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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)DescriptionActionsGraphical viewLength
Binding sitei129PhosphatidylserineCombined sources1 Publication1
Binding sitei183PhosphatidylserineCombined sources1 Publication1
Binding sitei351Phosphatidylinositol 4-phosphateCombined sources1 Publication1
Binding sitei355Phosphatidylinositol 4-phosphateCombined sources1 Publication1
Binding sitei359Phosphatidylinositol 4-phosphateCombined sources1 Publication1

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.
ReactomeiR-SCE-1482801. Acyl chain remodelling of PS.
R-SCE-192105. Synthesis of bile acids and bile salts.

Protein family/group databases

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

Chemistry databases

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)DescriptionActionsGraphical viewLength
Mutagenesisi69L → A or D: Strongly reduced binding to phosphatidylserine. 1 Publication1
Mutagenesisi69L → D: Strongly reduced binding to phosphatidylserine and phosphatidylinositol 4-phosphate (PI4P). 1 Publication1
Mutagenesisi69L → F: Does not affect binding to phosphatidylserine. 1 Publication1
Mutagenesisi71T → P: Abolished binding to phosphatidylserine. 1 Publication1
Mutagenesisi73I → D: Strongly reduced binding to phosphatidylserine. 1 Publication1
Mutagenesisi126K → A: Strongly reduced binding to phosphatidylserine. 1 Publication1
Mutagenesisi129N → A: Strongly reduced binding to phosphatidylserine. 1 Publication1
Mutagenesisi157 – 158HH → AA: Strongly reduced binding to phosphatidylinositol 4-phosphate (PI4P). Does not affect binding to phosphatidylserine. 1 Publication2
Mutagenesisi157H → A: Does not affect binding to phosphatidylserine. 1 Publication1
Mutagenesisi158H → A: Does not affect binding to phosphatidylserine. 1 Publication1
Mutagenesisi182K → A: Does not affect binding to phosphatidylserine. 1 Publication1
Mutagenesisi351K → A: Does not affect binding to phosphatidylserine. 1 Publication1
Mutagenesisi351K → E: Strongly reduced binding to phosphatidylinositol 4-phosphate (PI4P). Does not affect binding to phosphatidylserine. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001003901 – 448Oxysterol-binding protein homolog 6Add BLAST448

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei16PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ02201.
PRIDEiQ02201.

PTM databases

iPTMnetiQ02201.

Interactioni

Protein-protein interaction databases

BioGridi34135. 31 interactors.
IntActiQ02201. 11 interactors.
MINTiMINT-2780677.

Structurei

Secondary structure

1448
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi37 – 39Combined sources3
Helixi45 – 55Combined sources11
Helixi71 – 73Combined sources3
Beta strandi74 – 78Combined sources5
Helixi79 – 85Combined sources7
Helixi90 – 98Combined sources9
Helixi102 – 115Combined sources14
Turni116 – 118Combined sources3
Beta strandi122 – 124Combined sources3
Beta strandi126 – 128Combined sources3
Beta strandi135 – 141Combined sources7
Beta strandi147 – 156Combined sources10
Turni157 – 160Combined sources4
Beta strandi161 – 168Combined sources8
Helixi169 – 171Combined sources3
Beta strandi173 – 179Combined sources7
Beta strandi181 – 185Combined sources5
Beta strandi187 – 194Combined sources8
Beta strandi197 – 206Combined sources10
Beta strandi210 – 218Combined sources9
Beta strandi222 – 225Combined sources4
Beta strandi227 – 230Combined sources4
Beta strandi233 – 236Combined sources4
Beta strandi238 – 243Combined sources6
Beta strandi248 – 253Combined sources6
Beta strandi258 – 260Combined sources3
Beta strandi263 – 271Combined sources9
Beta strandi277 – 284Combined sources8
Beta strandi287 – 293Combined sources7
Beta strandi302 – 306Combined sources5
Turni307 – 309Combined sources3
Helixi320 – 322Combined sources3
Helixi328 – 331Combined sources4
Helixi333 – 340Combined sources8
Helixi344 – 367Combined sources24
Beta strandi375 – 379Combined sources5
Beta strandi387 – 392Combined sources6
Helixi400 – 410Combined sources11
Helixi421 – 424Combined sources4
Helixi427 – 433Combined sources7
Helixi436 – 440Combined sources5

3D structure databases

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

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni64 – 69Phosphatidylinositol 4-phosphate bindingCombined sources1 Publication6
Regioni64 – 69Phosphatidylserine bindingCombined sources1 Publication6
Regioni126 – 129Phosphatidylinositol 4-phosphate bindingCombined sources1 Publication4
Regioni157 – 158Phosphatidylinositol 4-phosphate bindingCombined sources1 Publication2

Sequence similaritiesi

Belongs to the OSBP family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000074515.
HOGENOMiHOG000233871.
InParanoidiQ02201.
KOiK20464.
OMAiAIQAKDM.
OrthoDBiEOG092C2XNN.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4B2ZX-ray1.95A/B1-448[»]
4PH7X-ray2.55A/B/C/D1-448[»]
ProteinModelPortaliQ02201.
SMRiQ02201.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34135. 31 interactors.
IntActiQ02201. 11 interactors.
MINTiMINT-2780677.

Chemistry databases

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.
PRIDEiQ02201.

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.
KOiK20464.
OMAiAIQAKDM.
OrthoDBiEOG092C2XNN.

Enzyme and pathway databases

BioCyciYEAST:G3O-31981-MONOMER.
ReactomeiR-SCE-1482801. Acyl chain remodelling of PS.
R-SCE-192105. Synthesis of bile acids and bile salts.

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...

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: November 30, 2016
This is version 132 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.