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P15367 (SEC11_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Signal peptidase complex catalytic subunit SEC11

EC=3.4.21.89
Alternative name(s):
Secretory protein 11
Signal peptidase I
Gene names
Name:SEC11
Ordered Locus Names:YIR022W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length167 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.7 Ref.9 Ref.10

Catalytic activity

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

Subunit structure

Component of the signal peptidase complex (SPC), which consists of SPC1, SPC2, SPC3 and SEC11. SPC associates with the translocon complex. Ref.6 Ref.8

Subcellular location

Endoplasmic reticulum membrane; Single-pass type II membrane protein Ref.5 Ref.11.

Disruption phenotype

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

Miscellaneous

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

Sequence similarities

Belongs to the peptidase S26B family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SPC1P469654EBI-16513,EBI-17823
SPC3Q121333EBI-16513,EBI-17829

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 167167Signal peptidase complex catalytic subunit SEC11
PRO_0000109540

Regions

Topological domain1 – 99Cytoplasmic Potential
Transmembrane10 – 3122Helical; Signal-anchor for type II membrane protein; Potential
Topological domain32 – 167136Lumenal Potential

Sites

Active site441 By similarity

Amino acid modifications

Glycosylation1211N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis441S → A or C: Nonviable. Ref.9
Mutagenesis831H → A or K: Nonviable; no protein expressed. Ref.9
Mutagenesis831H → F: Nonviable. Ref.9
Mutagenesis1031D → E: Nonviable; no protein expressed. Ref.9
Mutagenesis1031D → N: Nonviable. Ref.9
Mutagenesis1091D → E: Nonviable. Ref.9
Mutagenesis1091D → N: Nonviable; no protein expressed. Ref.9
Sequence conflict1621A → R in CAA30533. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P15367 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: FC877232D6888DF3

FASTA16718,762
        10         20         30         40         50         60 
MNLRFELQKL LNVCFLFASA YMFWQGLAIA TNSASPIVVV LSGSMEPAFQ RGDILFLWNR 

        70         80         90        100        110        120 
NTFNQVGDVV VYEVEGKQIP IVHRVLRQHN NHADKQFLLT KGDNNAGNDI SLYANKKIYL 

       130        140        150        160 
NKSKEIVGTV KGYFPQLGYI TIWISENKYA KFALLGMLGL SALLGGE 

« Hide

References

« Hide 'large scale' references
[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]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. expand/collapse author list , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[12]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X07694 Genomic DNA. Translation: CAA30533.1.
Z38061 Genomic DNA. Translation: CAA86182.1.
AY558239 Genomic DNA. Translation: AAS56565.1.
BK006942 Genomic DNA. Translation: DAA08569.1.
PIRS48484.
RefSeqNP_012288.1. NM_001179544.1.

3D structure databases

ProteinModelPortalP15367.
SMRP15367. Positions 34-136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35013. 107 interactions.
DIPDIP-5667N.
IntActP15367. 4 interactions.
MINTMINT-486420.
STRING4932.YIR022W.

Protein family/group databases

MEROPSS26.010.

Proteomic databases

PaxDbP15367.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYIR022W; YIR022W; YIR022W.
GeneID854840.
KEGGsce:YIR022W.

Organism-specific databases

CYGDYIR022w.
SGDS000001461. SEC11.

Phylogenomic databases

eggNOGCOG0681.
GeneTreeENSGT00390000015600.
HOGENOMHOG000111516.
KOK13280.
OMATILISEN.
OrthoDBEOG7BCNQ4.

Enzyme and pathway databases

BioCycYEAST:YIR022W-MONOMER.

Gene expression databases

GenevestigatorP15367.

Family and domain databases

InterProIPR019758. 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]
PANTHERPTHR10806. PTHR10806. 1 hit.
PfamPF00717. Peptidase_S24. 1 hit.
[Graphical view]
PRINTSPR00728. SIGNALPTASE.
SUPFAMSSF51306. SSF51306. 1 hit.
TIGRFAMsTIGR02228. sigpep_I_arch. 1 hit.
PROSITEPS00501. SPASE_I_1. 1 hit.
PS00761. SPASE_I_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio977719.

Entry information

Entry nameSEC11_YEAST
AccessionPrimary (citable) accession number: P15367
Secondary accession number(s): D6VVV3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IX

Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries