SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P15367

- SEC11_YEAST

UniProt

P15367 - SEC11_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Signal peptidase complex catalytic subunit SEC11
Gene
SEC11, YIR022W
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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 – 441 By similarity

GO - Molecular functioni

  1. peptidase activity Source: SGD
  2. protein binding Source: IntAct
  3. 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; Single-pass type II membrane protein 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99Cytoplasmic Reviewed prediction
Transmembranei10 – 3122Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini32 – 167136Lumenal Reviewed prediction
Add
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 SEC11
PRO_0000109540Add
BLAST

Amino acid modifications

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

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.
SMRiP15367. Positions 34-136.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S26B family.

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0681.
GeneTreeiENSGT00390000015600.
HOGENOMiHOG000111516.
KOiK13280.
OMAiTKGDNNM.
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

MNLRFELQKL LNVCFLFASA YMFWQGLAIA TNSASPIVVV LSGSMEPAFQ    50
RGDILFLWNR NTFNQVGDVV VYEVEGKQIP IVHRVLRQHN NHADKQFLLT 100
KGDNNAGNDI SLYANKKIYL NKSKEIVGTV KGYFPQLGYI TIWISENKYA 150
KFALLGMLGL SALLGGE 167
Length:167
Mass (Da):18,762
Last modified:February 1, 1995 - v2
Checksum:iFC877232D6888DF3
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti162 – 1621A → R in CAA30533. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi S48484.
RefSeqi NP_012288.1. NM_001179544.1.

3D structure databases

ProteinModelPortali P15367.
SMRi P15367. Positions 34-136.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 35013. 107 interactions.
DIPi DIP-5667N.
IntActi P15367. 4 interactions.
MINTi MINT-486420.
STRINGi 4932.YIR022W.

Protein family/group databases

MEROPSi S26.010.

Proteomic databases

MaxQBi P15367.
PaxDbi P15367.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YIR022W ; YIR022W ; YIR022W .
GeneIDi 854840.
KEGGi sce:YIR022W.

Organism-specific databases

CYGDi YIR022w.
SGDi S000001461. SEC11.

Phylogenomic databases

eggNOGi COG0681.
GeneTreei ENSGT00390000015600.
HOGENOMi HOG000111516.
KOi K13280.
OMAi TKGDNNM.
OrthoDBi EOG7BCNQ4.

Enzyme and pathway databases

BioCyci YEAST:YIR022W-MONOMER.

Miscellaneous databases

NextBioi 977719.

Gene expression databases

Genevestigatori P15367.

Family and domain databases

InterProi IPR019758. 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 ]
PANTHERi PTHR10806. PTHR10806. 1 hit.
Pfami PF00717. Peptidase_S24. 1 hit.
[Graphical view ]
PRINTSi PR00728. SIGNALPTASE.
SUPFAMi SSF51306. SSF51306. 1 hit.
TIGRFAMsi TIGR02228. sigpep_I_arch. 1 hit.
PROSITEi PS00501. SPASE_I_1. 1 hit.
PS00761. SPASE_I_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 135 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.

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