IF6_YEAST
ID IF6_YEAST Reviewed; 245 AA.
AC Q12522; D6W426;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Eukaryotic translation initiation factor 6 {ECO:0000255|HAMAP-Rule:MF_03132};
DE Short=eIF-6 {ECO:0000255|HAMAP-Rule:MF_03132};
GN Name=TIF6 {ECO:0000255|HAMAP-Rule:MF_03132}; Synonyms=CDC95;
GN OrderedLocusNames=YPR016C; ORFNames=LPZ15C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
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 [3]
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 [4]
RP CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=10206977; DOI=10.1074/jbc.274.17.11653;
RA Wood L.C., Ashby M.N., Grunfeld C., Feingold K.R.;
RT "Cloning of murine translation initiation factor 6 and functional analysis
RT of the homologous sequence YPR016c in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 274:11653-11659(1999).
RN [5]
RP FUNCTION.
RX PubMed=10085284; DOI=10.1083/jcb.144.5.823;
RA Sanvito F., Piatti S., Villa A., Bossi M., Lucchini G., Marchisio P.C.,
RA Biffo S.;
RT "The beta4 integrin interactor p27(BBP/eIF6) is an essential nuclear matrix
RT protein involved in 60S ribosomal subunit assembly.";
RL J. Cell Biol. 144:823-837(1999).
RN [6]
RP CHARACTERIZATION.
RX PubMed=9891075; DOI=10.1128/mcb.19.2.1416;
RA Si K., Maitra U.;
RT "The Saccharomyces cerevisiae homologue of mammalian translation initiation
RT factor 6 does not function as a translation initiation factor.";
RL Mol. Cell. Biol. 19:1416-1426(1999).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11779510; DOI=10.1016/s1097-2765(01)00403-8;
RA Senger B., Lafontaine D.L.J., Graindorge J.-S., Gadal O., Camasses A.,
RA Sanni A., Garnier J.-M., Breitenbach M., Hurt E., Fasiolo F.;
RT "The nucle(ol)ar Tif6p and Efl1p are required for a late cytoplasmic step
RT of ribosome synthesis.";
RL Mol. Cell 8:1363-1373(2001).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11238882; DOI=10.1128/mcb.21.5.1453-1462.2001;
RA Basu U., Si K., Warner J.R., Maitra U.;
RT "The Saccharomyces cerevisiae TIF6 gene encoding translation initiation
RT factor 6 is required for 60S ribosomal subunit biogenesis.";
RL Mol. Cell. Biol. 21:1453-1462(2001).
RN [9]
RP PHOSPHORYLATION, AND NUCLEOCYTOPLASMIC SHUTTLING.
RX PubMed=12917340; DOI=10.1128/mcb.23.17.6187-6199.2003;
RA Basu U., Si K., Deng H., Maitra U.;
RT "Phosphorylation of mammalian eukaryotic translation initiation factor 6
RT and its Saccharomyces cerevisiae homologue Tif6p: evidence that
RT phosphorylation of Tif6p regulates its nucleocytoplasmic distribution and
RT is required for yeast cell growth.";
RL Mol. Cell. Biol. 23:6187-6199(2003).
RN [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND IDENTIFICATION BY
RP 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 [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17353896; DOI=10.1038/ng1994;
RA Menne T.F., Goyenechea B., Sanchez-Puig N., Wong C.C., Tonkin L.M.,
RA Ancliff P.J., Brost R.L., Costanzo M., Boone C., Warren A.J.;
RT "The Shwachman-Bodian-Diamond syndrome protein mediates translational
RT activation of ribosomes in yeast.";
RL Nat. Genet. 39:486-495(2007).
RN [13]
RP FUNCTION, AND PHOSPHORYLATION AT SER-174.
RX PubMed=18256024; DOI=10.1074/jbc.m710294200;
RA Ray P., Basu U., Ray A., Majumdar R., Deng H., Maitra U.;
RT "The Saccharomyces cerevisiae 60 S ribosome biogenesis factor Tif6p is
RT regulated by Hrr25p-mediated phosphorylation.";
RL J. Biol. Chem. 283:9681-9691(2008).
RN [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND IDENTIFICATION BY
RP 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 [16]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS), AND FUNCTION.
RX PubMed=11101899; DOI=10.1038/82017;
RA Groft C.M., Beckmann R., Sali A., Burley S.K.;
RT "Crystal structures of ribosome anti-association factor IF6.";
RL Nat. Struct. Biol. 7:1156-1164(2000).
RN [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (11.8 ANGSTROMS) OF 1-224.
RX PubMed=20356839; DOI=10.1074/jbc.c109.096057;
RA Gartmann M., Blau M., Armache J.P., Mielke T., Topf M., Beckmann R.;
RT "Mechanism of eIF6-mediated inhibition of ribosomal subunit joining.";
RL J. Biol. Chem. 285:14848-14851(2010).
CC -!- FUNCTION: Binds to the 60S ribosomal subunit and prevents its
CC association with the 40S ribosomal subunit to form the 80S initiation
CC complex in the cytoplasm. Is also involved in ribosome biogenesis.
CC Associates with pre-60S subunits in the nucleus and is involved in its
CC nuclear export. Cytoplasmic release of TIF6 from 60S subunits and
CC nuclear relocalization is promoted by the GTPase RIA1/EFL1 and by SDO1.
CC Also required for pre-rRNA processing. {ECO:0000255|HAMAP-
CC Rule:MF_03132, ECO:0000269|PubMed:10085284,
CC ECO:0000269|PubMed:11101899, ECO:0000269|PubMed:11238882,
CC ECO:0000269|PubMed:11779510, ECO:0000269|PubMed:17353896,
CC ECO:0000269|PubMed:18256024}.
CC -!- SUBUNIT: Monomer. Associates with the 60S ribosomal subunit.
CC -!- INTERACTION:
CC Q12522; P53145: LSG1; NbExp=5; IntAct=EBI-9046, EBI-23885;
CC Q12522; P53742: NOG2; NbExp=4; IntAct=EBI-9046, EBI-28532;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Note=Shuttles
CC between cytoplasm and nucleus/nucleolus.
CC -!- PTM: Phosphorylation at Ser-174 and Ser-175 promotes nuclear export.
CC {ECO:0000255|HAMAP-Rule:MF_03132, ECO:0000269|PubMed:12917340,
CC ECO:0000269|PubMed:18256024}.
CC -!- MISCELLANEOUS: Present with 18600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eIF-6 family. {ECO:0000255|HAMAP-
CC Rule:MF_03132}.
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DR EMBL; Z71255; CAA95012.1; -; Genomic_DNA.
DR EMBL; Z49919; CAA90161.1; -; Genomic_DNA.
DR EMBL; U31900; AAA97594.1; -; Genomic_DNA.
DR EMBL; AY692916; AAT92935.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11442.1; -; Genomic_DNA.
DR PIR; S57550; S57550.
DR RefSeq; NP_015341.1; NM_001184113.1.
DR PDB; 1G62; X-ray; 2.50 A; A=1-224.
DR PDB; 2X7N; EM; 11.80 A; B=1-224.
DR PDB; 3J2I; EM; 11.90 A; B=1-245.
DR PDB; 3JCT; EM; 3.08 A; y=1-245.
DR PDB; 4V7F; EM; 8.70 A; m=1-245.
DR PDB; 5FL8; EM; 9.50 A; m=1-245.
DR PDB; 5H4P; EM; 3.07 A; y=1-227.
DR PDB; 5JCS; EM; 9.50 A; m=1-245.
DR PDB; 5T62; EM; 3.30 A; X=1-245.
DR PDB; 5Z3G; EM; 3.65 A; N=1-245.
DR PDB; 6C0F; EM; 3.70 A; y=1-245.
DR PDB; 6ELZ; EM; 3.30 A; y=1-245.
DR PDB; 6EM1; EM; 3.60 A; y=1-245.
DR PDB; 6EM4; EM; 4.10 A; y=1-245.
DR PDB; 6EM5; EM; 4.30 A; y=1-245.
DR PDB; 6FT6; EM; 3.90 A; y=1-245.
DR PDB; 6M62; EM; 3.20 A; y=1-245.
DR PDB; 6N8J; EM; 3.50 A; y=1-245.
DR PDB; 6N8K; EM; 3.60 A; y=1-245.
DR PDB; 6N8L; EM; 3.60 A; y=1-245.
DR PDB; 6N8M; EM; 3.50 A; X=1-245.
DR PDB; 6N8N; EM; 3.80 A; X=1-245.
DR PDB; 6N8O; EM; 3.50 A; X=1-245.
DR PDB; 6QIK; EM; 3.10 A; n=1-245.
DR PDB; 6QT0; EM; 3.40 A; n=1-245.
DR PDB; 6QTZ; EM; 3.50 A; n=1-245.
DR PDB; 6R84; EM; 3.60 A; X=1-224.
DR PDB; 6R86; EM; 3.40 A; X=1-224.
DR PDB; 6R87; EM; 3.40 A; X=1-224.
DR PDB; 6RI5; EM; 3.30 A; n=1-245.
DR PDB; 6RZZ; EM; 3.20 A; n=1-245.
DR PDB; 6S05; EM; 3.90 A; n=1-245.
DR PDB; 6YLG; EM; 3.00 A; y=1-245.
DR PDB; 6YLH; EM; 3.10 A; y=1-245.
DR PDB; 6YLX; EM; 3.90 A; y=1-245.
DR PDB; 6YLY; EM; 3.80 A; y=1-245.
DR PDB; 7BT6; EM; 3.12 A; y=1-245.
DR PDB; 7BTB; EM; 3.22 A; y=1-245.
DR PDB; 7OF1; EM; 3.10 A; y=1-245.
DR PDB; 7OH3; EM; 3.40 A; y=1-245.
DR PDB; 7OHP; EM; 3.90 A; y=1-245.
DR PDB; 7OHQ; EM; 3.10 A; y=1-245.
DR PDB; 7OHR; EM; 4.72 A; y=1-245.
DR PDB; 7OHS; EM; 4.38 A; y=1-245.
DR PDB; 7OHT; EM; 4.70 A; y=1-245.
DR PDB; 7OHU; EM; 3.70 A; y=1-245.
DR PDB; 7OHV; EM; 3.90 A; y=1-245.
DR PDB; 7OHW; EM; 3.50 A; y=1-245.
DR PDB; 7OHX; EM; 3.30 A; y=1-245.
DR PDB; 7OHY; EM; 3.90 A; y=1-245.
DR PDBsum; 1G62; -.
DR PDBsum; 2X7N; -.
DR PDBsum; 3J2I; -.
DR PDBsum; 3JCT; -.
DR PDBsum; 4V7F; -.
DR PDBsum; 5FL8; -.
DR PDBsum; 5H4P; -.
DR PDBsum; 5JCS; -.
DR PDBsum; 5T62; -.
DR PDBsum; 5Z3G; -.
DR PDBsum; 6C0F; -.
DR PDBsum; 6ELZ; -.
DR PDBsum; 6EM1; -.
DR PDBsum; 6EM4; -.
DR PDBsum; 6EM5; -.
DR PDBsum; 6FT6; -.
DR PDBsum; 6M62; -.
DR PDBsum; 6N8J; -.
DR PDBsum; 6N8K; -.
DR PDBsum; 6N8L; -.
DR PDBsum; 6N8M; -.
DR PDBsum; 6N8N; -.
DR PDBsum; 6N8O; -.
DR PDBsum; 6QIK; -.
DR PDBsum; 6QT0; -.
DR PDBsum; 6QTZ; -.
DR PDBsum; 6R84; -.
DR PDBsum; 6R86; -.
DR PDBsum; 6R87; -.
DR PDBsum; 6RI5; -.
DR PDBsum; 6RZZ; -.
DR PDBsum; 6S05; -.
DR PDBsum; 6YLG; -.
DR PDBsum; 6YLH; -.
DR PDBsum; 6YLX; -.
DR PDBsum; 6YLY; -.
DR PDBsum; 7BT6; -.
DR PDBsum; 7BTB; -.
DR PDBsum; 7OF1; -.
DR PDBsum; 7OH3; -.
DR PDBsum; 7OHP; -.
DR PDBsum; 7OHQ; -.
DR PDBsum; 7OHR; -.
DR PDBsum; 7OHS; -.
DR PDBsum; 7OHT; -.
DR PDBsum; 7OHU; -.
DR PDBsum; 7OHV; -.
DR PDBsum; 7OHW; -.
DR PDBsum; 7OHX; -.
DR PDBsum; 7OHY; -.
DR AlphaFoldDB; Q12522; -.
DR SMR; Q12522; -.
DR BioGRID; 36193; 616.
DR DIP; DIP-5395N; -.
DR IntAct; Q12522; 88.
DR MINT; Q12522; -.
DR STRING; 4932.YPR016C; -.
DR iPTMnet; Q12522; -.
DR MaxQB; Q12522; -.
DR PaxDb; Q12522; -.
DR PRIDE; Q12522; -.
DR EnsemblFungi; YPR016C_mRNA; YPR016C; YPR016C.
DR GeneID; 856126; -.
DR KEGG; sce:YPR016C; -.
DR SGD; S000006220; TIF6.
DR VEuPathDB; FungiDB:YPR016C; -.
DR eggNOG; KOG3185; Eukaryota.
DR GeneTree; ENSGT00390000015972; -.
DR HOGENOM; CLU_071894_0_0_1; -.
DR InParanoid; Q12522; -.
DR OMA; GEDTTGP; -.
DR BioCyc; YEAST:G3O-34176-MON; -.
DR EvolutionaryTrace; Q12522; -.
DR PRO; PR:Q12522; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12522; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR GO; GO:0043023; F:ribosomal large subunit binding; IDA:SGD.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:1902626; P:assembly of large subunit precursor of preribosome; IMP:SGD.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IBA:GO_Central.
DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0042256; P:mature ribosome assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD.
DR GO; GO:0000054; P:ribosomal subunit export from nucleus; IGI:SGD.
DR GO; GO:0006364; P:rRNA processing; IGI:SGD.
DR CDD; cd00527; IF6; 1.
DR HAMAP; MF_00032; eIF_6; 1.
DR InterPro; IPR002769; eIF6.
DR PANTHER; PTHR10784; PTHR10784; 1.
DR Pfam; PF01912; eIF-6; 1.
DR PIRSF; PIRSF006413; IF-6; 1.
DR SMART; SM00654; eIF6; 1.
DR TIGRFAMs; TIGR00323; eIF-6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Initiation factor; Nucleus; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Ribosome biogenesis.
FT CHAIN 1..245
FT /note="Eukaryotic translation initiation factor 6"
FT /id="PRO_0000153742"
FT MOD_RES 174
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03132"
FT MOD_RES 175
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03132"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:1G62"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:1G62"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:1G62"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:1G62"
FT HELIX 32..42
FT /evidence="ECO:0007829|PDB:1G62"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:1G62"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:1G62"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:1G62"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:1G62"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:1G62"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:1G62"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:1G62"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:1G62"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:1G62"
FT HELIX 123..133
FT /evidence="ECO:0007829|PDB:1G62"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:1G62"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1G62"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:1G62"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:1G62"
FT HELIX 167..177
FT /evidence="ECO:0007829|PDB:1G62"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:1G62"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:1G62"
FT HELIX 193..196
FT /evidence="ECO:0007829|PDB:1G62"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:1G62"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:1G62"
FT HELIX 212..221
FT /evidence="ECO:0007829|PDB:1G62"
SQ SEQUENCE 245 AA; 26458 MW; 1BCE041C61DFD2A8 CRC64;
MATRTQFENS NEIGVFSKLT NTYCLVAVGG SENFYSAFEA ELGDAIPIVH TTIAGTRIIG
RMTAGNRRGL LVPTQTTDQE LQHLRNSLPD SVKIQRVEER LSALGNVICC NDYVALVHPD
IDRETEELIS DVLGVEVFRQ TISGNILVGS YCSLSNQGGL VHPQTSVQDQ EELSSLLQVP
LVAGTVNRGS SVVGAGMVVN DYLAVTGLDT TAPELSVIES IFRLQDAQPE SISGNLRDTL
IETYS
