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Protein

Oxysterol-binding protein homolog 6

Gene

OSH6

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Lipid transporter involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane: specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P, which is degraded by the SAC1 phosphatase in the endoplasmic reticulum (PubMed:23934110, PubMed:26206936). Binds phosphatidylserine and PI4P in a mutually exclusive manner (PubMed:26206936).2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei129 – 1291PhosphatidylserineCombined sources1 Publication
Binding sitei183 – 1831PhosphatidylserineCombined sources1 Publication
Binding sitei351 – 3511Phosphatidylinositol 4-phosphateCombined sources1 Publication
Binding sitei355 – 3551Phosphatidylinositol 4-phosphateCombined sources1 Publication
Binding sitei359 – 3591Phosphatidylinositol 4-phosphateCombined sources1 Publication

GO - Molecular functioni

  • lipid binding Source: SGD
  • oxysterol binding Source: SGD
  • phosphatidic acid binding Source: SGD
  • phosphatidylinositol-3,4-bisphosphate binding Source: SGD
  • phosphatidylinositol-3,5-bisphosphate binding Source: SGD
  • phosphatidylinositol-4-phosphate binding Source: UniProtKB
  • phosphatidylinositol-5-phosphate binding Source: SGD
  • phosphatidylserine binding Source: UniProtKB
  • phospholipid transporter activity Source: UniProtKB

GO - Biological processi

  • endocytosis Source: SGD
  • exocytosis Source: SGD
  • maintenance of cell polarity Source: SGD
  • phospholipid transport Source: UniProtKB
  • piecemeal microautophagy of nucleus Source: SGD
  • sterol homeostasis Source: SGD
  • sterol metabolic process Source: SGD
  • sterol transport Source: SGD
Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31981-MONOMER.

Protein family/group databases

TCDBi2.D.1.1.3. the pi4p/ps counter transporter (p/p-ct) family.

Chemistry

SwissLipidsiSLP:000000525.

Names & Taxonomyi

Protein namesi
Recommended name:
Oxysterol-binding protein homolog 6
Gene namesi
Name:OSH6
Ordered Locus Names:YKR003W
ORF Names:YK102
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKR003W.
SGDiS000001711. OSH6.

Subcellular locationi

GO - Cellular componenti

  • cortical endoplasmic reticulum Source: UniProtKB
  • cytoplasm Source: SGD
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • extrinsic component of membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi69 – 691L → A or D: Strongly reduced binding to phosphatidylserine. 1 Publication
Mutagenesisi69 – 691L → D: Strongly reduced binding to phosphatidylserine and phosphatidylinositol 4-phosphate (PI4P). 1 Publication
Mutagenesisi69 – 691L → F: Does not affect binding to phosphatidylserine. 1 Publication
Mutagenesisi71 – 711T → P: Abolished binding to phosphatidylserine. 1 Publication
Mutagenesisi73 – 731I → D: Strongly reduced binding to phosphatidylserine. 1 Publication
Mutagenesisi126 – 1261K → A: Strongly reduced binding to phosphatidylserine. 1 Publication
Mutagenesisi129 – 1291N → A: Strongly reduced binding to phosphatidylserine. 1 Publication
Mutagenesisi157 – 1582HH → AA: Strongly reduced binding to phosphatidylinositol 4-phosphate (PI4P). Does not affect binding to phosphatidylserine. 1 Publication
Mutagenesisi157 – 1571H → A: Does not affect binding to phosphatidylserine. 1 Publication
Mutagenesisi158 – 1581H → A: Does not affect binding to phosphatidylserine. 1 Publication
Mutagenesisi182 – 1821K → A: Does not affect binding to phosphatidylserine. 1 Publication
Mutagenesisi351 – 3511K → A: Does not affect binding to phosphatidylserine. 1 Publication
Mutagenesisi351 – 3511K → E: Strongly reduced binding to phosphatidylinositol 4-phosphate (PI4P). Does not affect binding to phosphatidylserine. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 448448Oxysterol-binding protein homolog 6PRO_0000100390Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ02201.
PeptideAtlasiQ02201.

PTM databases

iPTMnetiQ02201.

Interactioni

Protein-protein interaction databases

BioGridi34135. 30 interactions.
IntActiQ02201. 11 interactions.
MINTiMINT-2780677.

Structurei

Secondary structure

1
448
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi37 – 393Combined sources
Helixi45 – 5511Combined sources
Helixi71 – 733Combined sources
Beta strandi74 – 785Combined sources
Helixi79 – 857Combined sources
Helixi90 – 989Combined sources
Helixi102 – 11514Combined sources
Turni116 – 1183Combined sources
Beta strandi122 – 1243Combined sources
Beta strandi126 – 1283Combined sources
Beta strandi135 – 1417Combined sources
Beta strandi147 – 15610Combined sources
Turni157 – 1604Combined sources
Beta strandi161 – 1688Combined sources
Helixi169 – 1713Combined sources
Beta strandi173 – 1797Combined sources
Beta strandi181 – 1855Combined sources
Beta strandi187 – 1948Combined sources
Beta strandi197 – 20610Combined sources
Beta strandi210 – 2189Combined sources
Beta strandi222 – 2254Combined sources
Beta strandi227 – 2304Combined sources
Beta strandi233 – 2364Combined sources
Beta strandi238 – 2436Combined sources
Beta strandi248 – 2536Combined sources
Beta strandi258 – 2603Combined sources
Beta strandi263 – 2719Combined sources
Beta strandi277 – 2848Combined sources
Beta strandi287 – 2937Combined sources
Beta strandi302 – 3065Combined sources
Turni307 – 3093Combined sources
Helixi320 – 3223Combined sources
Helixi328 – 3314Combined sources
Helixi333 – 3408Combined sources
Helixi344 – 36724Combined sources
Beta strandi375 – 3795Combined sources
Beta strandi387 – 3926Combined sources
Helixi400 – 41011Combined sources
Helixi421 – 4244Combined sources
Helixi427 – 4337Combined sources
Helixi436 – 4405Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B2ZX-ray1.95A/B1-448[»]
4PH7X-ray2.55A/B/C/D1-448[»]
ProteinModelPortaliQ02201.
SMRiQ02201. Positions 46-442.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni64 – 696Phosphatidylinositol 4-phosphate bindingCombined sources1 Publication
Regioni64 – 696Phosphatidylserine bindingCombined sources1 Publication
Regioni126 – 1294Phosphatidylinositol 4-phosphate bindingCombined sources1 Publication
Regioni157 – 1582Phosphatidylinositol 4-phosphate bindingCombined sources1 Publication

Sequence similaritiesi

Belongs to the OSBP family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000074515.
HOGENOMiHOG000233871.
InParanoidiQ02201.
OMAiAIQAKDM.
OrthoDBiEOG74BK24.

Family and domain databases

InterProiIPR000648. Oxysterol-bd.
IPR018494. Oxysterol-bd_CS.
[Graphical view]
PANTHERiPTHR10972. PTHR10972. 1 hit.
PfamiPF01237. Oxysterol_BP. 1 hit.
[Graphical view]
PROSITEiPS01013. OSBP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q02201-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSKKLTVGS DSHRLSKSSF SSNKSSHSAT KDQPIDTDDI DEDDESGHNI
60 70 80 90 100
ILNIISQLRP GCDLTRITLP TFILEKKSML ERVTNQLQFP EFLLQAHSEK
110 120 130 140 150
DPLKRFLYVM KWYLAGWHIA PKAVKKPLNP VLGEYFTAYW DLPNKQQAYY
160 170 180 190 200
ISEQTSHHPP ECAYFYMIPE SSIRVDGVVI PKSRFLGNSS AAMMDGSTVL
210 220 230 240 250
QFLDIKDGNG KPEKYVLTQP NVYVRGILFG KMRIELGDHM IIKSPNFQAD
260 270 280 290 300
IEFKTKGYVF GTYDAIEGTV KDYDGNAYYE ISGKWNDVMY LKDLKQPRSS
310 320 330 340 350
PKVFLDTHKE SPLRPKVRPL SEQGEYESRK LWKKVTDALA VRNHPVATEE
360 370 380 390 400
KFQIEDHQRQ LAKKRIEDGV EFHPKLFRRS KPGEDLDYCI YKNIPVDEDP
410 420 430 440
EKQIRSILQI APILPGQQFT DKFFIPAFEK IKSQKKMIEN EKQNPAKQ
Length:448
Mass (Da):51,588
Last modified:July 1, 1993 - v1
Checksum:i44C4E16CF320DB78
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65124 Genomic DNA. Translation: CAA46249.1.
Z28228 Genomic DNA. Translation: CAA82073.1.
BK006944 Genomic DNA. Translation: DAA09159.1.
PIRiS25324.
RefSeqiNP_012928.1. NM_001179793.1.

Genome annotation databases

EnsemblFungiiYKR003W; YKR003W; YKR003W.
GeneIDi853872.
KEGGisce:YKR003W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65124 Genomic DNA. Translation: CAA46249.1.
Z28228 Genomic DNA. Translation: CAA82073.1.
BK006944 Genomic DNA. Translation: DAA09159.1.
PIRiS25324.
RefSeqiNP_012928.1. NM_001179793.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B2ZX-ray1.95A/B1-448[»]
4PH7X-ray2.55A/B/C/D1-448[»]
ProteinModelPortaliQ02201.
SMRiQ02201. Positions 46-442.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34135. 30 interactions.
IntActiQ02201. 11 interactions.
MINTiMINT-2780677.

Chemistry

SwissLipidsiSLP:000000525.

Protein family/group databases

TCDBi2.D.1.1.3. the pi4p/ps counter transporter (p/p-ct) family.

PTM databases

iPTMnetiQ02201.

Proteomic databases

MaxQBiQ02201.
PeptideAtlasiQ02201.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKR003W; YKR003W; YKR003W.
GeneIDi853872.
KEGGisce:YKR003W.

Organism-specific databases

EuPathDBiFungiDB:YKR003W.
SGDiS000001711. OSH6.

Phylogenomic databases

GeneTreeiENSGT00550000074515.
HOGENOMiHOG000233871.
InParanoidiQ02201.
OMAiAIQAKDM.
OrthoDBiEOG74BK24.

Enzyme and pathway databases

BioCyciYEAST:G3O-31981-MONOMER.

Miscellaneous databases

PROiQ02201.

Family and domain databases

InterProiIPR000648. Oxysterol-bd.
IPR018494. Oxysterol-bd_CS.
[Graphical view]
PANTHERiPTHR10972. PTHR10972. 1 hit.
PfamiPF01237. Oxysterol_BP. 1 hit.
[Graphical view]
PROSITEiPS01013. OSBP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequencing and analysis of a 24.7 kb segment encompassing centromere CEN11 of Saccharomyces cerevisiae reveals nine previously unknown open reading frames."
    Duesterhoeft A., Philippsen P.
    Yeast 8:749-759(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "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.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "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-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Lipid-regulated sterol transfer between closely apposed membranes by oxysterol-binding protein homologues."
    Schulz T.A., Choi M.G., Raychaudhuri S., Mears J.A., Ghirlando R., Hinshaw J.E., Prinz W.A.
    J. Cell Biol. 187:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Interactome map uncovers phosphatidylserine transport by oxysterol-binding proteins."
    Maeda K., Anand K., Chiapparino A., Kumar A., Poletto M., Kaksonen M., Gavin A.C.
    Nature 501:257-261(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH PHOSPHATIDYLSERINE, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-69; THR-71; ILE-73; LYS-126; ASN-129; HIS-157; HIS-158; LYS-182 AND LYS-351.
  10. "Phosphatidylserine transport by ORP/Osh proteins is driven by phosphatidylinositol 4-phosphate."
    Moser von Filseck J., Copic A., Delfosse V., Vanni S., Jackson C.L., Bourguet W., Drin G.
    Science 349:432-436(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) IN COMPLEX WITH PHOSPHATIDYLINOSITOL 4-PHOSPHATE, FUNCTION, MUTAGENESIS OF LEU-69; 157-HIS-HIS-158 AND LYS-351.

Entry informationi

Entry nameiOSH6_YEAST
AccessioniPrimary (citable) accession number: Q02201
Secondary accession number(s): D6VXT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: June 8, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2550 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.