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Protein

Protein transport protein SSS1

Gene

SSS1

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

Part of the Sec61 complex, which is the major component of channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). The functional states of the translocon complex include co- and post-translational ER import, cotranslational membrane protein integration and retrograde transport of misfolded proteins out of the ER. In the cotranslational pathway, ribosomes synthesizing presecretory proteins are targeted to the translocon by the cytosolic signal recognition particle (SRP) and its ER-localized receptor. The association of the Sec61 complex with the ribosome is mediated by the 28S rRNA of the large ribosomal subunit. SRP-independent post-translational translocation requires the association of additional factors, such as the Sec62/63 complex and KAR2. Also part of the Ssh1 complex, which probably is the major component of a channel-forming translocon complex that may function exclusively in the cotranslational pathway of protein ER import.

GO - Molecular functioni

  • P-P-bond-hydrolysis-driven protein transmembrane transporter activity Source: InterPro
  • protein transporter activity Source: SGD
  • structural molecule activity Source: SGD

GO - Biological processi

  • posttranslational protein targeting to membrane, translocation Source: SGD
  • SRP-dependent cotranslational protein targeting to membrane, translocation Source: SGD
Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-29691-MONOMER.
ReactomeiR-SCE-381038. XBP1(S) activates chaperone genes.

Protein family/group databases

TCDBi3.A.5.8.1. the general secretory pathway (sec) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein transport protein SSS1
Alternative name(s):
Sec61 complex subunit SSS1
Sec61 complex subunit gamma
Ssh1 complex subunit SSS1
Ssh1 complex subunit gamma
Gene namesi
Name:SSS1
Ordered Locus Names:YDR086C
ORF Names:D4475
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR086C.
SGDiS000002493. SSS1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4646CytoplasmicSequence analysisAdd
BLAST
Transmembranei47 – 7529HelicalSequence analysisAdd
BLAST
Topological domaini76 – 805ExtracellularSequence analysis

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • Sec61 translocon complex Source: SGD
  • Ssh1 translocon complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8080Protein transport protein SSS1PRO_0000104211Add
BLAST

Proteomic databases

MaxQBiP35179.
PeptideAtlasiP35179.
TopDownProteomicsiP35179.

PTM databases

iPTMnetiP35179.

Interactioni

Subunit structurei

Component of the heterotrimeric Sec61 complex, which is composed of SSH1, SBH1 and SSS1. Presumably three to four Sec61 heterotrimers assemble into an oligomeric ring with a central aqueous pore. In cotranslational ER import, the pore diameter varies from 9-15 A in a ribosome-free resting state to 40-60 A in a functional state when associated with the ribosome. The Sec61 complex is part of a channel-forming translocon complex whose composition seem to change dependent upon different functional states. During post-translational ER import the Sec61 complex associates with the Sec62/63 complex to form the Sec complex. SSH1 is a component of the heterotrimeric Ssh1 complex, which is composed of SSH1, SBH2 and SSS1. SSS1 interacts with OST1, OST4, SWP1 and WBP1, components of the OT complex.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
OST1P415432EBI-16406,EBI-12651
OST4Q993802EBI-16406,EBI-12689
SEC61P3291513EBI-16406,EBI-16400
SSH1P383538EBI-16406,EBI-18175
SWP1Q027952EBI-16406,EBI-12666
WBP1P337672EBI-16406,EBI-12658

Protein-protein interaction databases

BioGridi32142. 36 interactions.
DIPiDIP-2432N.
IntActiP35179. 16 interactions.
MINTiMINT-1357799.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WW9electron microscopy8.60B1-80[»]
2WWAelectron microscopy8.90B1-80[»]
ProteinModelPortaliP35179.
SMRiP35179. Positions 21-80.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35179.

Family & Domainsi

Sequence similaritiesi

Belongs to the SecE/SEC61-gamma family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000001319.
HOGENOMiHOG000194479.
InParanoidiP35179.
KOiK07342.
OMAiRQFAKDS.
OrthoDBiEOG718KRM.

Family and domain databases

Gene3Di1.20.5.820. 1 hit.
HAMAPiMF_00422. SecE.
InterProiIPR023391. Prot_translocase_SecE_dom.
IPR022943. SecE.
IPR008158. Translocase_Sec61-g.
IPR001901. Translocase_SecE/Sec61-g.
[Graphical view]
PfamiPF00584. SecE. 1 hit.
[Graphical view]
SUPFAMiSSF103456. SSF103456. 1 hit.
TIGRFAMsiTIGR00327. secE_euk_arch. 1 hit.
PROSITEiPS01067. SECE_SEC61G. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35179-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARASEKGEE KKQSNNQVEK LVEAPVEFVR EGTQFLAKCK KPDLKEYTKI
60 70 80
VKAVGIGFIA VGIIGYAIKL IHIPIRYVIV
Length:80
Mass (Da):8,944
Last modified:September 27, 2004 - v2
Checksum:i340F2EA913850D85
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti58 – 581F → L in CAA52608 (PubMed:8223425).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46796 Genomic DNA. Translation: CAA86808.1.
X74499 Genomic DNA. Translation: CAA52608.1.
X82086 Genomic DNA. Translation: CAA57615.1.
Z74382 Genomic DNA. Translation: CAA98906.1.
AY557659 Genomic DNA. Translation: AAS55985.1.
BK006938 Genomic DNA. Translation: DAA11933.1.
PIRiS48775.
RefSeqiNP_010371.1. NM_001180394.1.

Genome annotation databases

EnsemblFungiiYDR086C; YDR086C; YDR086C.
GeneIDi851659.
KEGGisce:YDR086C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46796 Genomic DNA. Translation: CAA86808.1.
X74499 Genomic DNA. Translation: CAA52608.1.
X82086 Genomic DNA. Translation: CAA57615.1.
Z74382 Genomic DNA. Translation: CAA98906.1.
AY557659 Genomic DNA. Translation: AAS55985.1.
BK006938 Genomic DNA. Translation: DAA11933.1.
PIRiS48775.
RefSeqiNP_010371.1. NM_001180394.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WW9electron microscopy8.60B1-80[»]
2WWAelectron microscopy8.90B1-80[»]
ProteinModelPortaliP35179.
SMRiP35179. Positions 21-80.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32142. 36 interactions.
DIPiDIP-2432N.
IntActiP35179. 16 interactions.
MINTiMINT-1357799.

Protein family/group databases

TCDBi3.A.5.8.1. the general secretory pathway (sec) family.

PTM databases

iPTMnetiP35179.

Proteomic databases

MaxQBiP35179.
PeptideAtlasiP35179.
TopDownProteomicsiP35179.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR086C; YDR086C; YDR086C.
GeneIDi851659.
KEGGisce:YDR086C.

Organism-specific databases

EuPathDBiFungiDB:YDR086C.
SGDiS000002493. SSS1.

Phylogenomic databases

GeneTreeiENSGT00390000001319.
HOGENOMiHOG000194479.
InParanoidiP35179.
KOiK07342.
OMAiRQFAKDS.
OrthoDBiEOG718KRM.

Enzyme and pathway databases

BioCyciYEAST:G3O-29691-MONOMER.
ReactomeiR-SCE-381038. XBP1(S) activates chaperone genes.

Miscellaneous databases

EvolutionaryTraceiP35179.
NextBioi969263.
PROiP35179.

Family and domain databases

Gene3Di1.20.5.820. 1 hit.
HAMAPiMF_00422. SecE.
InterProiIPR023391. Prot_translocase_SecE_dom.
IPR022943. SecE.
IPR008158. Translocase_Sec61-g.
IPR001901. Translocase_SecE/Sec61-g.
[Graphical view]
PfamiPF00584. SecE. 1 hit.
[Graphical view]
SUPFAMiSSF103456. SSF103456. 1 hit.
TIGRFAMsiTIGR00327. secE_euk_arch. 1 hit.
PROSITEiPS01067. SECE_SEC61G. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The yeast SSS1 gene is essential for secretory protein translocation and encodes a conserved protein of the endoplasmic reticulum."
    Esnault Y., Blondel M.-O., Deshaies R.J., Schekman R., Kepes F.
    EMBO J. 12:4083-4093(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    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. "Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation."
    Hanein D., Matlack K.E., Jungnickel B., Plath K., Kalies K.-U., Miller K.R., Rapoport T.A., Akey C.W.
    Cell 87:721-732(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: ELECTRON MICROSCOPY OF THE SEC61 COMPLEX.
  6. "The aqueous pore through the translocon has a diameter of 40-60 A during cotranslational protein translocation at the ER membrane."
    Hamman B.D., Chen J.C., Johnson E.E., Johnson A.E.
    Cell 89:535-544(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: TRANSLOCON COMPLEX PORE.
  7. "The translocon: a dynamic gateway at the ER membrane."
    Johnson A.E., van Waes M.A.
    Annu. Rev. Cell Dev. Biol. 15:799-842(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON THE TRANSLOCON COMPLEX.
  8. "Evolutionarily conserved binding of ribosomes to the translocation channel via the large ribosomal RNA."
    Prinz A., Behrens C., Rapoport T.A., Hartmann E., Kalies K.-U.
    EMBO J. 19:1900-1906(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION OF THE SEC61 COMPLEX WITH RIBOSOMES.
  9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  10. "Subunits of the translocon interact with components of the oligosaccharyl transferase complex."
    Chavan M., Yan A., Lennarz W.J.
    J. Biol. Chem. 280:22917-22924(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH OST1; OST4; SWP1 AND WBP1.

Entry informationi

Entry nameiSC61G_YEAST
AccessioniPrimary (citable) accession number: P35179
Secondary accession number(s): D6VS73
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: September 27, 2004
Last modified: May 11, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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 one 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.