ARP4_YEAST
ID ARP4_YEAST Reviewed; 489 AA.
AC P80428; D6VWA2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Actin-related protein 4;
DE AltName: Full=Actin-like protein ARP4;
DE Short=Actin-like protein 4;
GN Name=ARP4; Synonyms=ACT3; OrderedLocusNames=YJL081C; ORFNames=J1012;
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].
RX PubMed=8058791; DOI=10.1073/pnas.91.17.8258;
RA Harata M., Karwan A., Wintersberger U.;
RT "An essential gene of Saccharomyces cerevisiae coding for an actin-related
RT protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:8258-8262(1994).
RN [2]
RP ERRATUM OF PUBMED:8058791.
RA Harata M., Karwan A., Wintersberger U.;
RL Proc. Natl. Acad. Sci. U.S.A. 91:10757-10757(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7483841; DOI=10.1002/yea.320110709;
RA Miosga T., Schaaff-Gerstenschlaeger I., Chalwatzis N., Baur A., Boles E.,
RA Fournier C., Schmitt S., Velten C., Wilhelm N., Zimmermann F.K.;
RT "Sequence analysis of a 33.1 kb fragment from the left arm of Saccharomyces
RT cerevisiae chromosome X, including putative proteins with leucine zippers,
RT a fungal Zn(II)2-Cys6 binuclear cluster domain and a putative alpha 2-SCB-
RT alpha 2 binding site.";
RL Yeast 11:681-689(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [5]
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 [6]
RP PROTEIN SEQUENCE OF 55-66; 202-210; 220-243; 269-296; 317-323; 378-430 AND
RP 448-482, IDENTIFICATION IN THE NUA4 COMPLEX, INTERACTION WITH HISTONES H2A;
RP H3 AND H4, MUTAGENESIS OF CYS-155 AND GLY-455, AND FUNCTION.
RX PubMed=10911987; DOI=10.1016/s1097-2765(00)80258-0;
RA Galarneau L., Nourani A., Boudreault A.A., Zhang Y., Heliot L., Allard S.,
RA Savard J., Lane W.S., Stillman D.J., Cote J.;
RT "Multiple links between the NuA4 histone acetyltransferase complex and
RT epigenetic control of transcription.";
RL Mol. Cell 5:927-937(2000).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=8573785; DOI=10.1091/mbc.6.10.1263;
RA Weber V., Harata M., Hauser H., Wintersberger U.;
RT "The actin-related protein Act3p of Saccharomyces cerevisiae is located in
RT the nucleus.";
RL Mol. Biol. Cell 6:1263-1270(1995).
RN [8]
RP IDENTIFICATION IN THE INO80 COMPLEX, FUNCTION OF THE INO80 COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10952318; DOI=10.1038/35020123;
RA Shen X., Mizuguchi G., Hamiche A., Wu C.;
RT "A chromatin remodelling complex involved in transcription and DNA
RT processing.";
RL Nature 406:541-544(2000).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF GLY-187 AND GLY-455.
RX PubMed=11937627; DOI=10.1093/nar/30.8.1743;
RA Harata M., Zhang Y., Stillman D.J., Matsui D., Oma Y., Nishimori K.,
RA Mochizuki R.;
RT "Correlation between chromatin association and transcriptional regulation
RT for the Act3p/Arp4 nuclear actin-related protein of Saccharomyces
RT cerevisiae.";
RL Nucleic Acids Res. 30:1743-1750(2002).
RN [10]
RP NOMENCLATURE.
RX PubMed=9290209;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1053::aid-yea164>3.0.co;2-4;
RA Poch O., Winsor B.;
RT "Who's who among the Saccharomyces cerevisiae actin-related proteins? A
RT classification and nomenclature proposal for a large family.";
RL Yeast 13:1053-1058(1997).
RN [11]
RP FUNCTION.
RX PubMed=12353039; DOI=10.1038/nature01035;
RA Bird A.W., Yu D.Y., Pray-Grant M.G., Qiu Q., Harmon K.E., Megee P.C.,
RA Grant P.A., Smith M.M., Christman M.F.;
RT "Acetylation of histone H4 by Esa1 is required for DNA double-strand break
RT repair.";
RL Nature 419:411-415(2002).
RN [12]
RP IDENTIFICATION IN THE INO80 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12887900; DOI=10.1016/s1097-2765(03)00264-8;
RA Shen X., Ranallo R., Choi E., Wu C.;
RT "Involvement of actin-related proteins in ATP-dependent chromatin
RT remodeling.";
RL Mol. Cell 12:147-155(2003).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [14]
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 [15]
RP FUNCTION, IDENTIFICATION IN THE SWR1 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=14690608; DOI=10.1016/s1097-2765(03)00497-0;
RA Krogan N.J., Keogh M.-C., Datta N., Sawa C., Ryan O.W., Ding H., Haw R.A.,
RA Pootoolal J., Tong A., Canadien V., Richards D.P., Wu X., Emili A.,
RA Hughes T.R., Buratowski S., Greenblatt J.F.;
RT "A Snf2 family ATPase complex required for recruitment of the histone H2A
RT variant Htz1.";
RL Mol. Cell 12:1565-1576(2003).
RN [16]
RP FUNCTION.
RX PubMed=15610740; DOI=10.1016/j.molcel.2004.12.003;
RA Downs J.A., Allard S., Jobin-Robitaille O., Javaheri A., Auger A.,
RA Bouchard N., Kron S.J., Jackson S.P., Cote J.;
RT "Binding of chromatin-modifying activities to phosphorylated histone H2A at
RT DNA damage sites.";
RL Mol. Cell 16:979-990(2004).
RN [17]
RP FUNCTION, AND MUTAGENESIS OF SER-23; ASP-159 AND GLY-161.
RX PubMed=14622406; DOI=10.1046/j.1365-2958.2003.03759.x;
RA Goerzer I., Schueller C., Heidenreich E., Krupanska L., Kuchler K.,
RA Wintersberger U.;
RT "The nuclear actin-related protein Act3p/Arp4p of Saccharomyces cerevisiae
RT is involved in transcription regulation of stress genes.";
RL Mol. Microbiol. 50:1155-1171(2003).
RN [18]
RP FUNCTION, IDENTIFICATION IN THE SWR1 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15045029; DOI=10.1371/journal.pbio.0020131;
RA Kobor M.S., Venkatasubrahmanyam S., Meneghini M.D., Gin J.W.,
RA Jennings J.L., Link A.J., Madhani H.D., Rine J.;
RT "A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p
RT deposits histone variant H2A.Z into euchromatin.";
RL PLoS Biol. 2:587-599(2004).
RN [19]
RP IDENTIFICATION IN THE SWR1 COMPLEX, FUNCTION OF THE SWR1 COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14645854; DOI=10.1126/science.1090701;
RA Mizuguchi G., Shen X., Landry J., Wu W.-H., Sen S., Wu C.;
RT "ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin
RT remodeling complex.";
RL Science 303:343-348(2004).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND IDENTIFICATION BY
RP 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 [22]
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).
CC -!- FUNCTION: Chromatin interaction component of the NuA4 histone
CC acetyltransferase complex which is involved in transcriptional
CC activation of selected genes principally by acetylation of nucleosomal
CC histone H4 and H2A. The NuA4 complex is also involved in DNA repair.
CC ARP4 recognizes H2AS128ph (gamma-H2A) and is required for NuA4 complex
CC integrity. Component of the SWR1 complex which mediates the ATP-
CC dependent exchange of histone H2A for the H2A variant HZT1 leading to
CC transcriptional regulation of selected genes by chromatin remodeling.
CC Component of the INO80 complex which remodels chromatin by shifting
CC nucleosomes. Its ability to induce transcription of some phosphate-
CC responsive genes is modulated by inositol polyphosphates. The INO80
CC complex is involved in DNA repair by associating to gamma-H2A as a
CC response to DNA damage. {ECO:0000269|PubMed:10911987,
CC ECO:0000269|PubMed:10952318, ECO:0000269|PubMed:11937627,
CC ECO:0000269|PubMed:12353039, ECO:0000269|PubMed:14622406,
CC ECO:0000269|PubMed:14645854, ECO:0000269|PubMed:14690608,
CC ECO:0000269|PubMed:15045029, ECO:0000269|PubMed:15610740}.
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex
CC composed of at least ACT1, ARP4, EAF3, EAF5, EAF6, EAF7, EPL1, ESA1,
CC SWC4, TRA1, VID21, YAF9 and YNG2. Component of the chromatin-remodeling
CC INO80 complex, at least composed of ARP4, ARP5, ARP8, RVB1, RVB2,
CC TAF14, NHP10, IES1, IES3, IES4, IES6, ACT1, IES2, IES5 and INO80.
CC Component of the SWR1 chromatin remodeling complex composed of at least
CC ACT1, ARP4, RVB1, RVB2, ARP6, YAF9, VPS71, VPS72, SWC3, SWC4, SWC5,
CC SWC7 and SWR1, and perhaps BDF1. Interacts with histones H4 (HHF1 and
CC HHF2), H3 (HHT1 and HHT2) and H2A (HTA1 and HTA2).
CC {ECO:0000269|PubMed:10911987, ECO:0000269|PubMed:10952318,
CC ECO:0000269|PubMed:12887900, ECO:0000269|PubMed:14645854,
CC ECO:0000269|PubMed:14690608, ECO:0000269|PubMed:15045029}.
CC -!- INTERACTION:
CC P80428; Q08649: ESA1; NbExp=9; IntAct=EBI-2939, EBI-6648;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8573785}.
CC -!- MISCELLANEOUS: Present with 1070 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the actin family. ARP4 subfamily. {ECO:0000305}.
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DR EMBL; X75317; CAA53066.1; -; Genomic_DNA.
DR EMBL; X83502; CAA58489.1; -; Genomic_DNA.
DR EMBL; Z49356; CAA89374.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08718.1; -; Genomic_DNA.
DR PIR; S47608; S47608.
DR RefSeq; NP_012454.1; NM_001181514.1.
DR PDB; 3QB0; X-ray; 3.40 A; A/B/C/D=1-489.
DR PDB; 5I9E; X-ray; 2.80 A; A/C=1-489.
DR PDB; 5NBL; X-ray; 2.80 A; A/B=1-489.
DR PDB; 5NBM; X-ray; 3.40 A; A/B=1-489.
DR PDB; 5NBN; X-ray; 4.00 A; A/B=1-489.
DR PDB; 5Y81; EM; 4.70 A; F=1-489.
DR PDBsum; 3QB0; -.
DR PDBsum; 5I9E; -.
DR PDBsum; 5NBL; -.
DR PDBsum; 5NBM; -.
DR PDBsum; 5NBN; -.
DR PDBsum; 5Y81; -.
DR AlphaFoldDB; P80428; -.
DR SMR; P80428; -.
DR BioGRID; 33675; 679.
DR ComplexPortal; CPX-2122; Swr1 chromatin remodelling complex.
DR ComplexPortal; CPX-3155; NuA4 histone acetyltransferase complex.
DR ComplexPortal; CPX-863; INO80 chromatin remodeling complex.
DR DIP; DIP-2361N; -.
DR IntAct; P80428; 57.
DR MINT; P80428; -.
DR STRING; 4932.YJL081C; -.
DR iPTMnet; P80428; -.
DR MaxQB; P80428; -.
DR PaxDb; P80428; -.
DR PRIDE; P80428; -.
DR EnsemblFungi; YJL081C_mRNA; YJL081C; YJL081C.
DR GeneID; 853364; -.
DR KEGG; sce:YJL081C; -.
DR SGD; S000003617; ARP4.
DR VEuPathDB; FungiDB:YJL081C; -.
DR eggNOG; KOG0679; Eukaryota.
DR GeneTree; ENSGT00940000172256; -.
DR HOGENOM; CLU_027965_6_2_1; -.
DR InParanoid; P80428; -.
DR OMA; GIVEKRC; -.
DR BioCyc; YEAST:G3O-31538-MON; -.
DR Reactome; R-SCE-3214858; RMTs methylate histone arginines.
DR PRO; PR:P80428; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P80428; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0031011; C:Ino80 complex; IPI:SGD.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0016514; C:SWI/SNF complex; IBA:GO_Central.
DR GO; GO:0000812; C:Swr1 complex; IDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0042393; F:histone binding; IDA:SGD.
DR GO; GO:0006325; P:chromatin organization; IMP:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IDA:SGD.
DR GO; GO:0006281; P:DNA repair; IDA:SGD.
DR GO; GO:0016573; P:histone acetylation; IDA:SGD.
DR GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
DR GO; GO:0051382; P:kinetochore assembly; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:SGD.
DR GO; GO:0006351; P:transcription, DNA-templated; IC:ComplexPortal.
DR DisProt; DP00872; -.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Chromatin regulator; Direct protein sequencing;
KW DNA damage; DNA repair; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation.
FT CHAIN 1..489
FT /note="Actin-related protein 4"
FT /id="PRO_0000089103"
FT REGION 323..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 23
FT /note="S->A: Lethal; when associated with D-161.
FT Formamide-, hydroxyurea and UV-hypersensitivity, suppressor
FT of TY phenotype; when associated with A-159."
FT /evidence="ECO:0000269|PubMed:14622406"
FT MUTAGEN 155
FT /note="C->Y: No histone acetyltransferase activity at 37
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:10911987"
FT MUTAGEN 159
FT /note="D->A: Formamide-, hydroxyurea and UV-
FT hypersensitivity, suppressor of TY phenotype; when
FT associated with S-23."
FT /evidence="ECO:0000269|PubMed:14622406"
FT MUTAGEN 161
FT /note="G->D: Formamide-, hydroxyurea and UV-
FT hypersensitivity, destabilization of ARP4, suppressor of TY
FT phenotype and elevated levels of MSN2/MSN4-regulated genes.
FT Lethal; when associated with A-23."
FT /evidence="ECO:0000269|PubMed:14622406"
FT MUTAGEN 187
FT /note="G->R: Defect in promoter association and change in
FT chromatin structure."
FT /evidence="ECO:0000269|PubMed:11937627"
FT MUTAGEN 455
FT /note="G->S: No histone acetyltransferase activity at 37
FT degrees Celsius. Defect in promoter association and change
FT in chromatin structure."
FT /evidence="ECO:0000269|PubMed:10911987,
FT ECO:0000269|PubMed:11937627"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:5I9E"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:5I9E"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:5I9E"
FT STRAND 37..47
FT /evidence="ECO:0007829|PDB:5I9E"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:5I9E"
FT STRAND 67..76
FT /evidence="ECO:0007829|PDB:5I9E"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:5I9E"
FT HELIX 83..96
FT /evidence="ECO:0007829|PDB:5I9E"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:5I9E"
FT HELIX 118..129
FT /evidence="ECO:0007829|PDB:5I9E"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:5I9E"
FT HELIX 142..149
FT /evidence="ECO:0007829|PDB:5I9E"
FT STRAND 153..160
FT /evidence="ECO:0007829|PDB:5I9E"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:5I9E"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:5NBL"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:5I9E"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:5I9E"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:3QB0"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:5NBL"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:5I9E"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:5I9E"
FT HELIX 227..235
FT /evidence="ECO:0007829|PDB:5I9E"
FT HELIX 238..245
FT /evidence="ECO:0007829|PDB:5I9E"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:5NBL"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:5I9E"
FT HELIX 258..261
FT /evidence="ECO:0007829|PDB:5I9E"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:5NBL"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:5NBL"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:3QB0"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:5NBL"
FT HELIX 282..290
FT /evidence="ECO:0007829|PDB:5I9E"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:5I9E"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:5I9E"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:5NBM"
FT HELIX 385..395
FT /evidence="ECO:0007829|PDB:5I9E"
FT HELIX 398..406
FT /evidence="ECO:0007829|PDB:5I9E"
FT STRAND 408..412
FT /evidence="ECO:0007829|PDB:5I9E"
FT HELIX 413..416
FT /evidence="ECO:0007829|PDB:5I9E"
FT HELIX 420..431
FT /evidence="ECO:0007829|PDB:5I9E"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:5NBM"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:5I9E"
FT HELIX 451..459
FT /evidence="ECO:0007829|PDB:5I9E"
FT HELIX 463..468
FT /evidence="ECO:0007829|PDB:5I9E"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:3QB0"
FT HELIX 472..478
FT /evidence="ECO:0007829|PDB:5I9E"
FT TURN 479..485
FT /evidence="ECO:0007829|PDB:5I9E"
SQ SEQUENCE 489 AA; 54832 MW; 6DE1C8938C6C3DBB CRC64;
MSNAALQVYG GDEVSAVVID PGSYTTNIGY SGSDFPQSIL PSVYGKYTAD EGNKKIFSEQ
SIGIPRKDYE LKPIIENGLV IDWDTAQEQW QWALQNELYL NSNSGIPALL TEPVWNSTEN
RKKSLEVLLE GMQFEACYLA PTSTCVSFAA GRPNCLVVDI GHDTCSVSPI VDGMTLSKST
RRNFIAGKFI NHLIKKALEP KEIIPLFAIK QRKPEFIKKT FDYEVDKSLY DYANNRGFFQ
ECKETLCHIC PTKTLEETKT ELSSTAKRSI ESPWNEEIVF DNETRYGFAE ELFLPKEDDI
PANWPRSNSG VVKTWRNDYV PLKRTKPSGV NKSDKKVTPT EEKEQEAVSK STSPAANSAD
TPNETGKRPL EEEKPPKENN ELIGLADLVY SSIMSSDVDL RATLAHNVVL TGGTSSIPGL
SDRLMTELNK ILPSLKFRIL TTGHTIERQY QSWLGGSILT SLGTFHQLWV GKKEYEEVGV
ERLLNDRFR
