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Protein

Signal peptidase complex catalytic subunit SEC11

Gene

SEC11

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum.4 Publications

Catalytic activityi

Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei44 – 441By similarity

GO - Molecular functioni

  1. peptidase activity Source: SGD
  2. serine-type peptidase activity Source: InterPro

GO - Biological processi

  1. protein targeting to ER Source: SGD
  2. signal peptide processing Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease

Enzyme and pathway databases

BioCyciYEAST:YIR022W-MONOMER.

Protein family/group databases

MEROPSiS26.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal peptidase complex catalytic subunit SEC11 (EC:3.4.21.89)
Alternative name(s):
Secretory protein 11
Signal peptidase I
Gene namesi
Name:SEC11
Ordered Locus Names:YIR022W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IX

Organism-specific databases

CYGDiYIR022w.
SGDiS000001461. SEC11.

Subcellular locationi

Endoplasmic reticulum membrane 2 Publications; Single-pass type II membrane protein 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99CytoplasmicSequence Analysis
Transmembranei10 – 3122Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini32 – 167136LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: SGD
  2. integral component of membrane Source: UniProtKB-KW
  3. signal peptidase complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

Leads to accumulation of core-glycosylated glycoprotein precursors.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi44 – 441S → A or C: Nonviable. 1 Publication
Mutagenesisi83 – 831H → A or K: Nonviable; no protein expressed. 1 Publication
Mutagenesisi83 – 831H → F: Nonviable. 1 Publication
Mutagenesisi103 – 1031D → E: Nonviable; no protein expressed. 1 Publication
Mutagenesisi103 – 1031D → N: Nonviable. 1 Publication
Mutagenesisi109 – 1091D → E: Nonviable. 1 Publication
Mutagenesisi109 – 1091D → N: Nonviable; no protein expressed. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 167167Signal peptidase complex catalytic subunit SEC11PRO_0000109540Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi121 – 1211N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP15367.
PaxDbiP15367.

Expressioni

Gene expression databases

GenevestigatoriP15367.

Interactioni

Subunit structurei

Component of the signal peptidase complex (SPC), which consists of SPC1, SPC2, SPC3 and SEC11. SPC associates with the translocon complex.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SPC1P469654EBI-16513,EBI-17823
SPC3Q121333EBI-16513,EBI-17829

Protein-protein interaction databases

BioGridi35013. 107 interactions.
DIPiDIP-5667N.
IntActiP15367. 4 interactions.
MINTiMINT-486420.
STRINGi4932.YIR022W.

Structurei

3D structure databases

ProteinModelPortaliP15367.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S26B family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0681.
GeneTreeiENSGT00390000015600.
HOGENOMiHOG000111516.
InParanoidiP15367.
KOiK13280.
OMAiWKGISVI.
OrthoDBiEOG7BCNQ4.

Family and domain databases

InterProiIPR019758. Pept_S26A_signal_pept_1_CS.
IPR019756. Pept_S26A_signal_pept_1_Ser-AS.
IPR019759. Peptidase_S24_S26.
IPR015927. Peptidase_S24_S26A/B/C.
IPR001733. Peptidase_S26B.
[Graphical view]
PANTHERiPTHR10806. PTHR10806. 1 hit.
PfamiPF00717. Peptidase_S24. 1 hit.
[Graphical view]
PRINTSiPR00728. SIGNALPTASE.
SUPFAMiSSF51306. SSF51306. 1 hit.
TIGRFAMsiTIGR02228. sigpep_I_arch. 1 hit.
PROSITEiPS00501. SPASE_I_1. 1 hit.
PS00761. SPASE_I_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P15367-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLRFELQKL LNVCFLFASA YMFWQGLAIA TNSASPIVVV LSGSMEPAFQ
60 70 80 90 100
RGDILFLWNR NTFNQVGDVV VYEVEGKQIP IVHRVLRQHN NHADKQFLLT
110 120 130 140 150
KGDNNAGNDI SLYANKKIYL NKSKEIVGTV KGYFPQLGYI TIWISENKYA
160
KFALLGMLGL SALLGGE
Length:167
Mass (Da):18,762
Last modified:February 1, 1995 - v2
Checksum:iFC877232D6888DF3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti162 – 1621A → R in CAA30533 (PubMed:3283143).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07694 Genomic DNA. Translation: CAA30533.1.
Z38061 Genomic DNA. Translation: CAA86182.1.
AY558239 Genomic DNA. Translation: AAS56565.1.
BK006942 Genomic DNA. Translation: DAA08569.1.
PIRiS48484.
RefSeqiNP_012288.1. NM_001179544.1.

Genome annotation databases

EnsemblFungiiYIR022W; YIR022W; YIR022W.
GeneIDi854840.
KEGGisce:YIR022W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07694 Genomic DNA. Translation: CAA30533.1.
Z38061 Genomic DNA. Translation: CAA86182.1.
AY558239 Genomic DNA. Translation: AAS56565.1.
BK006942 Genomic DNA. Translation: DAA08569.1.
PIRiS48484.
RefSeqiNP_012288.1. NM_001179544.1.

3D structure databases

ProteinModelPortaliP15367.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35013. 107 interactions.
DIPiDIP-5667N.
IntActiP15367. 4 interactions.
MINTiMINT-486420.
STRINGi4932.YIR022W.

Protein family/group databases

MEROPSiS26.010.

Proteomic databases

MaxQBiP15367.
PaxDbiP15367.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYIR022W; YIR022W; YIR022W.
GeneIDi854840.
KEGGisce:YIR022W.

Organism-specific databases

CYGDiYIR022w.
SGDiS000001461. SEC11.

Phylogenomic databases

eggNOGiCOG0681.
GeneTreeiENSGT00390000015600.
HOGENOMiHOG000111516.
InParanoidiP15367.
KOiK13280.
OMAiWKGISVI.
OrthoDBiEOG7BCNQ4.

Enzyme and pathway databases

BioCyciYEAST:YIR022W-MONOMER.

Miscellaneous databases

NextBioi977719.

Gene expression databases

GenevestigatoriP15367.

Family and domain databases

InterProiIPR019758. Pept_S26A_signal_pept_1_CS.
IPR019756. Pept_S26A_signal_pept_1_Ser-AS.
IPR019759. Peptidase_S24_S26.
IPR015927. Peptidase_S24_S26A/B/C.
IPR001733. Peptidase_S26B.
[Graphical view]
PANTHERiPTHR10806. PTHR10806. 1 hit.
PfamiPF00717. Peptidase_S24. 1 hit.
[Graphical view]
PRINTSiPR00728. SIGNALPTASE.
SUPFAMiSSF51306. SSF51306. 1 hit.
TIGRFAMsiTIGR02228. sigpep_I_arch. 1 hit.
PROSITEiPS00501. SPASE_I_1. 1 hit.
PS00761. SPASE_I_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "SEC11 is required for signal peptide processing and yeast cell growth."
    Boehni P.C., Deshaies R.J., Schekman R.W.
    J. Cell Biol. 106:1035-1042(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE.
    Strain: PBY408A.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Solubilization and characterization of yeast signal peptidase."
    YaDeau J.T., Blobel G.
    J. Biol. Chem. 264:2928-2934(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. "Yeast signal peptidase contains a glycoprotein and the Sec11 gene product."
    YaDeau J.T., Klein C., Blobel G.
    Proc. Natl. Acad. Sci. U.S.A. 88:517-521(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SIGNAL PEPTIDASE COMPLEX.
  7. "A mutation affecting signal peptidase inhibits degradation of an abnormal membrane protein in Saccharomyces cerevisiae."
    Mullins C., Lu Y., Campbell A., Fang H., Green N.
    J. Biol. Chem. 270:17139-17147(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "The yeast SPC22/23 homolog Spc3p is essential for signal peptidase activity."
    Meyer H.A., Hartmann E.
    J. Biol. Chem. 272:13159-13164(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SIGNAL PEPTIDASE COMPLEX.
  9. "The catalytic mechanism of endoplasmic reticulum signal peptidase appears to be distinct from most eubacterial signal peptidases."
    VanValkenburgh C., Chen X., Mullins C., Fang H., Green N.
    J. Biol. Chem. 274:11519-11525(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF SER-44; HIS-83; ASP-103 AND ASP-109.
  10. "Signal peptidase and oligosaccharyltransferase interact in a sequential and dependent manner within the endoplasmic reticulum."
    Chen X., VanValkenburgh C., Liang H., Fang H., Green N.
    J. Biol. Chem. 276:2411-2416(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSEC11_YEAST
AccessioniPrimary (citable) accession number: P15367
Secondary accession number(s): D6VVV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: February 1, 1995
Last modified: January 7, 2015
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3150 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.