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P46965 (SPC1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 subunit SPC1
Alternative name(s):
Microsomal signal peptidase subunit 1
Gene names
Name:SPC1
Ordered Locus Names:YJR010C-A
ORF Names:YJR010BW
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length94 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Nonessential 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. SPC3 is not required for signal peptidase activity. Ref.1

Subunit structure

Component of the signal peptidase complex (SPC), which consists of SPC1, SPC2, SPC3 and SEC11. SPC associates with the translocon complex. SPC1 interacts with SBH1 and SEB2. Ref.5 Ref.6

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Miscellaneous

Present with 5550 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the SPCS1 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SEC11P153674EBI-17823,EBI-16513

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 9493Signal peptidase complex subunit SPC1
PRO_0000215162

Regions

Topological domain2 – 2827Cytoplasmic Potential
Transmembrane29 – 4921Helical; Potential
Topological domain501Lumenal Potential
Transmembrane51 – 7121Helical; Potential
Topological domain72 – 9423Cytoplasmic Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.8

Sequences

Sequence LengthMass (Da)Tools
P46965 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 814D7C7A49F49D6D

FASTA9410,819
        10         20         30         40         50         60 
MSEILQDVQR KLVFPIDFPS QRKTEKFQQL SLMIGALVAC ILGFAQQSLK VLLTAYGISC 

        70         80         90 
VITLICVLPA YPWYNKQKLR WAQPKIEINV DQYD 

« Hide

References

« Hide 'large scale' references
[1]"The homologue of mammalian SPC12 is important for efficient signal peptidase activity in Saccharomyces cerevisiae."
Fang H., Panzner S., Mullins C., Hartmann E., Green N.
J. Biol. Chem. 271:16460-16465(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: AB320 / ATCC 37323.
[2]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. expand/collapse author list , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
EMBO J. 15:2031-2049(1996) [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]"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.
[6]"Interactions between Spc2p and other components of the endoplasmic reticulum translocation sites of the yeast Saccharomyces cerevisiae."
Antonin W., Meyer H.A., Hartmann E.
J. Biol. Chem. 275:34068-34072(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SBH1 AND SEB2.
[7]"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].
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U26257 Genomic DNA. Translation: AAC49366.1.
Z49510 Genomic DNA. Translation: CAA89533.1.
Z49511 Genomic DNA. Translation: CAA89535.1.
AY557861 Genomic DNA. Translation: AAS56187.1.
BK006943 Genomic DNA. Translation: DAA08802.1.
PIRS61934.
RefSeqNP_012544.1. NM_001181667.1.

3D structure databases

ProteinModelPortalP46965.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33767. 88 interactions.
DIPDIP-2770N.
IntActP46965. 17 interactions.
MINTMINT-482750.
STRING4932.YJR010C-A.

Proteomic databases

PaxDbP46965.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYJR010C-A; YJR010C-A; YJR010C-A.
GeneID853467.
KEGGsce:YJR010C-A.

Organism-specific databases

CYGDYJR010c-a.
SGDS000003770. SPC1.

Phylogenomic databases

eggNOGNOG267017.
HOGENOMHOG000000815.
KOK12946.
OMAGISCVIT.
OrthoDBEOG74R240.

Enzyme and pathway databases

BioCycYEAST:G3O-31655-MONOMER.

Gene expression databases

GenevestigatorP46965.

Family and domain databases

InterProIPR009542. SPC12.
[Graphical view]
PANTHERPTHR13202. PTHR13202. 1 hit.
PfamPF06645. SPC12. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio974059.
PROP46965.

Entry information

Entry nameSPC1_YEAST
AccessionPrimary (citable) accession number: P46965
Secondary accession number(s): D6VWI6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: March 19, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome X

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

Yeast

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

SIMILARITY comments

Index of protein domains and families