESEEA
ETKDIRKQIQ LLKKIIFEKE LMYQIKKECA LLISYGVSIE NENKVIIELP NEKFEIELLS
LDDDSIVNHE QDLPKINDKR ANLMLVMLRL LLVVIFKKTL RSRISSPHGL INLNVDDDIL
IIRPILGKVR FANYKLLLKK IIKDYVLDIV PGSSITETEV EREQPQENKN IDDENITKLN
KEIRAFDKLL NIPRRELKIN LPLTEHKSPN LSLMLESPNY CNALIHIKFS AGTEANAVSF
DTTFSDFKEV EDFLHFIVAE YIQQKKV
