Protein transport protein SEC61 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P32915 (SC61A_YEAST)

Last modified November 24, 2009. Version 85. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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 (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	480 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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.10
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein.
Miscellaneous	Present with 24800 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the secY/SEC61-alpha family.

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Ontologies

Keywords
Biological process	Protein transport Translocation Transport
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	SRP-dependent cotranslational protein targeting to membrane, translocation Inferred from direct assay. Source: SGD peptide transport Inferred from mutant phenotype. Source: SGD posttranslational protein targeting to membrane, translocation Inferred from direct assay. Source: SGD retrograde protein transport, ER to cytosol Inferred from mutant phenotype. Source: SGD
Cellular component	integral to endoplasmic reticulum membrane Ref.1 Inferred from direct assay. Source: SGD translocon complex Inferred from direct assay. Source: SGD
Molecular function	P-P-bond-hydrolysis-driven protein transmembrane transporter activity Ref.1 Inferred from direct assay. Source: SGD peptide transporter activity Inferred from mutant phenotype. Source: SGD
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
AGP1	P25376	1	EBI-16400,EBI-2357
CHO1	P08456	1	EBI-16400,EBI-14055
ERV25	P54837	1	EBI-16400,EBI-6642
ERV29	P53337	1	EBI-16400,EBI-23662
OST1	P41543	2	EBI-16400,EBI-12651
OST2	P46964	1	EBI-16400,EBI-12673
OST4	Q99380	1	EBI-16400,EBI-12689
PMP2	P40975	1	EBI-16400,EBI-2043041
PMP3	P87284	1	EBI-16400,EBI-13555
RPS27A	P62990	1	EBI-16400,EBI-413053	From a different organism.
SAC1	P32368	1	EBI-16400,EBI-16210
SEC62	P21825	1	EBI-16400,EBI-16632
SEC63	P14906	1	EBI-16400,EBI-16636
SPF1	P39986	1	EBI-16400,EBI-3128
STT3	P39007	1	EBI-16400,EBI-18447
SWP1	Q02795	2	EBI-16400,EBI-12666
WBP1	P33767	1	EBI-16400,EBI-12658
YEL001C	P40006	1	EBI-16400,EBI-2050819
YER053C-A	Q3E7B0	1	EBI-16400,EBI-2047907

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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

1 Probable

Topological domain

56 – 75

Lumenal Probable

Transmembrane

76 – 95

2 Probable

Topological domain

96 – 119

Cytoplasmic Probable

Transmembrane

120 – 141

3 Probable

Topological domain

142 – 146

Lumenal Probable

Transmembrane

147 – 167

4 Probable

Topological domain

168 – 212

Cytoplasmic Probable

Transmembrane

213 – 224

5 Probable

Topological domain

225 – 240

Lumenal Probable

Transmembrane

241 – 260

6 Probable

Topological domain

261 – 290

Cytoplasmic Probable

Transmembrane

291 – 311

7 Probable

Topological domain

312 – 361

Lumenal Probable

Transmembrane

362 – 381

8 Probable

Topological domain

382 – 416

Cytoplasmic Probable

Transmembrane

417 – 434

9 Probable

Topological domain

435 – 437

Lumenal Probable

Transmembrane

438 – 459

10 Probable

Topological domain

460 – 480

Cytoplasmic Probable

Experimental info

Mutagenesis

273

K → P or G: Severe growth defect. Ref.11

Mutagenesis

275

R → D, G, P, Q or Y: Severe growth defect. Ref.11

Mutagenesis

275

R → E, F or V: Severe growth defect; lowers SRP-dependent and SRP-independent translocation. Ref.11

Mutagenesis

276

G → P: Severe growth defect. Ref.11

Mutagenesis

405

K → D, E or P: Severe growth defect. Ref.11

Mutagenesis

406

R → D: Severe growth defect; lowers SRP-dependent translocation. Ref.11

Mutagenesis

406

R → E: Severe growth defect; lowers SRP-dependent and SRP-independent translocation. Ref.11

Mutagenesis

406

R → H or W: Severe growth defect. Ref.11

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Sequences

Sequence

Length

Mass (Da)

Tools

P32915-1 [UniParc].

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

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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: 1550957] [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: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"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: 8810333] [Abstract] Cited for: TOPOLOGY.
[4]	"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: 8929540] [Abstract] Cited for: ELECTRON MICRSOCOPY OF THE SEC61 COMPLEX.
[5]	"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: 9160745] [Abstract] Cited for: TRANSLOCON COMPLEX PORE.
[6]	"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: 10611978] [Abstract] Cited for: REVIEW ON THE TRANSLOCON COMPLEX.
[7]	"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: 10775273] [Abstract] Cited for: ASSOCIATION OF THE SEC61 COMPLEX WITH RIBOSOMES.
[8]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"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: 14617809] [Abstract] Cited for: ASSOCIATION WITH THE SIGNAL SEQUENCE.
[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: 15831493] [Abstract] Cited for: INTERACTION WITH STT3; OST1; OST2; OST4; SWP1 AND WBP1.
[11]	"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: 15631991] [Abstract] Cited for: ASSOCIATION WITH THE RIBOSOME, MUTAGENESIS OF LYS-273; ARG-275; GLY-276; LYS-405 AND ARG-406.
[12]	"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: 16847258] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	X62340 Genomic DNA. Translation: CAA44215.1. U19104 Genomic DNA. Translation: AAB67276.1. U19103 Genomic DNA. Translation: AAB67581.1.
PIR	A60043.
RefSeq	NP_013482.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2433N.
IntAct	P32915. 23 interactions.
STRING	P32915.
Protein family/group databases
TCDB	3.A.5.8.1. general secretory pathway (Sec) family.
Proteomic databases
PeptideAtlas	P32915.
PRIDE	P32915.
Genome annotation databases
Ensembl	YLR378C; YLR378C; YLR378C; Saccharomyces cerevisiae. [Genome view]
GeneID	851095.
KEGG	sce:YLR378C.
NMPDR	fig\|4932.3.peg.4507.
Organism-specific databases
CYGD	YLR378c.
SGD	S000004370. SEC61.
Phylogenomic databases
HOGENOM	P32915.
OMA	TINIGRG
OrthoDB	EOG96DNJW
Gene expression databases
ArrayExpress	P32915.
Genevestigator	P32915.
GermOnline	YLR378C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR002208. SecY. IPR019561. Translocon_Sec61/SecY_plug_dom. [Graphical view]
PANTHER	PTHR10906. SecY. 1 hit.
Pfam	PF10559. Plug_translocon. 1 hit. PF00344. SecY. 1 hit. [Graphical view]
PIRSF	PIRSF004557. SecY. 1 hit.
TIGRFAMs	TIGR00967. 3a0501s007. 1 hit.
PROSITE	PS00755. SECY_1. 1 hit. PS00756. SECY_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	967773.

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Entry information

Entry name

SC61A_YEAST

Accession

Primary (citable) accession number: P32915

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	November 24, 2009
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

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

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

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents