G2WN38 · G2WN38_YEASK

Function

function

Cooperates with the reticulon proteins RTN1 and RTN2 and the tubule-shaping DP1 family protein YOP1 to generate and maintain the structure of the tubular endoplasmic reticulum network. Has GTPase activity, which is required for its function in ER organization.

Features

Showing features for binding site.

1776100200300400500600700
TypeIDPosition(s)Description
Binding site44-51GTP (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 FunctionGTP binding
Molecular FunctionGTPase activity
Biological Processendoplasmic reticulum organization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein SEY1
  • EC number
  • Alternative names
    • Synthetic enhancer of YOP1 protein

Gene names

    • Name
      K7_SEY1
    • Synonyms
      SEY1
    • ORF names
      SYK7_065511

Organism names

Accessions

  • Primary accession
    G2WN38

Proteomes

Subcellular Location

Endoplasmic reticulum membrane
; Multi-pass membrane protein
Note: Enriched in the cortical ER. Concentrated in punctae along the ER tubules.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-681Cytoplasmic
Transmembrane682-699Helical
Topological domain703-705Lumenal
Transmembrane706-726Helical
Topological domain727-776Cytoplasmic

Keywords

Interaction

Subunit

Interacts with RTN1 and YOP1; GTP binding is not required for these interactions.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain34-263GB1/RHD3-type G

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    776
  • Mass (Da)
    89,452
  • Last updated
    2011-11-16 v1
  • Checksum
    6C5BCBF2A48EA55E
MTDRSAIQLIDEEKEFHQSALQYFQQCIGNRDVGLDYHVISVFGSQSSGKSTLLNVLFNTNFDTMDAQVKRQQTTKGIWLAHTKQVNTTIEIDNDRPDIFVLDVEGSDGSERGEDQDFERKAALFAIAVSEVLIVNMWEQQIGLYQGNNMALLKTVFEVNLSLFGKNDNDHKVLLLFVIRDHVGVTPLSSLSDSVTRELEKIWTELSKPAGCEGSSLYDYFDLKFVGLAHKLLQEDKFTQDVKKLGDSFVMKGTENYYFKPQYHHRLPLDGWTMYAENCWDQIERNKDLDLPTQQILVARFKTEEISNEALEEFISKYDESIAPLKGNLGSLTSQLVKLKEECLTKYDEQASRYARNVYMEKREALNTKLNSHISGTINEFLESLMEKLWDDLKLEVSSRDKATTSFVESVAAGKSKIEKEFNESMETFKKLGLLISNEEITCKFSDDIEERIKQLRDAELKAKIGRIRKNLVPELKDHVIHLLSHPSKKVWDDIMNDFESTIKDNISAYQVEKDKYDFKIGLSESENAKIYKNIRILAWRTLDTTVHDYLKIDTIVSILRDRFEDVFKYDAEGSPRLWKTEEEIDGAFRVAKEHALEVFEVLSLAVTSDNVEIIPDVPMAEEESGEDNEIYRDNEGVFHSRRFAHILTELQKENVLDQFRRQINITVLDSKRSIITTRTHIPPWIYVLLAVLGWNEFVAVIRNPLFVTLTLILGATFFVIHKFGLWGPVVNVVQSAVGETRTAIKDKLRQFVVEDHEVKESFEMKDFSKNEQKEK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DG000051
EMBL· GenBank· DDBJ
GAA26481.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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