Q91XL9 · OSBL1_MOUSE

  • Protein
    Oxysterol-binding protein-related protein 1
  • Gene
    Osbpl1a
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

Binds phospholipids; exhibits strong binding to phosphatidic acid and weak binding to phosphatidylinositol 3-phosphate. Stabilizes GTP-bound RAB7A on late endosomes/lysosomes and alters functional properties of late endocytic compartments via its interaction with RAB7A. Binds 25-hydroxycholesterol and cholesterol.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentlate endosome
Cellular Componentorganelle membrane contact site
Molecular Functionlipid binding
Biological Processlipid transport

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Oxysterol-binding protein-related protein 1
  • Short names
    ORP-1; OSBP-related protein 1

Gene names

    • Name
      Osbpl1a
    • Synonyms
      Orp1, Orp1a, Orp1l

Organism names

  • Taxonomic identifier
  • Strains
    • BALB/cJ
    • C57BL/6J
    • OF1
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q91XL9
  • Secondary accessions
    • O88318
    • Q3TH97
    • Q673L8
    • Q6DFU6

Proteomes

Organism-specific databases

Subcellular Location

Late endosome
Note: Colocalizes with RAB7A, RAB9A and LAMP1 in late endosomes.

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00001003681-950Oxysterol-binding protein-related protein 1
Modified residue499Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Ubiquitous.

Gene expression databases

Interaction

Subunit

Interacts (via FFAT motif) with VAPA and VAPB (By similarity).
Interacts with the GTP-bound form of RAB7A (By similarity).
Interacts with OAS1B (PubMed:22623793).
Interacts (via FFAT motif) with MOSPD2 (via MSP domain) (By similarity).

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, repeat, domain, coiled coil, motif, compositional bias.

Type
IDPosition(s)Description
Region1-237Interaction with RAB7A
Repeat47-76ANK 1
Repeat80-109ANK 2
Repeat175-204ANK 3
Domain235-334PH
Coiled coil430-463
Motif469-483FFAT
Region502-530Disordered
Compositional bias505-519Basic and acidic residues
Compositional bias795-809Basic and acidic residues
Region795-821Disordered
Coiled coil879-913

Domain

The FFAT motif is required for interaction with MOSPD2.
The FFAT motif is required for interaction with MOSPD2, VAPA and VAPB.

Sequence similarities

Belongs to the OSBP family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

Q91XL9-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Name
    1
  • Synonyms
    Osbpl1b
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    950
  • Mass (Da)
    107,795
  • Last updated
    2006-03-21 v2
  • Checksum
    AA4F5678999B0EB5
MNTEAEQQLLHHARNGNAEEVRKLLAAMARMEVVADIDCKGRSKSNLGWTPLHLACYFGHKQVVEDLLKAGAKVNMLNDMGDTPLHRAAFTGRKELVLLLLEYDADSTVVNGSGQTAKEATHDKEIRNMLEAVERTQQRKLEELLLGAAREGRTAEVSALLSRPNPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLAQGAEMKHILVGNKVVHKALKRYEGPLWKSSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYRQGCKHLTQAVCTVKPTDSCLFSIRCFDDTVHCFRVPKNSVQQSREKWLEAIEEHSAYSTHYCSQDQVTDDEEEDVVSAMDLKESLARAQTCQQRLDREIYNFLKMIKECDVAKDMLPSFLQKADIVSEASRETCVALNDCLNLFTKQEGVRNFKLEQEQEKNKILSEALETLATEHHELERSLVEGSPPVSILSEEEFYDALSGSESEGSLTCLEAVTAHSFEENEVPGSSGKHRMSEGKDCGGGDALSNGIKKHRTSLPSPMFSRNDFSIWSILRKCIGMELSKITMPVIFNEPLSFLQRLTEYMEHTYLIHKASSLSDPVERMQCVAAFAVSAVASQWERTGKPFNPLLGETYELVRDDLGFRLISEQVSHHPPISAFHAEGLNNDFIFHGSIYPKLKFWGKSVEAEPKGTITLELLDHNEAYTWTNPTCCVHNIIVGKLWIEQYGNVEIINHKTGDKCVLNFKPCGLFGKELHKVEGYIQDKSKKKLCALYGKWTECLYSVDPATFDAYKKNDKKNTEEKKNSKQTSSSEESDEMPVPDSESVFIIPGSVLLWRIAPRPPNSAQMYNFTSFAMVLNEVDKEMESVIPKTDCRLRPDIRAMENGEIDLASEEKKRLEEKQRAARKNRSKSEEDWKTRWFHQGPNPYSGAQDWIYSGSYWDRNYFNLPDIY

Q91XL9-2

  • Name
    2
  • Synonyms
    Osbpl1a
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q91XL9-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 11 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
Q8K2D2Q8K2D2_MOUSEOsbpl1a338
A0A3Q4L372A0A3Q4L372_MOUSEOsbpl1a37
A0A3Q4L2S6A0A3Q4L2S6_MOUSEOsbpl1a200
A0A3Q4EG54A0A3Q4EG54_MOUSEOsbpl1a528
A0A3Q4EG41A0A3Q4EG41_MOUSEOsbpl1a51
D3YZ66D3YZ66_MOUSEOsbpl1a187
D3Z754D3Z754_MOUSEOsbpl1a281
Q3V156Q3V156_MOUSEOsbpl1a558
D3Z7I9D3Z7I9_MOUSEOsbpl1a184
D6RDE4D6RDE4_MOUSEOsbpl1a66
A0A3Q4EI24A0A3Q4EI24_MOUSEOsbpl1a547

Features

Showing features for alternative sequence, compositional bias, sequence conflict.

Type
IDPosition(s)Description
Alternative sequenceVSP_0177241-513in isoform 2
Alternative sequenceVSP_0177231-540in isoform 3
Compositional bias505-519Basic and acidic residues
Sequence conflict572in Ref. 5; AAH76637
Sequence conflict599in Ref. 3; BAA33012
Sequence conflict685in Ref. 1; AAK71661
Sequence conflict697-698in Ref. 1; AAK71661
Sequence conflict713in Ref. 1; AAK71661
Sequence conflict732in Ref. 1; AAK71661
Sequence conflict744in Ref. 1; AAK71661
Sequence conflict759in Ref. 1; AAK71661
Compositional bias795-809Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF394063
EMBL· GenBank· DDBJ
AAK71661.2
EMBL· GenBank· DDBJ
mRNA
AY536214
EMBL· GenBank· DDBJ
AAT06024.1
EMBL· GenBank· DDBJ
mRNA
AB017026
EMBL· GenBank· DDBJ
BAA33012.1
EMBL· GenBank· DDBJ
mRNA
AK168366
EMBL· GenBank· DDBJ
BAE40301.1
EMBL· GenBank· DDBJ
mRNA
BC076637
EMBL· GenBank· DDBJ
AAH76637.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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