A0A836KP25 · A0A836KP25_9TRYP

  • Protein
    Endoplasmic reticulum oxidoreductin
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    2/5

Function

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Features

Showing features for binding site, active site.

142950100150200250300350400
TypeIDPosition(s)Description
Binding site176FAD (UniProtKB | ChEBI)
Binding site187FAD (UniProtKB | ChEBI)
Binding site215FAD (UniProtKB | ChEBI)
Binding site218FAD (UniProtKB | ChEBI)
Binding site262FAD (UniProtKB | ChEBI)
Active site365Nucleophile
Active site368

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

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Endoplasmic reticulum oxidoreductin

Gene names

    • ORF names
      LSCM4_05694

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • LSCM4
  • Taxonomic lineage
    Eukaryota > Discoba > Euglenozoa > Kinetoplastea > Metakinetoplastina > Trypanosomatida > Trypanosomatidae > Leishmaniinae > Leishmania

Accessions

  • Primary accession
    A0A836KP25

Proteomes

Subcellular Location

Endoplasmic reticulum membrane
; Peripheral membrane protein

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

TypeIDPosition(s)Description
Signal1-24
ChainPRO_503232376225-429Endoplasmic reticulum oxidoreductin
Disulfide bond103↔110Redox-active
Disulfide bond365↔368Redox-active

Keywords

Interaction

Subunit

May function both as a monomer and a homodimer.

Family & Domains

Sequence similarities

Belongs to the EROs family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    429
  • Mass (Da)
    48,013
  • Last updated
    2021-09-29 v1
  • Checksum
    0A0BE47EC393D810
MNIEIGIKCIYTALLVLFLFFTHEAPKATTSSAAVLHNRTHPRIILNATKLDYGYCHSSPAEVDEGTESLLDVLNRITVSPYFRYFKVNSAKPCPYWAVSLLCTSAENTCNVCKCDENSIPEALRANEDMSELNTPDGSVTQSVLRPSNLDDWGDWLKADDGAEYVDLVSNPEGNTGYSGPLAAQVWRAIYAENCLSSDKDEACQEVSILKTLLSGLHMSINIHVCTSFYKDPELTSPQRNAGIYNNLNISFYPNCEMYNRRVAPFPDFVGNLYILYQFTLRALAKSKPSFTNDFNIFNTGARGEATLTDLELHENIKELFSSPLICYRTFDESAFLESEKGRALIPQFASVMLNVTRLMDCVTCEKCRIWGKLETKGIAVAMKVILNPKNEQITLDRSEMVTLVNLARQLAFSVRNAQRLGTVCKEEA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAFHLR010000016
EMBL· GenBank· DDBJ
KAG5482434.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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