OSH1_YEAST
ID OSH1_YEAST Reviewed; 1188 AA.
AC P35845; D6VPN6; P39555; P80234; Q86ZC4; Q86ZS1;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 4.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Oxysterol-binding protein homolog 1 {ECO:0000303|PubMed:11238399};
DE AltName: Full=Oxysterol-binding protein-related protein 1;
DE Short=ORP 1;
DE Short=OSBP-related protein 1;
GN Name=SWH1 {ECO:0000303|PubMed:8086466};
GN Synonyms=OSH1 {ECO:0000303|PubMed:11238399}; OrderedLocusNames=YAR042W;
GN ORFNames=YAR044W;
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=DL-1;
RX PubMed=8086466; DOI=10.1016/0167-4781(94)90273-9;
RA Schmalix W.A., Bandlow W.;
RT "SWH1 from yeast encodes a candidate nuclear factor containing ankyrin
RT repeats and showing homology to mammalian oxysterol-binding protein.";
RL Biochim. Biophys. Acta 1219:205-210(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DOMAIN FFAT MOTIF, MUTAGENESIS OF
RP ASP-719, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 96099 / S288c / SEY6210;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RA Bussey H., Keng T., Storms R.K., Vo D., Zhong W., Fortin N., Barton A.B.,
RA Kaback D.B., Clark M.W.;
RT "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 52
RT Kbp CDC15-FLO1-PHO11-YAR074 region.";
RL Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [5]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Sethuraman A., Cherry J.M.;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 199-264.
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA Gates K., Gaffney T.D., Philippsen P.;
RT "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT comparison to the genome of a related fungus: Ashbya gossypii.";
RL Genome Biol. 4:R45.1-R45.13(2003).
RN [8]
RP FUNCTION.
RX PubMed=8017104; DOI=10.1002/yea.320100307;
RA Jiang B., Brown J.L., Sheraton J., Fortin N., Bussey H.;
RT "A new family of yeast genes implicated in ergosterol synthesis is related
RT to the human oxysterol binding protein.";
RL Yeast 10:341-353(1994).
RN [9]
RP FUNCTION.
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 [10]
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 [11]
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 [12]
RP INTERACTION WITH NVJ1, AND SUBCELLULAR LOCATION.
RX PubMed=15367582; DOI=10.1242/jcs.01372;
RA Kvam E., Goldfarb D.S.;
RT "Nvj1p is the outer-nuclear-membrane receptor for oxysterol-binding protein
RT homolog Osh1p in Saccharomyces cerevisiae.";
RL J. Cell Sci. 117:4959-4968(2004).
RN [13]
RP SUBCELLULAR LOCATION.
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 [14]
RP INTERACTION WITH AFG2.
RX PubMed=16096648; DOI=10.1038/sj.emboj.7600764;
RA Wang P., Zhang Y., Li H., Chieu H.K., Munn A.L., Yang H.;
RT "AAA ATPases regulate membrane association of yeast oxysterol binding
RT proteins and sterol metabolism.";
RL EMBO J. 24:2989-2999(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-490; SER-678;
RP SER-708 AND SER-712, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-490; SER-500; SER-678;
RP THR-694; SER-708 AND SER-712, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [17]
RP DOMAIN.
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-490; SER-678; SER-683;
RP SER-691; THR-692; THR-694; SER-708 AND SER-712, AND IDENTIFICATION BY MASS
RP 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 [19]
RP SUBCELLULAR LOCATION.
RX PubMed=25420878; DOI=10.1007/s00018-014-1786-x;
RA Weber-Boyvat M., Kentala H., Peraenen J., Olkkonen V.M.;
RT "Ligand-dependent localization and function of ORP-VAP complexes at
RT membrane contact sites.";
RL Cell. Mol. Life Sci. 72:1967-1987(2015).
RN [20] {ECO:0007744|PDB:5H28, ECO:0007744|PDB:5H2C}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 12-274.
RX PubMed=28319008; DOI=10.1016/j.str.2017.02.010;
RA Manik M.K., Yang H., Tong J., Im Y.J.;
RT "Structure of yeast OSBP-related protein Osh1 reveals key determinants for
RT lipid transport and protein targeting at the nucleus-vacuole junction.";
RL Structure 25:617-629.e3(2017).
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:8017104, PubMed:11238399,
CC PubMed:15173322). Involved in non-vesicular transport of ergosterol and
CC PI(4)P at the NVJ. Binds sterol and PI4P in a mutually exclusive manner
CC (PubMed:28319008). May be involved in formation of PMN vesicles by
CC altering the membrane lipid composition (PubMed:15173322).
CC {ECO:0000269|PubMed:11238399, ECO:0000269|PubMed:15173322,
CC ECO:0000269|PubMed:28319008, ECO:0000269|PubMed:8017104}.
CC -!- SUBUNIT: Interacts with NVJ1 (PubMed:15367582, PubMed:28319008).
CC Interacts with the AAA ATPase AFG2; regulates OSH1 membrane
CC association. AFG2 is required for membrane dissociation of OSH1
CC (Probable). Interacts with SCS2 (PubMed:12727870).
CC {ECO:0000269|PubMed:12727870, ECO:0000269|PubMed:15367582,
CC ECO:0000269|PubMed:28319008, ECO:0000305|PubMed:16096648}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:11408574}. Nucleus outer membrane
CC {ECO:0000269|PubMed:11408574, ECO:0000269|PubMed:12727870,
CC ECO:0000269|PubMed:15367582, ECO:0000269|PubMed:25420878}. Endoplasmic
CC reticulum membrane {ECO:0000269|PubMed:12727870}. Vacuole membrane
CC {ECO:0000269|PubMed:11408574, ECO:0000269|PubMed:15367582,
CC ECO:0000269|PubMed:25420878}. Note=Soluble protein that accumulates on
CC the surface of late Golgi membranes and at nucleus-vacuole (NV)
CC junctions, interorganelle interfaces between the nuclear envelope and
CC the vacuole membrane formed during piecemeal microautophagy of the
CC nucleus (PMN). Targeted exclusively to NV junctions in stationary
CC phase. {ECO:0000269|PubMed:11408574, ECO:0000269|PubMed:15367582,
CC ECO:0000269|PubMed:25420878}.
CC -!- DOMAIN: The ankyrin repeats are required for targeting the protein to
CC the NV junction by interacting with NVJ1. {ECO:0000269|PubMed:12727870,
CC ECO:0000269|PubMed:28319008}.
CC -!- DOMAIN: The PH domain strongly binds to phosphoinositides and is
CC required for targeting the protein to the late Golgi membranes.
CC {ECO:0000269|PubMed:15023338}.
CC -!- DOMAIN: The FFAT (two phenylalanines in an acidic tract) motif is
CC required for interaction with SCS2 and is required for targeting the
CC protein to the ER. {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. {ECO:0000305|PubMed:20008566}.
CC -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X74552; CAA52646.1; -; Genomic_DNA.
DR EMBL; AY241177; AAP31019.1; -; Genomic_DNA.
DR EMBL; L28920; AAC09496.2; -; Genomic_DNA.
DR EMBL; AY260892; AAP21760.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA07006.1; -; Genomic_DNA.
DR PIR; S47536; S47536.
DR RefSeq; NP_009421.3; NM_001178227.1.
DR PDB; 5H28; X-ray; 1.50 A; A=12-274.
DR PDB; 5H2C; X-ray; 3.51 A; A=7-274.
DR PDBsum; 5H28; -.
DR PDBsum; 5H2C; -.
DR AlphaFoldDB; P35845; -.
DR SMR; P35845; -.
DR BioGRID; 31812; 133.
DR DIP; DIP-6839N; -.
DR ELM; P35845; -.
DR IntAct; P35845; 26.
DR MINT; P35845; -.
DR STRING; 4932.YAR042W; -.
DR iPTMnet; P35845; -.
DR MaxQB; P35845; -.
DR PaxDb; P35845; -.
DR PRIDE; P35845; -.
DR EnsemblFungi; YAR042W_mRNA; YAR042W; YAR042W.
DR GeneID; 851286; -.
DR KEGG; sce:YAR042W; -.
DR SGD; S000000081; SWH1.
DR VEuPathDB; FungiDB:YAR042W; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG1737; Eukaryota.
DR GeneTree; ENSGT00940000173329; -.
DR HOGENOM; CLU_001040_1_1_1; -.
DR InParanoid; P35845; -.
DR OMA; AQGHKWS; -.
DR BioCyc; YEAST:G3O-28883-MON; -.
DR Reactome; R-SCE-192105; Synthesis of bile acids and bile salts.
DR PRO; PR:P35845; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P35845; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005769; C:early endosome; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000138; C:Golgi trans cisterna; IDA:SGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR GO; GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071561; C:nucleus-vacuole junction; IDA:SGD.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
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:0006887; P:exocytosis; 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:0015918; P:sterol transport; IDA:SGD.
DR Gene3D; 1.25.40.20; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_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; IPR001849; PH_domain.
DR PANTHER; PTHR10972; PTHR10972; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF144000; SSF144000; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS01013; OSBP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Endoplasmic reticulum; Golgi apparatus;
KW Lipid transport; Lipid-binding; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transport; Vacuole.
FT CHAIN 1..1188
FT /note="Oxysterol-binding protein homolog 1"
FT /id="PRO_0000100387"
FT REPEAT 51..80
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 96..125
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 196..225
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT DOMAIN 330..379
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 415..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..1174
FT /note="OSBP-related domain (ORD)"
FT /evidence="ECO:0000305"
FT MOTIF 716..722
FT /note="FFAT"
FT COMPBIAS 444..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..474
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 834
FT /ligand="ergosterol"
FT /ligand_id="ChEBI:CHEBI:16933"
FT /evidence="ECO:0000250|UniProtKB:Q6CUK7"
FT BINDING 962
FT /ligand="ergosterol"
FT /ligand_id="ChEBI:CHEBI:16933"
FT /evidence="ECO:0000250|UniProtKB:Q6CUK7"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 691
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 692
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 694
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 712
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MUTAGEN 719
FT /note="D->A: Abolishes function."
FT /evidence="ECO:0000269|PubMed:12727870"
FT CONFLICT 244
FT /note="D -> Y (in Ref. 1; CAA52646)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="N -> S (in Ref. 3; AAC09496 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="P -> A (in Ref. 1; CAA52646)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="D -> NNN (in Ref. 1; CAA52646)"
FT /evidence="ECO:0000305"
FT CONFLICT 468..469
FT /note="YD -> DY (in Ref. 1; CAA52646)"
FT /evidence="ECO:0000305"
FT CONFLICT 495..496
FT /note="TP -> AS (in Ref. 1; CAA52646)"
FT /evidence="ECO:0000305"
FT HELIX 13..26
FT /evidence="ECO:0007829|PDB:5H28"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:5H28"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:5H28"
FT HELIX 55..62
FT /evidence="ECO:0007829|PDB:5H28"
FT HELIX 65..75
FT /evidence="ECO:0007829|PDB:5H28"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:5H28"
FT HELIX 110..117
FT /evidence="ECO:0007829|PDB:5H28"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:5H28"
FT HELIX 141..167
FT /evidence="ECO:0007829|PDB:5H28"
FT HELIX 171..178
FT /evidence="ECO:0007829|PDB:5H28"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:5H28"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:5H28"
FT HELIX 200..207
FT /evidence="ECO:0007829|PDB:5H28"
FT HELIX 210..218
FT /evidence="ECO:0007829|PDB:5H28"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:5H28"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:5H28"
FT HELIX 252..267
FT /evidence="ECO:0007829|PDB:5H28"
SQ SEQUENCE 1188 AA; 135098 MW; B9DA826745CEB30B CRC64;
MEQPDLSSVA ISKPLLKLKL LDALRQGSFP NLQDLLKKQF QPLDDPNVQQ VLHLMLHYAV
QVAPMAVIKE IVHHWVSTTN TTFLNIHLDL NERDSNGNTP LHIAAYQSRG DIVAFLLDQP
TINDCVLNNS HLQAIEMCKN LNIAQMMQVK RSTYVAETAQ EFRTAFNNRD FGHLESILSS
PRNAELLDIN GMDPETGDTV LHEFVKKRDV IMCRWLLEHG ADPFKRDRKG KLPIELVRKV
NENDTATNTK IAIDIELKKL LERATREQSV IDVTNNNLHE APTYKGYLKK WTNFAQGYKL
RWFILSSDGK LSYYIDQADT KNACRGSLNM SSCSLHLDSS EKLKFEIIGG NNGVIRWHLK
GNHPIETNRW VWAIQGAIRY AKDREILLHN GPYSPSLALS HGLSSKVSNK ENLHATSKRL
TKSPHLSKST LTQNDHDNDD DSTNNNNNKS NNDYDDNNNN NNNDDDDYDD DDESRPLIEP
LPLISSRSQS LSEITPGPHS RKSTVSSTRA ADIPSDDEGY SEDDSDDDGN SSYTMENGGE
NDGDEDLNAI YGPYIQKLHM LQRSISIELA SLNELLQDKQ QHDEYWNTVN TSIETVSEFF
DKLNRLTSQR EKRMIAQMTK QRDVNNVWIQ SVKDLEMELV DKDEKLVALD KERKNLKKML
QKKLNNQPQV ETEANEESDD ANSMIKGSQE STNTLEEIVK FIEATKESDE DSDADEFFDA
EEAASDKKAN DSEDLTTNKE TPANAKPQEE APEDESLIVI SSPQVEKKNQ LLKEGSFVGY
EDPVRTKLAL DEDNRPKIGL WSVLKSMVGQ DLTKLTLPVS FNEPTSLLQR VSEDIEYSHI
LDQAATFEDS SLRMLYVAAF TASMYASTTN RVSKPFNPLL GETFEYARTD GQYRFFTEQV
SHHPPISATW TESPKWDFYG ECNVDSSFNG RTFAVQHLGL WYITIRPDHN ISVPEETYSW
KKPNNTVIGI LMGKPQVDNS GDVKVTNHTT GDYCMLHYKA HGWTSAGAYE VRGEVFNKDD
KKLWVLGGHW NDSIYGKKVT ARGGELTLDR IKTANSATGG PKLDGSKFLI WKANERPSVP
FNLTSFALTL NALPPHLIPY LAPTDSRLRP DQRAMENGEY DKAAAEKHRV EVKQRAAKKE
REQKGEEYRP KWFVQEEHPV TKSLYWKFNG EYWNKRKNHD FKDCADIF
