Oxysterol-binding protein homolog 1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P35845 (OSH1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 134. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Oxysterol-binding protein homolog 1

Gene names

Name:	SWH1
Synonyms:	OSH1
Ordered Locus Names:	YAR042W
ORF Names:	YAR044W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	1188 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Lipid-binding protein involved in maintenance of intracellular sterol distribution and homeostasis. Binds to phosphoinositides. May be involved in formation of PMN vesicles by altering the membrane lipid composition. Ref.11
Subunit structure	Interacts with NVJ1. Ref.12
Subcellular location	Cytoplasm. Golgi apparatus membrane. Nucleus outer membrane. Note: Soluble protein that accumulates on the surface of late Golgi membranes and at nucleus-vacuole (NV) junctions, interorganelle interfaces between the nuclear envelope and the vacuole membrane formed during piecemeal microautophagy of the nucleus (PMN). Targeted exclusively to NV junctions in stationary phase. Ref.2 Ref.9 Ref.12
Domain	The ankyrin repeats are required for targeting the protein to the NV junction. Ref.2 The PH domain is required for targeting the protein to the late Golgi. Ref.2 The FFAT motif is required for interaction with SCS2 and proper localization of the protein. Ref.2
Sequence similarities	Belongs to the OSBP family. Contains 3 ANK repeats. Contains 1 PH domain.

Ontologies

Keywords
Biological process	Lipid transport Transport
Cellular component	Cytoplasm Golgi apparatus Membrane Nucleus
Domain	ANK repeat Repeat
Ligand	Lipid-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	endocytosis Inferred from genetic interaction Ref.11. Source: SGD exocytosis Inferred from genetic interaction PubMed 17004323. Source: SGD maintenance of cell polarity Inferred from genetic interaction PubMed 17004323. Source: SGD
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell Golgi trans cisterna Inferred from direct assay Ref.9. Source: SGD early endosome Inferred from direct assay Ref.9. Source: SGD endoplasmic reticulum Inferred from direct assay Ref.2. Source: SGD nuclear envelope Inferred from direct assay Ref.2. Source: SGD nuclear outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	1-phosphatidylinositol binding Inferred from sequence or structural similarity Ref.10 PubMed 9651677. Source: SGD oxysterol binding Inferred from sequence or structural similarity Ref.10. Source: SGD sterol transporter activity Inferred from direct assay PubMed 20008566. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1188

1188

Oxysterol-binding protein homolog 1

PRO_0000100387

Regions

Repeat

51 – 80

ANK 1

Repeat

96 – 125

ANK 2

Repeat

196 – 225

ANK 3

Domain

330 – 379

Motif

716 – 722

FFAT

Compositional bias

434 – 472

Asn/Asp-rich

Amino acid modifications

Modified residue

394

Phosphoserine Ref.15

Modified residue

396

Phosphoserine Ref.16

Modified residue

442

Phosphoserine Ref.17 Ref.18

Modified residue

488

Phosphoserine Ref.17

Modified residue

490

Phosphoserine Ref.14 Ref.15 Ref.17 Ref.18

Modified residue

492

Phosphoserine Ref.18

Modified residue

500

Phosphoserine Ref.18

Modified residue

678

Phosphoserine Ref.15 Ref.17 Ref.18

Modified residue

683

Phosphoserine Ref.18

Modified residue

691

Phosphoserine Ref.18

Modified residue

692

Phosphothreonine Ref.18

Modified residue

694

Phosphothreonine Ref.18

Modified residue

708

Phosphoserine Ref.15 Ref.18

Modified residue

712

Phosphoserine Ref.15 Ref.17 Ref.18

Modified residue

762

Phosphoserine Ref.18

Modified residue

1053

Phosphothreonine Ref.17 Ref.18

Modified residue

1056

Phosphoserine Ref.17 Ref.18

Experimental info

Mutagenesis

719

D → A: Abolishes function. Ref.2

Sequence conflict

244

D → Y in CAA52646. Ref.1

Sequence conflict

248

N → S Ref.3

Sequence conflict

248

N → S Ref.4

Sequence conflict

424

P → A in CAA52646. Ref.1

Sequence conflict

464

D → NNN Ref.1

Sequence conflict

468 – 469

YD → DY Ref.1

Sequence conflict

495 – 496

TP → AS in CAA52646. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P35845 [UniParc].

Last modified December 6, 2005. Version 4.
Checksum: B9DA826745CEB30B
Show »

FASTA

1,188

135,098

        10         20         30         40         50         60 
MEQPDLSSVA ISKPLLKLKL LDALRQGSFP NLQDLLKKQF QPLDDPNVQQ VLHLMLHYAV 

        70         80         90        100        110        120 
QVAPMAVIKE IVHHWVSTTN TTFLNIHLDL NERDSNGNTP LHIAAYQSRG DIVAFLLDQP 

       130        140        150        160        170        180 
TINDCVLNNS HLQAIEMCKN LNIAQMMQVK RSTYVAETAQ EFRTAFNNRD FGHLESILSS 

       190        200        210        220        230        240 
PRNAELLDIN GMDPETGDTV LHEFVKKRDV IMCRWLLEHG ADPFKRDRKG KLPIELVRKV 

       250        260        270        280        290        300 
NENDTATNTK IAIDIELKKL LERATREQSV IDVTNNNLHE APTYKGYLKK WTNFAQGYKL 

       310        320        330        340        350        360 
RWFILSSDGK LSYYIDQADT KNACRGSLNM SSCSLHLDSS EKLKFEIIGG NNGVIRWHLK 

       370        380        390        400        410        420 
GNHPIETNRW VWAIQGAIRY AKDREILLHN GPYSPSLALS HGLSSKVSNK ENLHATSKRL 

       430        440        450        460        470        480 
TKSPHLSKST LTQNDHDNDD DSTNNNNNKS NNDYDDNNNN NNNDDDDYDD DDESRPLIEP 

       490        500        510        520        530        540 
LPLISSRSQS LSEITPGPHS RKSTVSSTRA ADIPSDDEGY SEDDSDDDGN SSYTMENGGE 

       550        560        570        580        590        600 
NDGDEDLNAI YGPYIQKLHM LQRSISIELA SLNELLQDKQ QHDEYWNTVN TSIETVSEFF 

       610        620        630        640        650        660 
DKLNRLTSQR EKRMIAQMTK QRDVNNVWIQ SVKDLEMELV DKDEKLVALD KERKNLKKML 

       670        680        690        700        710        720 
QKKLNNQPQV ETEANEESDD ANSMIKGSQE STNTLEEIVK FIEATKESDE DSDADEFFDA 

       730        740        750        760        770        780 
EEAASDKKAN DSEDLTTNKE TPANAKPQEE APEDESLIVI SSPQVEKKNQ LLKEGSFVGY 

       790        800        810        820        830        840 
EDPVRTKLAL DEDNRPKIGL WSVLKSMVGQ DLTKLTLPVS FNEPTSLLQR VSEDIEYSHI 

       850        860        870        880        890        900 
LDQAATFEDS SLRMLYVAAF TASMYASTTN RVSKPFNPLL GETFEYARTD GQYRFFTEQV 

       910        920        930        940        950        960 
SHHPPISATW TESPKWDFYG ECNVDSSFNG RTFAVQHLGL WYITIRPDHN ISVPEETYSW 

       970        980        990       1000       1010       1020 
KKPNNTVIGI LMGKPQVDNS GDVKVTNHTT GDYCMLHYKA HGWTSAGAYE VRGEVFNKDD 

      1030       1040       1050       1060       1070       1080 
KKLWVLGGHW NDSIYGKKVT ARGGELTLDR IKTANSATGG PKLDGSKFLI WKANERPSVP 

      1090       1100       1110       1120       1130       1140 
FNLTSFALTL NALPPHLIPY LAPTDSRLRP DQRAMENGEY DKAAAEKHRV EVKQRAAKKE 

      1150       1160       1170       1180 
REQKGEEYRP KWFVQEEHPV TKSLYWKFNG EYWNKRKNHD FKDCADIF

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"SWH1 from yeast encodes a candidate nuclear factor containing ankyrin repeats and showing homology to mammalian oxysterol-binding protein." Schmalix W.A., Bandlow W. Biochim. Biophys. Acta 1219:205-210(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DL-1.
[2]	"A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP." Loewen C.J.R., Roy A., Levine T.P. EMBO J. 22:2025-2035(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DOMAIN FFAT MOTIF, MUTAGENESIS OF ASP-719, SUBCELLULAR LOCATION. Strain: ATCC 96099 / S288c / SEY6210.
[3]	"Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 52 Kbp CDC15-FLO1-PHO11-YAR074 region." Bussey H., Keng T., Storms R.K., Vo D., Zhong W., Fortin N., Barton A.B., Kaback D.B., Clark M.W. Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"The nucleotide sequence of chromosome I from Saccharomyces cerevisiae." Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., Storms R.K. Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[5]	Sethuraman A., Cherry J.M. Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO C-TERMINUS.
[6]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[7]	"Reinvestigation of the Saccharomyces cerevisiae genome annotation by comparison to the genome of a related fungus: Ashbya gossypii." Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A., Gates K., Gaffney T.D., Philippsen P. Genome Biol. 4:R45.1-R45.13(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 199-264. Strain: ATCC 204511 / S288c / AB972.
[8]	"A new family of yeast genes implicated in ergosterol synthesis is related to the human oxysterol binding protein." Jiang B., Brown J.L., Sheraton J., Fortin N., Bussey H. Yeast 10:341-353(1994) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[9]	"Dual targeting of Osh1p, a yeast homologue of oxysterol-binding protein, to both the Golgi and the nucleus-vacuole junction." Levine T.P., Munro S. Mol. Biol. Cell 12:1633-1644(2001) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[10]	"Overlapping functions of the yeast oxysterol-binding protein homologues." Beh C.T., Cool L., Phillips J., Rine J. Genetics 157:1117-1140(2001) [PubMed] [Europe PMC] [Abstract] Cited for: GENETIC ANALYSIS.
[11]	"A role for yeast oxysterol-binding protein homologs in endocytosis and in the maintenance of intracellular sterol-lipid distribution." Beh C.T., Rine J. J. Cell Sci. 117:2983-2996(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Nvj1p is the outer-nuclear-membrane receptor for oxysterol-binding protein homolog Osh1p in Saccharomyces cerevisiae." Kvam E., Goldfarb D.S. J. Cell Sci. 117:4959-4968(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NVJ1, SUBCELLULAR LOCATION.
[13]	"Genome-wide analysis of membrane targeting by S.cerevisiae pleckstrin homology domains." Yu J.W., Mendrola J.M., Audhya A., Singh S., Keleti D., DeWald D.B., Murray D., Emr S.D., Lemmon M.A. Mol. Cell 13:677-688(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHOINOSITIDE-BINDING.
[14]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-490, MASS SPECTROMETRY. Strain: YAL6B.
[15]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-490; SER-678; SER-708 AND SER-712, MASS SPECTROMETRY. Strain: ADR376.
[16]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396, MASS SPECTROMETRY.
[17]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442; SER-488; SER-490; SER-678; SER-712; THR-1053 AND SER-1056, MASS SPECTROMETRY.
[18]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442; SER-490; SER-492; SER-500; SER-678; SER-683; SER-691; THR-692; THR-694; SER-708; SER-712; SER-762; THR-1053 AND SER-1056, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X74552 Genomic DNA. Translation: CAA52646.1. AY241177 Genomic DNA. Translation: AAP31019.1. L28920 Genomic DNA. Translation: AAC09496.2. AY260892 Genomic DNA. Translation: AAP21760.1. BK006935 Genomic DNA. Translation: DAA07006.1.
PIR	S47536.
RefSeq	NP_009421.3. NM_001178227.1.
3D structure databases
ProteinModelPortal	P35845.
SMR	P35845. Positions 21-245, 285-374, 874-1161.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6269N. DIP-6839N.
IntAct	P35845. 26 interactions.
MINT	MINT-571501.
Proteomic databases
PaxDb	P35845.
PeptideAtlas	P35845.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YAR042W; YAR042W; YAR042W.
GeneID	851286.
KEGG	sce:YAR042W.
Organism-specific databases
CYGD	YAR042w.
SGD	S000000081. SWH1.
Phylogenomic databases
eggNOG	COG0666.
GeneTree	ENSGT00700000104473.
HOGENOM	HOG000186039.
KO	K06867.
OMA	SFNEPTS.
OrthoDB	EOG4G7G6M.
Gene expression databases
Genevestigator	P35845.
GermOnline	YAR042W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	1.25.40.20. 2 hits. 2.30.29.30. 1 hit.
InterPro	IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR000648. Oxysterol-bd. IPR018494. Oxysterol-bd_CS. IPR011993. PH_like_dom. IPR001849. Pleckstrin_homology. [Graphical view]
PANTHER	PTHR10972. PTHR10972. 1 hit.
Pfam	PF00023. Ank. 2 hits. PF01237. Oxysterol_BP. 1 hit. PF00169. PH. 1 hit. [Graphical view]
SMART	SM00248. ANK. 2 hits. SM00233. PH. 1 hit. [Graphical view]
SUPFAM	SSF48403. ANK. 1 hit.
PROSITE	PS50297. ANK_REP_REGION. 2 hits. PS50088. ANK_REPEAT. 2 hits. PS01013. OSBP. 1 hit. PS50003. PH_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	968288.

Entry information

Entry name

OSH1_YEAST

Accession

Primary (citable) accession number: P35845
Secondary accession number(s): D6VPN6

Q86ZS1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	December 6, 2005
Last modified:	May 1, 2013
This is version 134 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome I

Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents