P38755 · OSH7_YEAST

Function

function

ipid transport protein (LTP) involved in non-vesicular transfer of lipids between membranes. Functions in phosphoinositide-coupled directional transport of various lipids by carrying the lipid molecule in a hydrophobic pocket and transferring it between membranes through the cytosol. Involved in maintenance of intracellular sterol distribution and homeostasis (PubMed:15173322).
Involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane. Specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the PM in exchange for PI4P, which is delivered to the ER-localized PI4P phosphatase SAC1 for degradation. Thus, by maintaining a PI4P gradient at the ER/PM interface, SAC1 drives PS transport (PubMed:23934110, PubMed:26206936).
Binds phosphatidylserine and PI4P in a mutually exclusive manner (PubMed:26206936).

Miscellaneous

Present with 2350 molecules/cell in log phase SD medium.

Catalytic activity

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site64-69a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) (UniProtKB | ChEBI)
Binding site64-69a 1,2-diacyl-sn-glycero-3-phospho-L-serine (UniProtKB | ChEBI)
Binding site126-129a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) (UniProtKB | ChEBI)
Binding site129a 1,2-diacyl-sn-glycero-3-phospho-L-serine (UniProtKB | ChEBI)
Binding site157-158a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) (UniProtKB | ChEBI)
Binding site183a 1,2-diacyl-sn-glycero-3-phospho-L-serine (UniProtKB | ChEBI)
Binding site351a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) (UniProtKB | ChEBI)
Binding site355a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) (UniProtKB | ChEBI)
Binding site359a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcortical endoplasmic reticulum
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentendoplasmic reticulum membrane
Cellular Componentmembrane
Cellular Componentplasma membrane
Molecular Functionlipid binding
Molecular Functionphosphatidylinositol-4-phosphate binding
Molecular Functionphosphatidylserine binding
Molecular Functionphospholipid transporter activity
Molecular Functionsterol binding
Molecular Functionsterol transfer activity
Biological Processendocytosis
Biological Processexocytosis
Biological Processlate endosome to vacuole transport
Biological Processmaintenance of cell polarity
Biological Processphospholipid transport
Biological Processpiecemeal microautophagy of the nucleus
Biological Processsterol metabolic process
Biological Processsterol transport

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Oxysterol-binding protein homolog 7
  • Alternative names
    • Oxysterol-binding protein-related protein 7 (ORP 7; OSBP-related protein 7)

Gene names

    • Name
      OSH7
    • Ordered locus names
      YHR001W

Organism names

Accessions

  • Primary accession
    P38755
  • Secondary accessions
    • D3DKR7

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Cell membrane
Note: Localizes to the cortical endoplasmic reticulum at the endoplasmic reticulum-plasma membrane contact sites.

Keywords

PTM/Processing

Features

Showing features for chain, cross-link.

Type
IDPosition(s)Description
ChainPRO_00001003911-437Oxysterol-binding protein homolog 7
Cross-link276Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Interacts with the AAA ATPase VPS4; regulates OSH7 membrane association. VPS4 is required for membrane dissociation of OSH7.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region23-42Disordered
Region54-393OSBP-related domain (ORD)

Domain

The OSBP-related domain (ORD) mediates binding of sterols and phospholipids. It displays an incomplete beta-barrel containing a central hydrophobic tunnel that can accommodate a single lipid molecule with a flexible lid covering the tunnel entrance. The ORD can bind two membranes simultaneously. It has at least two membrane-binding surfaces; one near the mouth of the lipid-binding pocket and a distal site that can bind a second membrane. These structural features correlate with the phosphatidylinositol 4-phosphate (PI4P)-coupled lipid transport optimized in closely apposed membranes, such as organelle contact sites. The lipid transfer cycle starts from the association of the LTP with a donor membrane, which accompanies conformational changes that uncover the ligand-binding pocket. The tunnel opening is generally mediated by displacement of the lid covering the binding pocket allowing uptake or release of a lipid molecule. The LTPs extract the lipid from the membrane by providing a hydrophobic environment as well as specific interaction. Dissociation from the donor membrane shifts the conformation to a closed form. Then, the LTPs loaded with a cargo lipid diffuse through the aqueous phase. Lid opening may be induced by the interaction of a hydrophobic side of the lid with the target membranes.

Sequence similarities

Belongs to the OSBP family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    437
  • Mass (Da)
    49,805
  • Last updated
    1995-02-01 v1
  • Checksum
    1C972ED6517D529B
MALNKLKNIPSLTNSSHSSINGIASNAANSKPSGADTDDIDENDESGQSILLNIISQLKPGCDLSRITLPTFILEKKSMLERITNQLQFPDVLLEAHSNKDGLQRFVKVVAWYLAGWHIGPRAVKKPLNPILGEHFTAYWDLPNKQQAFYIAEQTSHHPPESAYFYMIPESNIRVDGVVVPKSKFLGNSSAAMMEGLTVLQFLDIKDANGKPEKYTLSQPNVYARGILFGKMRIELGDHMVIMGPKYQVDIEFKTKGFISGTYDAIEGTIKDYDGKEYYQISGKWNDIMYIKDLREKSSKKTVLFDTHQHFPLAPKVRPLEEQGEYESRRLWKKVTDALAVRDHEVATEEKFQIENRQRELAKKRAEDGVEFHSKLFRRAEPGEDLDYYIYKHIPEGTDKHEEQIRSILETAPILPGQTFTEKFSIPAYKKHGIQKN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U10555
EMBL· GenBank· DDBJ
AAB68425.1
EMBL· GenBank· DDBJ
Genomic DNA
AY692903
EMBL· GenBank· DDBJ
AAT92922.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006934
EMBL· GenBank· DDBJ
DAA06687.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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