OSH3_YEAST
ID OSH3_YEAST Reviewed; 996 AA.
AC P38713; D3DL23;
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=Oxysterol-binding protein homolog 3 {ECO:0000303|PubMed:11238399};
DE AltName: Full=Oxysterol-binding protein-related protein 3;
DE Short=ORP 3;
DE Short=OSBP-related protein 3;
GN Name=OSH3 {ECO:0000303|PubMed:11238399}; OrderedLocusNames=YHR073W;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 SUBCELLULAR LOCATION.
RX PubMed=11408574; DOI=10.1091/mbc.12.6.1633;
RA Levine T.P., Munro S.;
RT "Dual targeting of Osh1p, a yeast homologue of oxysterol-binding protein,
RT to both the Golgi and the nucleus-vacuole junction.";
RL Mol. Biol. Cell 12:1633-1644(2001).
RN [4]
RP GENETIC ANALYSIS.
RX PubMed=11238399; DOI=10.1093/genetics/157.3.1117;
RA Beh C.T., Cool L., Phillips J., Rine J.;
RT "Overlapping functions of the yeast oxysterol-binding protein homologues.";
RL Genetics 157:1117-1140(2001).
RN [5]
RP DOMAIN.
RX PubMed=12049664; DOI=10.1186/gb-2002-3-5-research0023;
RA Anantharaman V., Aravind L.;
RT "The GOLD domain, a novel protein module involved in Golgi function and
RT secretion.";
RL Genome Biol. 3:RESEARCH0023.1-RESEARCH0023.7(2002).
RN [6]
RP DOMAIN FFAT MOTIF, AND SUBCELLULAR LOCATION.
RX PubMed=12727870; DOI=10.1093/emboj/cdg201;
RA Loewen C.J.R., Roy A., Levine T.P.;
RT "A conserved ER targeting motif in three families of lipid binding proteins
RT and in Opi1p binds VAP.";
RL EMBO J. 22:2025-2035(2003).
RN [7]
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 [8]
RP FUNCTION.
RX PubMed=15173322; DOI=10.1242/jcs.01157;
RA Beh C.T., Rine J.;
RT "A role for yeast oxysterol-binding protein homologs in endocytosis and in
RT the maintenance of intracellular sterol-lipid distribution.";
RL J. Cell Sci. 117:2983-2996(2004).
RN [9]
RP DOMAIN.
RX PubMed=15023338; DOI=10.1016/s1097-2765(04)00083-8;
RA Yu J.W., Mendrola J.M., Audhya A., Singh S., Keleti D., DeWald D.B.,
RA Murray D., Emr S.D., Lemmon M.A.;
RT "Genome-wide analysis of membrane targeting by S.cerevisiae pleckstrin
RT homology domains.";
RL Mol. Cell 13:677-688(2004).
RN [10]
RP FUNCTION.
RX PubMed=16585271; DOI=10.1083/jcb.200510084;
RA Raychaudhuri S., Im Y.J., Hurley J.H., Prinz W.A.;
RT "Nonvesicular sterol movement from plasma membrane to ER requires
RT oxysterol-binding protein-related proteins and phosphoinositides.";
RL J. Cell Biol. 173:107-119(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-210, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-352, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-605, 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 [14]
RP DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=20008566; DOI=10.1083/jcb.200905007;
RA Schulz T.A., Choi M.G., Raychaudhuri S., Mears J.A., Ghirlando R.,
RA Hinshaw J.E., Prinz W.A.;
RT "Lipid-regulated sterol transfer between closely apposed membranes by
RT oxysterol-binding protein homologues.";
RL J. Cell Biol. 187:889-903(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193; THR-210;
RP THR-323; SER-324 AND THR-325, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21295699; DOI=10.1016/j.cell.2010.12.034;
RA Stefan C.J., Manford A.G., Baird D., Yamada-Hanff J., Mao Y., Emr S.D.;
RT "Osh proteins regulate phosphoinositide metabolism at ER-plasma membrane
RT contact sites.";
RL Cell 144:389-401(2011).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP FUNCTION.
RX PubMed=24213531; DOI=10.1242/jcs.132001;
RA Kajiwara K., Ikeda A., Aguilera-Romero A., Castillon G.A., Kagiwada S.,
RA Hanada K., Riezman H., Muniz M., Funato K.;
RT "Osh proteins regulate COPII-mediated vesicular transport of ceramide from
RT the endoplasmic reticulum in budding yeast.";
RL J. Cell Sci. 127:376-387(2014).
RN [19] {ECO:0007744|PDB:4IAP, ECO:0007744|PDB:4IC4, ECO:0007744|PDB:4INQ}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 605-996 IN COMPLEX WITH
RP 1,2-DIOCTANOYL-SN-GLYCERO-3-PHOSPHO-(1D-MYO-INOSITOL-4-PHOSPHATE).
RX PubMed=23791945; DOI=10.1016/j.str.2013.05.007;
RA Tong J., Yang H., Yang H., Eom S.H., Im Y.J.;
RT "Structure of Osh3 reveals a conserved mode of phosphoinositide binding in
RT oxysterol-binding proteins.";
RL Structure 21:1203-1213(2013).
CC -!- FUNCTION: Lipid transport protein (LTP) involved in non-vesicular
CC transfer of lipids between membranes. Functions in phosphoinositide-
CC coupled directional transport of various lipids by carrying the lipid
CC molecule in a hydrophobic pocket and transfering it between membranes
CC through the cytosol. Involved in maintenance of intracellular sterol
CC distribution and homeostasis (PubMed:11238399, PubMed:15173322). May
CC serve as a sensor of PI4P levels at PM-ER membrane contact site,
CC regulating PI4P phosphatase SAC1 activity (PubMed:21295699). May be
CC involved in ergosterol transport from the plasma membrane (PM) to the
CC ER, however it does not bind sterols directly (PubMed:16585271,
CC PubMed:23791945). Plays a role in the positive regulation of vesicular
CC transport of ceramide from the ER to the Golgi, negatively regulating
CC COPII-mediated ER export of cargos (PubMed:24213531).
CC {ECO:0000269|PubMed:11238399, ECO:0000269|PubMed:15173322,
CC ECO:0000269|PubMed:16585271, ECO:0000269|PubMed:21295699,
CC ECO:0000269|PubMed:23791945, ECO:0000269|PubMed:24213531}.
CC -!- SUBUNIT: Interacts with SCS2. {ECO:0000305|PubMed:12727870}.
CC -!- INTERACTION:
CC P38713; P45818: ROK1; NbExp=3; IntAct=EBI-12630, EBI-15686;
CC P38713; P32368: SAC1; NbExp=2; IntAct=EBI-12630, EBI-16210;
CC P38713; P40075: SCS2; NbExp=2; IntAct=EBI-12630, EBI-16735;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11408574,
CC ECO:0000269|PubMed:12727870, ECO:0000269|PubMed:20008566}. Endoplasmic
CC reticulum membrane {ECO:0000269|PubMed:20008566}. Note=Enriched at the
CC cell periphery in a SCS2-dependent manner (PubMed:12727870). Enriched
CC on regions of the ER in close proximity with the plasma membrane (PM),
CC which may represent PM-ER membrane contact sites (MCS)
CC (PubMed:20008566). Localizes to PM-ER membrane contact sites dependent
CC upon PM PI4P levels (PubMed:21295699). {ECO:0000269|PubMed:12727870,
CC ECO:0000269|PubMed:20008566, ECO:0000269|PubMed:21295699}.
CC -!- DOMAIN: The GOLD (Golgi dynamics) domain is predicted to mediate
CC diverse protein-protein interactions. {ECO:0000305|PubMed:12049664}.
CC -!- DOMAIN: The PH domain weakly binds to phosphoinositides.
CC {ECO:0000269|PubMed:15023338}.
CC -!- DOMAIN: The FFAT (two phenylalanines in an acidic tract) motif is
CC required for interaction with SCS2 and proper localization of the
CC protein. {ECO:0000269|PubMed:12727870}.
CC -!- DOMAIN: The OSBP-related domain (ORD) mediates binding of sterols and
CC phospholipids. It displays an incomplete beta-barrel containing a
CC central hydrophobic tunnel that can accommodate a single lipid molecule
CC with a flexible lid covering the tunnel entrance. The ORD can bind two
CC membranes simultaneously. It has at least two membrane-binding
CC surfaces; one near the mouth of the lipid-binding pocket and a distal
CC site that can bind a second membrane. These structural features
CC correlate with the phosphatidylinositol 4-phosphate (PI(4)P)-coupled
CC lipid transport optimized in closely apposed membranes, such as
CC organelle contact sites. The lipid transfer cycle starts from the
CC association of the LTP with a donor membrane, which accompanies
CC conformational changes that uncover the ligand-binding pocket. The
CC tunnel opening is generally mediated by displacement of the lid
CC covering the binding pocket allowing uptake or release of a lipid
CC molecule. The LTPs extract the lipid from the membrane by providing a
CC hydrophobic environment as well as specific interaction. Dissociation
CC from the donor membrane shifts the conformation to a closed form. Then,
CC the LTPs loaded with a cargo lipid diffuse through the aqueous phase.
CC Lid opening may be induced by the interaction of a hydrophobic side of
CC the lid with the target membranes (Probable). The OSH3 ORD does not
CC accept sterols due to the small hydrophobic tunnel (PubMed:23791945).
CC {ECO:0000269|PubMed:23791945, ECO:0000305|PubMed:20008566}.
CC -!- MISCELLANEOUS: Present with 589 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
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DR EMBL; U10556; AAB68890.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06767.1; -; Genomic_DNA.
DR PIR; S46812; S46812.
DR RefSeq; NP_011940.1; NM_001179203.1.
DR PDB; 4IAP; X-ray; 2.30 A; A/B=221-315.
DR PDB; 4IC4; X-ray; 1.50 A; A=605-996.
DR PDB; 4INQ; X-ray; 2.20 A; A=605-996.
DR PDBsum; 4IAP; -.
DR PDBsum; 4IC4; -.
DR PDBsum; 4INQ; -.
DR AlphaFoldDB; P38713; -.
DR SMR; P38713; -.
DR BioGRID; 36507; 153.
DR DIP; DIP-2148N; -.
DR ELM; P38713; -.
DR IntAct; P38713; 10.
DR MINT; P38713; -.
DR STRING; 4932.YHR073W; -.
DR iPTMnet; P38713; -.
DR MaxQB; P38713; -.
DR PaxDb; P38713; -.
DR PRIDE; P38713; -.
DR EnsemblFungi; YHR073W_mRNA; YHR073W; YHR073W.
DR GeneID; 856472; -.
DR KEGG; sce:YHR073W; -.
DR SGD; S000001115; OSH3.
DR VEuPathDB; FungiDB:YHR073W; -.
DR eggNOG; KOG1737; Eukaryota.
DR HOGENOM; CLU_007105_4_0_1; -.
DR InParanoid; P38713; -.
DR OMA; WHLRASN; -.
DR BioCyc; YEAST:G3O-31122-MON; -.
DR Reactome; R-SCE-192105; Synthesis of bile acids and bile salts.
DR PRO; PR:P38713; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38713; protein.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0008289; F:lipid binding; IDA:SGD.
DR GO; GO:0032934; F:sterol binding; IBA:GO_Central.
DR GO; GO:0120015; F:sterol transfer activity; IDA:SGD.
DR GO; GO:0015248; F:sterol transporter activity; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IGI:SGD.
DR GO; GO:0035621; P:ER to Golgi ceramide transport; IMP:SGD.
DR GO; GO:0006887; P:exocytosis; IGI:SGD.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IGI:SGD.
DR GO; GO:0000742; P:karyogamy involved in conjugation with cellular fusion; IGI:SGD.
DR GO; GO:0030011; P:maintenance of cell polarity; IGI:SGD.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IGI:SGD.
DR GO; GO:0010922; P:positive regulation of phosphatase activity; IDA:SGD.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR GO; GO:0015918; P:sterol transport; IDA:SGD.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR036598; GOLD_dom_sf.
DR InterPro; IPR037239; OSBP_sf.
DR InterPro; IPR000648; Oxysterol-bd.
DR InterPro; IPR018494; Oxysterol-bd_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041680; PH_8.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR10972; PTHR10972; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR Pfam; PF15409; PH_8; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF101576; SSF101576; 1.
DR SUPFAM; SSF144000; SSF144000; 1.
DR PROSITE; PS01013; OSBP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endoplasmic reticulum; Lipid transport;
KW Lipid-binding; Membrane; Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..996
FT /note="Oxysterol-binding protein homolog 3"
FT /id="PRO_0000100389"
FT DOMAIN 221..315
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..183
FT /note="GOLD domain"
FT /evidence="ECO:0000255"
FT REGION 75..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..982
FT /note="OSBP-related domain (ORD)"
FT /evidence="ECO:0000305"
FT MOTIF 514..520
FT /note="FFAT"
FT COMPBIAS 346..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..602
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 657..660
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0007744|PDB:4INQ"
FT BINDING 717
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0007744|PDB:4INQ"
FT BINDING 745..746
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0007744|PDB:4INQ"
FT BINDING 945..949
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0007744|PDB:4INQ"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 210
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 323
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 325
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 352
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT STRAND 240..247
FT /evidence="ECO:0007829|PDB:4IAP"
FT TURN 248..251
FT /evidence="ECO:0007829|PDB:4IAP"
FT STRAND 252..260
FT /evidence="ECO:0007829|PDB:4IAP"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:4IAP"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:4IAP"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:4IAP"
FT TURN 279..282
FT /evidence="ECO:0007829|PDB:4IAP"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:4IAP"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:4IAP"
FT HELIX 300..311
FT /evidence="ECO:0007829|PDB:4IAP"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:4IAP"
FT HELIX 643..649
FT /evidence="ECO:0007829|PDB:4IC4"
FT STRAND 650..653
FT /evidence="ECO:0007829|PDB:4IC4"
FT HELIX 655..657
FT /evidence="ECO:0007829|PDB:4IC4"
FT HELIX 662..664
FT /evidence="ECO:0007829|PDB:4IC4"
FT STRAND 665..669
FT /evidence="ECO:0007829|PDB:4IC4"
FT HELIX 670..675
FT /evidence="ECO:0007829|PDB:4IC4"
FT HELIX 676..678
FT /evidence="ECO:0007829|PDB:4IC4"
FT TURN 679..681
FT /evidence="ECO:0007829|PDB:4IC4"
FT HELIX 682..687
FT /evidence="ECO:0007829|PDB:4IC4"
FT HELIX 693..703
FT /evidence="ECO:0007829|PDB:4IC4"
FT HELIX 704..708
FT /evidence="ECO:0007829|PDB:4IC4"
FT HELIX 711..715
FT /evidence="ECO:0007829|PDB:4IC4"
FT STRAND 717..719
FT /evidence="ECO:0007829|PDB:4IC4"
FT STRAND 726..731
FT /evidence="ECO:0007829|PDB:4IC4"
FT HELIX 732..734
FT /evidence="ECO:0007829|PDB:4IC4"
FT STRAND 736..744
FT /evidence="ECO:0007829|PDB:4IC4"
FT TURN 745..748
FT /evidence="ECO:0007829|PDB:4IC4"
FT STRAND 749..771
FT /evidence="ECO:0007829|PDB:4IC4"
FT STRAND 773..788
FT /evidence="ECO:0007829|PDB:4IC4"
FT TURN 789..791
FT /evidence="ECO:0007829|PDB:4IC4"
FT STRAND 794..798
FT /evidence="ECO:0007829|PDB:4IC4"
FT STRAND 802..805
FT /evidence="ECO:0007829|PDB:4IC4"
FT STRAND 807..810
FT /evidence="ECO:0007829|PDB:4IC4"
FT STRAND 813..816
FT /evidence="ECO:0007829|PDB:4IC4"
FT STRAND 818..824
FT /evidence="ECO:0007829|PDB:4IC4"
FT STRAND 829..834
FT /evidence="ECO:0007829|PDB:4IC4"
FT STRAND 838..841
FT /evidence="ECO:0007829|PDB:4IC4"
FT STRAND 846..852
FT /evidence="ECO:0007829|PDB:4IC4"
FT STRAND 862..867
FT /evidence="ECO:0007829|PDB:4IC4"
FT TURN 868..870
FT /evidence="ECO:0007829|PDB:4IC4"
FT STRAND 871..874
FT /evidence="ECO:0007829|PDB:4IC4"
FT TURN 875..877
FT /evidence="ECO:0007829|PDB:4IC4"
FT STRAND 880..883
FT /evidence="ECO:0007829|PDB:4IC4"
FT HELIX 891..893
FT /evidence="ECO:0007829|PDB:4IC4"
FT TURN 894..896
FT /evidence="ECO:0007829|PDB:4IC4"
FT HELIX 899..904
FT /evidence="ECO:0007829|PDB:4IC4"
FT TURN 909..914
FT /evidence="ECO:0007829|PDB:4IC4"
FT HELIX 920..922
FT /evidence="ECO:0007829|PDB:4IC4"
FT HELIX 924..930
FT /evidence="ECO:0007829|PDB:4IC4"
FT HELIX 934..953
FT /evidence="ECO:0007829|PDB:4IC4"
FT STRAND 961..967
FT /evidence="ECO:0007829|PDB:4IC4"
FT STRAND 970..973
FT /evidence="ECO:0007829|PDB:4IC4"
FT HELIX 980..985
FT /evidence="ECO:0007829|PDB:4IC4"
SQ SEQUENCE 996 AA; 113760 MW; B1AD1210EFFB9AFE CRC64;
METIDIQNRS FVVRWVKCGR GDVINYQIKP LKKSIEVGIY KKLKSSVDDH ASAVHIAPDT
KTLLDYTTKS LLHKGSSSNI EEHHRRSSQH SHSSSNGSDN KRKERSYSSL SISGIQQQSQ
EIPLREKLSA SGFTLVKRVG NVSGNTMVQG DLEVKDTDYY YAFILDNSSS KNAKKKILFN
ASVINGDNQS MISTRSTPPA RPTALSRTST QQDMLFRVGQ GRYLQGYLLK KRRKRLQGFK
KRFFTLDFRY GTLSYYLNDH NQTCRGEIVI SLSSVSANKK DKIIIIDSGM EVWVLKATTK
ENWQSWVDAL QTCFDDQFED KDTSTLEENP DILDDDKEVI NKSSPQDHDH LTPTATTKSA
LSHRQHTQKD MDDIYVPLPS ESYATFSMNL RLIQQRLEQC KKDSLSYKPT TLHQRSEGLN
GTHSSSSVFT NNRVSSFNHS SSGMTSSDSL ASEEVPSNKT YIEHALYNQL ADLEVFVSRF
VTQGEVLFKD HQILCKKAKD TRVSLTSYLS ENDEFFDAEE EISRGVIILP DTEDDINNIV
EETPLLGKSD QNEFTKEVQL SGSEQIASSS VESYTTNDEN HSRKHLKNRH KNRRRGHPHH
QKTKSAQSST ETFTSKDLFA LSYPKSVTRR NDIPEAAASP PSLLSFLRKN VGKDLSSIAM
PVTSNEPISI LQLISETFEY APLLTKATQR PDPITFVSAF AISFLSIYRD KTRTLRKPFN
PLLAETFELI REDMGFRLIS EKVSHRPPVF AFFAEHLDWE CSYTVTPSQK FWGKSIELNN
EGILRLKFKT TGELFEWTQP TTILKNLIAG ERYMEPVNEF EVHSSKGDKS HILFDKAGMF
SGRSEGFKVS IIPPPSSNRK KETLAGKWTQ SLANETTHET IWEVGDLVSN PKKKYGFTKF
TANLNEITEI EKGNLPPTDS RLRPDIRAYE EGNVDKAEEW KLKLEQLQRE RRNKGQDVEP
KYFEKVSKNE WKYITGPKSY WERRKKHDWS DISQLW
