E9CXH2 · SEC11_COCPS

Function

function

Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity).
Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino acids (By similarity).

Catalytic activity

  • Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
    EC:3.4.21.89 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site.

121020406080100120140160180200
TypeIDPosition(s)Description
Active site53Charge relay system
Active site92Charge relay system
Active site152Charge relay system

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 Componentsignal peptidase complex
Molecular Functionserine-type endopeptidase activity
Biological Processsignal peptide processing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Signal peptidase complex catalytic subunit SEC11
  • EC number
  • Alternative names
    • Signal peptidase I

Gene names

    • Name
      SEC11
    • ORF names
      CPSG_02492

Organism names

Accessions

  • Primary accession
    E9CXH2

Proteomes

Organism-specific databases

Subcellular Location

Endoplasmic reticulum membrane
; Single-pass type II membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-21Cytoplasmic
Transmembrane22-38Helical; Signal-anchor for type II membrane protein
Topological domain39-210Lumenal

Keywords

PTM/Processing

Features

Showing features for chain, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00004123261-210Signal peptidase complex catalytic subunit SEC11
Glycosylation41N-linked (GlcNAc...) asparagine

Keywords

PTM databases

Interaction

Subunit

Component of the signal peptidase complex (SPC) composed of a catalytic subunit SEC11 and three accessory subunits SPC1, SPC2 and SPC3 (By similarity).
The complex induces a local thinning of the ER membrane which is used to measure the length of the signal peptide (SP) h-region of protein substrates. This ensures the selectivity of the complex towards h-regions shorter than 18-20 amino acids (By similarity).
SPC associates with the translocon complex (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region196-207C-terminal short (CTS) helix

Domain

The C-terminal short (CTS) helix is essential for catalytic activity. It may be accommodated as a transmembrane helix in the thinned membrane environment of the complex, similarly to the signal peptide in the complex substrates.

Sequence similarities

Belongs to the peptidase S26B family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    210
  • Mass (Da)
    23,125
  • Last updated
    2011-04-05 v1
  • Checksum
    B688B0924A390F12
MLAGLSPHLSNLRRSLTQVLNFALVLSTAFMMWKGLSIYTNSSSPIVVVLSGSMEPAFQRGDLLFLWNRSPRAEVGEIVVYNVRGKDIPIVHRVVRAFGDDEKSPKETNGQKKKKVMSSGKKDSIAAGALHSDSALVSHRILTKGDNNIADDTELYAQGQDYLDRKLDLVGSVRGYIPAVGYVTIMLSEHPWLKTVLLGIMGAMVILQRE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GL636488
EMBL· GenBank· DDBJ
EFW20649.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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