Protein transport protein SEC61 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P32915 (SC61A_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 118. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Protein transport protein SEC61

Alternative name(s):
Sec61 complex subunit SEC61
Sec61 complex subunit alpha

Gene names

Name:	SEC61
Ordered Locus Names:	YLR378C
ORF Names:	L3502.5

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	480 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Part of the Sec61 complex, which is the major component of a 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. In an initial step, the signal sequence seems to bind simultaneously to SEC61 and SEC62. A cycle of assembly and disassembly of Sec62/63 complex from SEC61 may govern the activity of the translocon. SEC61 mediates the association with the ribosome.
Subunit structure	Component of the heterotrimeric Sec61 complex, which is composed of SEC61, SBH1 and SSS1. Presumably three to four Sec61 heterotrimers assemble into an oligomeric ring with a central aeqeous 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. SEC61 interacts with STT3, OST1, OST2, OST4, SWP1 AND WBP1 components of the OT complex. Ref.11
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein.
Miscellaneous	Present with 24800 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the SecY/SEC61-alpha family.

Ontologies

Keywords
Biological process	Protein transport Translocation Transport
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ER-associated protein catabolic process Inferred from physical interaction PubMed 19696741. Source: SGD SRP-dependent cotranslational protein targeting to membrane, translocation Inferred from direct assay PubMed 11076036. Source: SGD posttranslational protein targeting to membrane, translocation Inferred from direct assay PubMed 7758110 PubMed 9252322. Source: SGD retrograde protein transport, ER to cytosol Inferred from mutant phenotype PubMed 10635318 PubMed 9303298. Source: SGD
Cellular_component	Sec61 translocon complex Inferred from direct assay PubMed 8612571 PubMed 9252322. Source: SGD integral to membrane Inferred from sequence model PubMed 12192589. Source: SGD
Molecular_function	P-P-bond-hydrolysis-driven protein transmembrane transporter activity Inferred from direct assay PubMed 9252322. Source: SGD peptide transporter activity Inferred from mutant phenotype PubMed 10758167. Source: SGD signal sequence binding Inferred from direct assay PubMed 12134063. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
OST2	P46964	2	EBI-16400,EBI-12673
OST4	Q99380	2	EBI-16400,EBI-12689
SEC62	P21825	3	EBI-16400,EBI-16632
SSS1	P35179	7	EBI-16400,EBI-16406
STT3	P39007	2	EBI-16400,EBI-18447
SWP1	Q02795	3	EBI-16400,EBI-12666
WBP1	P33767	2	EBI-16400,EBI-12658

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 480

480

Protein transport protein SEC61

PRO_0000131789

Regions

Topological domain

1 – 32

Cytoplasmic Probable

Transmembrane

33 – 55

Helical; Name=1; Probable

Topological domain

56 – 75

Lumenal Probable

Transmembrane

76 – 95

Helical; Name=2; Probable

Topological domain

96 – 119

Cytoplasmic Probable

Transmembrane

120 – 141

Helical; Name=3; Probable

Topological domain

142 – 146

Lumenal Probable

Transmembrane

147 – 167

Helical; Name=4; Probable

Topological domain

168 – 212

Cytoplasmic Probable

Transmembrane

213 – 224

Helical; Name=5; Probable

Topological domain

225 – 240

Lumenal Probable

Transmembrane

241 – 260

Helical; Name=6; Probable

Topological domain

261 – 290

Cytoplasmic Probable

Transmembrane

291 – 311

Helical; Name=7; Probable

Topological domain

312 – 361

Lumenal Probable

Transmembrane

362 – 381

Helical; Name=8; Probable

Topological domain

382 – 416

Cytoplasmic Probable

Transmembrane

417 – 434

Helical; Name=9; Probable

Topological domain

435 – 437

Lumenal Probable

Transmembrane

438 – 459

Helical; Name=10; Probable

Topological domain

460 – 480

Cytoplasmic Probable

Experimental info

Mutagenesis

273

K → P or G: Severe growth defect. Ref.12

Mutagenesis

275

R → D, G, P, Q or Y: Severe growth defect. Ref.12

Mutagenesis

275

R → E, F or V: Severe growth defect; lowers SRP-dependent and SRP-independent translocation. Ref.12

Mutagenesis

276

G → P: Severe growth defect. Ref.12

Mutagenesis

405

K → D, E or P: Severe growth defect. Ref.12

Mutagenesis

406

R → D: Severe growth defect; lowers SRP-dependent translocation. Ref.12

Mutagenesis

406

R → E: Severe growth defect; lowers SRP-dependent and SRP-independent translocation. Ref.12

Mutagenesis

406

R → H or W: Severe growth defect. Ref.12

Sequences

Sequence

Length

Mass (Da)

Tools

P32915 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: AB34F12FB7B3CBD4
Show »

FASTA

480

52,937

        10         20         30         40         50         60 
MSSNRVLDLF KPFESFLPEV IAPERKVPYN QKLIWTGVSL LIFLILGQIP LYGIVSSETS 

        70         80         90        100        110        120 
DPLYWLRAML ASNRGTLLEL GVSPIITSSM IFQFLQGTQL LQIRPESKQD RELFQIAQKV 

       130        140        150        160        170        180 
CAIILILGQA LVVVMTGNYG APSDLGLPIC LLLIFQLMFA SLIVMLLDEL LSKGYGLGSG 

       190        200        210        220        230        240 
ISLFTATNIA EQIFWRAFAP TTVNSGRGKE FEGAVIAFFH LLAVRKDKKR ALVEAFYRTN 

       250        260        270        280        290        300 
LPNMFQVLMT VAIFLFVLYL QGFRYELPIR STKVRGQIGI YPIKLFYTSN TPIMLQSALT 

       310        320        330        340        350        360 
SNIFLISQIL FQKYPTNPLI RLIGVWGIRP GTQGPQMALS GLAYYIQPLM SLSEALLDPI 

       370        380        390        400        410        420 
KTIVYITFVL GSCAVFSKTW IEISGTSPRD IAKQFKDQGM VINGKRETSI YRELKKIIPT 

       430        440        450        460        470        480 
AAAFGGATIG ALSVGSDLLG TLGSGASILM ATTTIYGYYE AAAKEGGFTK NLVPGFSDLM

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum." Stirling C.J., Rothblatt J., Hosobuchi M., Deshaies R., Schekman R. Mol. Biol. Cell 3:129-142(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. Hoheisel J.D. Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Determination of the transmembrane topology of yeast Sec61p, an essential component of the endoplasmic reticulum translocation complex." Wilkinson B.M., Critchley A.J., Stirling J. J. Biol. Chem. 271:25590-25597(1996) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY.
[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]	"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].
[10]	"Interactions between Sec complex and prepro-alpha-factor during posttranslational protein transport into the endoplasmic reticulum." Plath K., Wilkinson B.M., Stirling C.J., Rapoport T.A. Mol. Biol. Cell 15:1-10(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION WITH THE SIGNAL SEQUENCE.
[11]	"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 STT3; OST1; OST2; OST4; SWP1 AND WBP1.
[12]	"Identification of cytoplasmic residues of Sec61p involved in ribosome binding and cotranslational translocation." Cheng Z., Jiang Y., Mandon E.C., Gilmore R. J. Cell Biol. 168:67-77(2005) [PubMed] [Europe PMC] [Abstract] Cited for: ASSOCIATION WITH THE RIBOSOME, MUTAGENESIS OF LYS-273; ARG-275; GLY-276; LYS-405 AND ARG-406.
[13]	"A global topology map of the Saccharomyces cerevisiae membrane proteome." Kim H., Melen K., Oesterberg M., von Heijne G. Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS]. Strain: ATCC 208353 / W303-1A.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X62340 Genomic DNA. Translation: CAA44215.1. U19104 Genomic DNA. Translation: AAB67276.1. U19103 Genomic DNA. Translation: AAB67581.1. BK006945 Genomic DNA. Translation: DAA09680.1.
PIR	A60043.
RefSeq	NP_013482.1. NM_001182267.1.
3D structure databases
ProteinModelPortal	P32915.
SMR	P32915. Positions 5-465.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2433N.
IntAct	P32915. 14 interactions.
MINT	MINT-547730.
STRING	4932.YLR378C.
Protein family/group databases
TCDB	3.A.5.8.1. general secretory pathway (Sec) family.
Proteomic databases
PaxDb	P32915.
PeptideAtlas	P32915.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR378C; YLR378C; YLR378C.
GeneID	851095.
KEGG	sce:YLR378C.
Organism-specific databases
CYGD	YLR378c.
SGD	S000004370. SEC61.
Phylogenomic databases
eggNOG	COG0201.
GeneTree	ENSGT00390000003721.
HOGENOM	HOG000231249.
KO	K10956.
OMA	VEIPLSY.
OrthoDB	EOG4CRQ7J.
Enzyme and pathway databases
BioCyc	YEAST:G3O-32445-MONOMER.
Gene expression databases
Genevestigator	P32915.
GermOnline	YLR378C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	1.10.3370.10. 1 hit.
InterPro	IPR002208. SecY/SEC61-alpha. IPR023201. SecY_su_dom. IPR019561. Translocon_Sec61/SecY_plug_dom. [Graphical view]
PANTHER	PTHR10906. PTHR10906. 1 hit.
Pfam	PF10559. Plug_translocon. 1 hit. PF00344. SecY. 1 hit. [Graphical view]
PIRSF	PIRSF004557. SecY. 1 hit.
SUPFAM	SSF103491. SecY. 1 hit.
TIGRFAMs	TIGR00967. 3a0501s007. 1 hit.
PROSITE	PS00755. SECY_1. 1 hit. PS00756. SECY_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	967773.

Entry information

Entry name

SC61A_YEAST

Accession

Primary (citable) accession number: P32915
Secondary accession number(s): D6VZ14

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	May 29, 2013
This is version 118 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XII

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents