Q67WM9 · OS9_ORYSJ

Function

function

Lectin which functions in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). May bind terminally misfolded non-glycosylated proteins as well as improperly folded glycoproteins, retain them in the ER, and possibly transfer them to the ubiquitination machinery and promote their degradation.

Features

Showing features for binding site.

129820406080100120140160180200220240260280
TypeIDPosition(s)Description
Binding site130a mannooligosaccharide derivative (UniProtKB | ChEBI)
Binding site131a mannooligosaccharide derivative (UniProtKB | ChEBI)
Binding site143a mannooligosaccharide derivative (UniProtKB | ChEBI)
Binding site202a mannooligosaccharide derivative (UniProtKB | ChEBI)
Binding site208a mannooligosaccharide derivative (UniProtKB | ChEBI)
Binding site228a mannooligosaccharide derivative (UniProtKB | ChEBI)
Binding site234a mannooligosaccharide derivative (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentendoplasmic reticulum lumen
Molecular Functioncarbohydrate binding
Biological Processendoplasmic reticulum unfolded protein response
Biological Processresponse to salt stress
Biological Processretrograde protein transport, ER to cytosol

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Protein OS-9 homolog
  • Short names
    OsOS9

Gene names

    • Name
      OS9
    • ORF names
      OsJ_22141
      , P0017B12.18-1
    • Ordered locus names
      Os06g0644800
      , LOC_Os06g43710

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Nipponbare
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa

Accessions

  • Primary accession
    Q67WM9
  • Secondary accessions
    • A0A0P0WZD9

Proteomes

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond.

TypeIDPosition(s)Description
Signal1-25
ChainPRO_000043127726-298Protein OS-9 homolog
Glycosylation95N-linked (GlcNAc...) asparagine
Disulfide bond123↔136
Glycosylation171N-linked (GlcNAc...) asparagine
Glycosylation197N-linked (GlcNAc...) asparagine
Disulfide bond201↔232
Disulfide bond216↔244

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Interacts with HRD3.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain121-246MRH

Sequence similarities

Belongs to the OS-9 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    298
  • Mass (Da)
    33,439
  • Last updated
    2004-10-11 v1
  • Checksum
    73B0E5B070415475
MGLAGGARVVLFVVAAAAAAALTAAADQIFTSSGAPFGRNSREPRYHVEFHPVDAPFNPENGQESVPMTSHVGKHYTCFLPVEETKTMKSIIPQNATNVIIESERRVKPKDPDELLEILKDQCFYRHEGWWSYEFCYYGKIRQVHVEGEKVIQEYVLGEYDADATDAYYENQTSDSADEDDNLIDTSKRYHVHLYTNGTVCDLTDMPRETEVRFVCSEPTVVISSIKEISSCKYVLTVQSPMLCKNPLFQQEKRTLSIHCNELLAEAEATVDDDSLPKEAQIIIPDPDGLHNYAAYAT

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0P0WZ99A0A0P0WZ99_ORYSJOs06g0644800174

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP003568
EMBL· GenBank· DDBJ
BAD37440.1
EMBL· GenBank· DDBJ
Genomic DNA
AP008212
EMBL· GenBank· DDBJ
BAH93656.1
EMBL· GenBank· DDBJ
Genomic DNA
AP014962
EMBL· GenBank· DDBJ
BAS98847.1
EMBL· GenBank· DDBJ
Genomic DNA
CM000143
EMBL· GenBank· DDBJ
EAZ37805.1
EMBL· GenBank· DDBJ
Genomic DNA
AK109442
EMBL· GenBank· DDBJ
BAG98751.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp