Q7YTU4 · ERO1_CAEEL

  • Protein
    Endoplasmic reticulum oxidoreductin-1
  • Gene
    ero-1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes pdi-1, the enzyme catalyzing protein disulfide formation, in order to allow pdi-1 to sustain additional rounds of disulfide formation. Following pdi reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell (By similarity).

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Features

Showing features for binding site.

147850100150200250300350400450
TypeIDPosition(s)Description
Binding site188FAD (UniProtKB | ChEBI)
Binding site190FAD (UniProtKB | ChEBI)
Binding site201FAD (UniProtKB | ChEBI)
Binding site241FAD (UniProtKB | ChEBI)
Binding site244FAD (UniProtKB | ChEBI)
Binding site283FAD (UniProtKB | ChEBI)
Binding site295FAD (UniProtKB | ChEBI)

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 Componentendoplasmic reticulum membrane
Molecular FunctionFAD binding
Molecular Functionprotein-disulfide reductase activity
Molecular Functionthiol oxidase activity
Biological Processprotein folding in endoplasmic reticulum
Biological Processresponse to endoplasmic reticulum stress

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Endoplasmic reticulum oxidoreductin-1
  • EC number

Gene names

    • Name
      ero-1
    • ORF names
      Y105E8B.8

Organism names

  • Taxonomic identifier
  • Strain
    • Bristol N2
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis

Accessions

  • Primary accession
    Q7YTU4
  • Secondary accessions
    • Q95Q33

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

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

TypeIDPosition(s)Description
Signal1-20
ChainPRO_000000842021-478Endoplasmic reticulum oxidoreductin-1
Disulfide bond28↔41
Disulfide bond30↔39
Disulfide bond79↔384
Disulfide bond88↔93Redox-active
Disulfide bond209↔230
Glycosylation377N-linked (GlcNAc...) asparagine
Disulfide bond387↔390Redox-active

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

May function both as a monomer and a homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region117-143Disordered
Region459-478Disordered

Sequence similarities

Belongs to the EROs family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 2 isoforms produced by Alternative splicing.

Q7YTU4-1

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.

  • Length
    478
  • Mass (Da)
    55,154
  • Last updated
    2004-07-19 v2
  • Checksum
    1AFDDF7976154ADE
MREPLLQLIVLSLIIIVVNTQFESGRLCFCKGFEAVEPCDCSKPQTIDKLNNHRIYEKVQKLLKKDFFRFYKVNMDKTCPFWADDRQCGTNQCGIAFCDDEVPAGLRRRNAVNMEAAAVKEEEDDDAEKCADAGNNIDPMDRTLHDDEKRQLDAMDHHDDGLEDKFCEIEDDESDGMHYVDLSKNPERYTGYAGKSPQRVWKSIYEENCFKPDPKFDKNFLTNPSNFGMCLEKRVFYRLISGLHSAITISIAAYNYKPPPPSLGQFGSQMGTWFRNTEMFAGRFGTKWSWEGPQRLRNVYFIYLLELRALLKAAPYLQNELFYTGNDVEDAETRKAVEDLLEEIRAYPNHFDESEMFTGVESHARALREEFRSHFVNISRIMDCVECDKCRLWGKVQTHGMGTALKILFSDLPHSHYKQDSSKFQLTRNEVVALLQSFGRYSSSILEVDNFREDMYPGESVMNTAADGPPRKSNKIDL

Q7YTU4-2

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

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
V6CLA8V6CLA8_CAEELero-1250
B7FAS8B7FAS8_CAEELero-1513

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_0360061-139in isoform b

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL132877
EMBL· GenBank· DDBJ
CAC70110.4
EMBL· GenBank· DDBJ
Genomic DNA
AL132877
EMBL· GenBank· DDBJ
CAD92388.2
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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