VPS75_YEAST
ID VPS75_YEAST Reviewed; 264 AA.
AC P53853; D6W0U7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Vacuolar protein sorting-associated protein 75;
GN Name=VPS75; OrderedLocusNames=YNL246W; ORFNames=N0890;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9234673;
RX DOI=10.1002/(sici)1097-0061(199707)13:9<849::aid-yea106>3.0.co;2-n;
RA Sen-Gupta M., Gueldener U., Beinhauer J.D., Fiedler T.A., Hegemann J.H.;
RT "Sequence analysis of the 33 kb long region between ORC5 and SUI1 from the
RT left arm of chromosome XIV from Saccharomyces cerevisiae.";
RL Yeast 13:849-860(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(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 DISRUPTION PHENOTYPE.
RX PubMed=12134085; DOI=10.1091/mbc.02-01-0005;
RA Bonangelino C.J., Chavez E.M., Bonifacino J.S.;
RT "Genomic screen for vacuolar protein sorting genes in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 13:2486-2501(2002).
RN [5]
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 [6]
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 [7]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH RTT109, AND INTERACTION WITH
RP RTT109.
RX PubMed=17320445; DOI=10.1016/j.molcel.2007.02.006;
RA Tsubota T., Berndsen C.E., Erkmann J.A., Smith C.L., Yang L., Freitas M.A.,
RA Denu J.M., Kaufman P.D.;
RT "Histone H3-K56 acetylation is catalyzed by histone chaperone-dependent
RT complexes.";
RL Mol. Cell 25:703-712(2007).
RN [8]
RP INTERACTION WITH RTT109.
RX PubMed=17272723; DOI=10.1126/science.1133234;
RA Han J., Zhou H., Horazdovsky B., Zhang K., Xu R.-M., Zhang Z.;
RT "Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication.";
RL Science 315:653-655(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND IDENTIFICATION BY MASS
RP 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 [10]
RP IDENTIFICATION IN A COMPLEX WITH RTT109, AND INTERACTION WITH RTT109.
RX PubMed=18719104; DOI=10.1073/pnas.0805813105;
RA Stavropoulos P., Nagy V., Blobel G., Hoelz A.;
RT "Molecular basis for the autoregulation of the protein acetyl transferase
RT Rtt109.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12236-12241(2008).
RN [11]
RP IDENTIFICATION IN A COMPLEX WITH RTT109, AND INTERACTION WITH RTT109.
RX PubMed=20560668; DOI=10.1021/bi100381y;
RA Albaugh B.N., Kolonko E.M., Denu J.M.;
RT "Kinetic mechanism of the Rtt109-Vps75 histone acetyltransferase-chaperone
RT complex.";
RL Biochemistry 49:6375-6385(2010).
RN [12]
RP FUNCTION.
RX PubMed=29300933; DOI=10.1093/nar/gkx1283;
RA Lercher L., Danilenko N., Kirkpatrick J., Carlomagno T.;
RT "Structural characterization of the Asf1-Rtt109 interaction and its role in
RT histone acetylation.";
RL Nucleic Acids Res. 46:2279-2289(2018).
RN [13] {ECO:0007744|PDB:3C9B, ECO:0007744|PDB:3C9D}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-259, FUNCTION, SUBUNIT,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 21-CYS--VAL-32 AND
RP 205-SER--GLU-207.
RX PubMed=19172748; DOI=10.1038/nsmb.1459;
RA Berndsen C.E., Tsubota T., Lindner S.E., Lee S., Holton J.M., Kaufman P.D.,
RA Keck J.L., Denu J.M.;
RT "Molecular functions of the histone acetyltransferase chaperone complex
RT Rtt109-Vps75.";
RL Nat. Struct. Mol. Biol. 15:948-956(2008).
RN [14] {ECO:0007744|PDB:3Q66, ECO:0007744|PDB:3Q68}
RP X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 2-231 AND 9-225 IN COMPLEX WITH
RP RTT109, SUBUNIT, AND INTERACTION WITH RTT109 AND HISTONE H3/H4
RP HETERODIMERS.
RX PubMed=21454705; DOI=10.1074/jbc.c111.220715;
RA Su D., Hu Q., Zhou H., Thompson J.R., Xu R.M., Zhang Z., Mer G.;
RT "Structure and histone binding properties of the Vps75-Rtt109 chaperone-
RT lysine acetyltransferase complex.";
RL J. Biol. Chem. 286:15625-15629(2011).
RN [15] {ECO:0007744|PDB:3Q33, ECO:0007744|PDB:3Q35}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 9-130 AND 136-226 IN COMPLEX WITH
RP RTT109, FUNCTION, SUBUNIT, INTERACTION WITH RTT109, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF ALA-19; 21-CYS--VAL-32; 73-ARG-ALA-74; 167-GLU--THR-178;
RP 173-ARG--LYS-177; 206-GLU-GLU-207; 218-GLU--ASP-222 AND 233-SER--VAL-264.
RX PubMed=21256037; DOI=10.1016/j.str.2010.12.012;
RA Tang Y., Holbert M.A., Delgoshaie N., Wurtele H., Guillemette B., Meeth K.,
RA Yuan H., Drogaris P., Lee E.H., Durette C., Thibault P., Verreault A.,
RA Cole P.A., Marmorstein R.;
RT "Structure of the Rtt109-AcCoA/Vps75 complex and implications for
RT chaperone-mediated histone acetylation.";
RL Structure 19:221-231(2011).
RN [16] {ECO:0007744|PDB:5AGC}
RP X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS), SUBUNIT, AND INTERACTION WITH
RP HISTONE H3/H4 HETERODIMERS AND HETEROTETRAMERS.
RX PubMed=27036862; DOI=10.1093/nar/gkw209;
RA Hammond C.M., Sundaramoorthy R., Larance M., Lamond A., Stevens M.A.,
RA El-Mkami H., Norman D.G., Owen-Hughes T.;
RT "The histone chaperone Vps75 forms multiple oligomeric assemblies capable
RT of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4
RT complexes.";
RL Nucleic Acids Res. 44:6157-6172(2016).
RN [17] {ECO:0007744|PDB:6O22}
RP STRUCTURE BY NMR IN COMPLEX WITH RTT109 AND ASF1, FUNCTION, SUBUNIT,
RP INTERACTION WITH RTT109; ASF1 AND HISTONE H3/H4 HETERODIMERS, DOMAIN, AND
RP MUTAGENESIS OF 206-GLU-GLU-207.
RX PubMed=31387991; DOI=10.1038/s41467-019-11410-7;
RA Danilenko N., Lercher L., Kirkpatrick J., Gabel F., Codutti L.,
RA Carlomagno T.;
RT "Histone chaperone exploits intrinsic disorder to switch acetylation
RT specificity.";
RL Nat. Commun. 10:3435-3435(2019).
CC -!- FUNCTION: Histone chaperone which acts as a cofactor stimulating
CC histone H3 acetylation by RTT109 (PubMed:21256037, PubMed:17320445,
CC PubMed:31387991, PubMed:29300933, PubMed:19172748). Preferentially
CC stimulates histone H3 'Lys-9' acetylation by RTT109 (PubMed:21256037,
CC PubMed:31387991, PubMed:29300933). May also stimulate histone H3 'Lys-
CC 56' acetylation by RTT109 (PubMed:17320445). Assembles nucleosomes (in
CC vitro) (PubMed:19172748). {ECO:0000269|PubMed:17320445,
CC ECO:0000269|PubMed:19172748, ECO:0000269|PubMed:21256037,
CC ECO:0000269|PubMed:29300933, ECO:0000269|PubMed:31387991}.
CC -!- SUBUNIT: Homodimer (PubMed:31387991, PubMed:21256037, PubMed:21454705,
CC PubMed:19172748). Homotetramer (PubMed:27036862). Forms a complex with
CC RTT109; consisting of a VPS75 dimer contacted by two RTT109 subunits
CC (PubMed:21256037, PubMed:20560668, PubMed:17320445, PubMed:31387991,
CC PubMed:18719104, PubMed:21454705). Interacts with RTT109; the
CC interaction is direct (PubMed:20560668, PubMed:17272723,
CC PubMed:17320445, PubMed:31387991, PubMed:18719104, PubMed:21256037).
CC Interacts with ASF1 (PubMed:31387991). Interacts with histone H3/H4
CC heterodimers and heterotetramers via histone H3 (PubMed:31387991,
CC PubMed:21454705, PubMed:27036862). {ECO:0000269|PubMed:17272723,
CC ECO:0000269|PubMed:17320445, ECO:0000269|PubMed:18719104,
CC ECO:0000269|PubMed:19172748, ECO:0000269|PubMed:20560668,
CC ECO:0000269|PubMed:21256037, ECO:0000269|PubMed:21454705,
CC ECO:0000269|PubMed:27036862, ECO:0000269|PubMed:31387991}.
CC -!- INTERACTION:
CC P53853; Q07794: RTT109; NbExp=20; IntAct=EBI-29225, EBI-2887026;
CC P53853; P53853: VPS75; NbExp=9; IntAct=EBI-29225, EBI-29225;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The C-terminal part interacts with the N-terminal part of
CC histone H3 and promotes acetylation of histone H3 'Lys-9'.
CC {ECO:0000269|PubMed:31387991}.
CC -!- DISRUPTION PHENOTYPE: Decreases acetylation of histone H3 'Lys-9' and
CC 'Lys-23' (PubMed:19172748). Simultaneous disruption of GCN5 abolishes
CC acetylation of histone H3 'Lys-9' and 'Lys-27' (PubMed:21256037).
CC Abnormal protein sorting to vacuole (PubMed:12134085).
CC {ECO:0000269|PubMed:12134085, ECO:0000269|PubMed:19172748,
CC ECO:0000269|PubMed:21256037}.
CC -!- MISCELLANEOUS: Present with 3120 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family.
CC {ECO:0000305}.
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DR EMBL; Z71522; CAA96152.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10313.1; -; Genomic_DNA.
DR PIR; S63214; S63214.
DR RefSeq; NP_014153.1; NM_001183084.1.
DR PDB; 2ZD7; X-ray; 1.85 A; A/B=1-264.
DR PDB; 3C9B; X-ray; 2.42 A; A/B=1-259.
DR PDB; 3C9D; X-ray; 2.00 A; A/B=1-259.
DR PDB; 3DM7; X-ray; 2.00 A; A/B=1-232.
DR PDB; 3Q33; X-ray; 2.80 A; B=1-232.
DR PDB; 3Q35; X-ray; 3.30 A; B=1-232.
DR PDB; 3Q66; X-ray; 2.70 A; A/B=1-264.
DR PDB; 3Q68; X-ray; 2.70 A; A/B=1-264.
DR PDB; 5AGC; X-ray; 4.00 A; A/B/C/D=1-264.
DR PDB; 6O22; Other; -; A/B=1-264.
DR PDBsum; 2ZD7; -.
DR PDBsum; 3C9B; -.
DR PDBsum; 3C9D; -.
DR PDBsum; 3DM7; -.
DR PDBsum; 3Q33; -.
DR PDBsum; 3Q35; -.
DR PDBsum; 3Q66; -.
DR PDBsum; 3Q68; -.
DR PDBsum; 5AGC; -.
DR PDBsum; 6O22; -.
DR AlphaFoldDB; P53853; -.
DR SASBDB; P53853; -.
DR SMR; P53853; -.
DR BioGRID; 35593; 112.
DR ComplexPortal; CPX-1333; RTT109-VPS75 histone acetyltransferase complex.
DR DIP; DIP-3896N; -.
DR IntAct; P53853; 4.
DR MINT; P53853; -.
DR STRING; 4932.YNL246W; -.
DR iPTMnet; P53853; -.
DR MaxQB; P53853; -.
DR PaxDb; P53853; -.
DR PRIDE; P53853; -.
DR EnsemblFungi; YNL246W_mRNA; YNL246W; YNL246W.
DR GeneID; 855475; -.
DR KEGG; sce:YNL246W; -.
DR SGD; S000005190; VPS75.
DR VEuPathDB; FungiDB:YNL246W; -.
DR eggNOG; KOG1508; Eukaryota.
DR GeneTree; ENSGT00940000169229; -.
DR HOGENOM; CLU_072852_0_0_1; -.
DR InParanoid; P53853; -.
DR OMA; LRFTFEF; -.
DR BioCyc; YEAST:G3O-33243-MON; -.
DR EvolutionaryTrace; P53853; -.
DR PRO; PR:P53853; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53853; protein.
DR GO; GO:0000785; C:chromatin; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0070775; C:H3 histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0010698; F:acetyltransferase activator activity; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:SGD.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
DR GO; GO:0043972; P:histone H3-K23 acetylation; IMP:UniProtKB.
DR GO; GO:0097043; P:histone H3-K56 acetylation; IDA:UniProtKB.
DR GO; GO:0043970; P:histone H3-K9 acetylation; IDA:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IDA:SGD.
DR GO; GO:2000617; P:positive regulation of histone H3-K9 acetylation; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR DisProt; DP02908; -.
DR IDEAL; IID50212; -.
DR InterPro; IPR037231; NAP-like_sf.
DR InterPro; IPR002164; NAP_family.
DR PANTHER; PTHR11875; PTHR11875; 1.
DR Pfam; PF00956; NAP; 1.
DR SUPFAM; SSF143113; SSF143113; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..264
FT /note="Vacuolar protein sorting-associated protein 75"
FT /id="PRO_0000185675"
FT REGION 223..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..249
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 19
FT /note="A->D: Decreases RTT109 binding."
FT /evidence="ECO:0000269|PubMed:21256037"
FT MUTAGEN 19
FT /note="A->I: Mildly decreases RTT109 activity stimulation."
FT /evidence="ECO:0000269|PubMed:21256037"
FT MUTAGEN 21..32
FT /note="CEEEVDAIEREV->EEEESDAEEREE: Abolishes dimer
FT formation. Decreases activity and binding to RTT109."
FT /evidence="ECO:0000269|PubMed:19172748,
FT ECO:0000269|PubMed:21256037"
FT MUTAGEN 73..74
FT /note="RA->DD: Decreases RTT109 binding and activity
FT stimulation."
FT /evidence="ECO:0000269|PubMed:21256037"
FT MUTAGEN 167..178
FT /note="Missing: Decreases RTT109 activity stimulation."
FT /evidence="ECO:0000269|PubMed:21256037"
FT MUTAGEN 173..177
FT /note="RQGMK->EQGME: Decreases RTT109 binding and activity
FT stimulation."
FT /evidence="ECO:0000269|PubMed:21256037"
FT MUTAGEN 205..207
FT /note="SEE->AAA: Decreases RTT109 activity stimulation."
FT /evidence="ECO:0000269|PubMed:19172748"
FT MUTAGEN 206..207
FT /note="EE->AA: Increases acetylation of histone H3 'Lys-
FT 56'."
FT /evidence="ECO:0000269|PubMed:31387991"
FT MUTAGEN 206..207
FT /note="EE->KK: Decreases RTT109 activity stimulation."
FT /evidence="ECO:0000269|PubMed:21256037"
FT MUTAGEN 218..222
FT /note="EAQRD->KAQRK: Decreases RTT109 binding and activity
FT stimulation."
FT /evidence="ECO:0000269|PubMed:21256037"
FT MUTAGEN 233..264
FT /note="Missing: Decreases RTT109 activity stimulation."
FT /evidence="ECO:0000269|PubMed:21256037"
FT HELIX 7..51
FT /evidence="ECO:0007829|PDB:2ZD7"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:2ZD7"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:3DM7"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:2ZD7"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:2ZD7"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:2ZD7"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:2ZD7"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:2ZD7"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:2ZD7"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:2ZD7"
FT STRAND 119..128
FT /evidence="ECO:0007829|PDB:2ZD7"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:2ZD7"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:2ZD7"
FT HELIX 150..155
FT /evidence="ECO:0007829|PDB:2ZD7"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:2ZD7"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:2ZD7"
FT HELIX 166..176
FT /evidence="ECO:0007829|PDB:2ZD7"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:2ZD7"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:2ZD7"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:2ZD7"
FT HELIX 197..206
FT /evidence="ECO:0007829|PDB:2ZD7"
FT HELIX 208..221
FT /evidence="ECO:0007829|PDB:2ZD7"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:3Q66"
FT TURN 227..230
FT /evidence="ECO:0007829|PDB:3Q68"
SQ SEQUENCE 264 AA; 30615 MW; 779F12CEA27B3E6B CRC64;
MMSDQENENE HAKAFLGLAK CEEEVDAIER EVELYRLNKM KPVYEKRDAY IDEIAEFWKI
VLSQHVSFAN YIRASDFKYI DTIDKIKVEW LALESEMYDT RDFSITFHFH GIEGDFKEQQ
VTKVFQIKKG KDDQEDGILT SEPVPIEWPQ SYDSINPDLI KDKRSPEGKK KYRQGMKTIF
GWFRWTGLKP GKEFPHGDSL ASLFSEEIYP FCVKYYAEAQ RDLEDEEGES GLSADGDSED
DDGSLGEVDL PLSDEEPSSK KRKV
