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Protein

Translocation protein SEC62

Gene

SEC62

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

Acts as component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and KAR2 in a channel-forming translocon complex. In an initial step, the signal sequence seems to bind simultaneously to SEC61 and SEC62. SEC62 and SEC63 are required for interactions between SEC61 and translocating polypeptides. SEC62 may affect SEC1-polypeptide interactions by increasing the affinity of targeting pathways for SEC61 and/or by modifying SEC61 to allow more efficient polypeptide interaction. A cycle of assembly and disassembly of Sec62/63 complex from SEC61 may govern the activity of the translocon. SEC62 is essential for cell growth.

GO - Molecular functioni

  • protein transporter activity Source: SGD

GO - Biological processi

  • posttranslational protein targeting to membrane, translocation Source: SGD
Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-33998-MONOMER.
ReactomeiR-SCE-381038. XBP1(S) activates chaperone genes.

Protein family/group databases

TCDBi1.A.15.1.1. the non-selective cation channel-2 (nscc2) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Translocation protein SEC62
Alternative name(s):
Sec62/63 complex 30 kDa subunit
Gene namesi
Name:SEC62
Ordered Locus Names:YPL094C
ORF Names:LPG14C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL094C.
SGDiS000006015. SEC62.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 149148CytoplasmicSequence analysisAdd
BLAST
Transmembranei150 – 16920HelicalSequence analysisAdd
BLAST
Topological domaini170 – 18314LumenalSequence analysisAdd
BLAST
Transmembranei184 – 20421HelicalSequence analysisAdd
BLAST
Topological domaini205 – 27470CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of endoplasmic reticulum membrane Source: InterPro
  • Sec62/Sec63 complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 274273Translocation protein SEC62PRO_0000206627Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP21825.

PTM databases

iPTMnetiP21825.

Interactioni

Subunit structurei

Component of the heterotetrameric Sec62/63complex composed of SEC62, SEC63, SEC71 and SEC72. The Sec62/63 complex associates with the Sec61 complex to form the Sec complex.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SEC61P3291510EBI-16632,EBI-16400
SEC63P149068EBI-16632,EBI-16636

Protein-protein interaction databases

BioGridi36087. 88 interactions.
DIPiDIP-3827N.
IntActiP21825. 41 interactions.
MINTiMINT-495147.

Structurei

3D structure databases

ProteinModelPortaliP21825.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi246 – 27025Arg/Lys-rich (basic)Add
BLAST

Sequence similaritiesi

Belongs to the SEC62 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000002757.
HOGENOMiHOG000248588.
InParanoidiP21825.
KOiK12275.
OMAiIVRLIIY.
OrthoDBiEOG7PK9B1.

Family and domain databases

InterProiIPR004728. Sec62.
IPR011553. Sec62_asco.
[Graphical view]
PANTHERiPTHR12443. PTHR12443. 1 hit.
PfamiPF03839. Sec62. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00869. sec62. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21825-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAVGPGSNA GASVNGGSAT AIATLLRNHK ELKQRQGLFQ AKQTDFFRYK
60 70 80 90 100
RFVRALHSEE YANKSARQPE IYPTIPSNKI EDQLKSREIF IQLIKAQMVI
110 120 130 140 150
PVKKLHSQEC KEHGLKPSKD FPHLIVSNKA QLEADEYFVW NYNPRTYMDY
160 170 180 190 200
LIVIGVVSII LALVCYPLWP RSMRRGSYYV SLGAFGILAG FFAVAILRLI
210 220 230 240 250
LYVLSLIVYK DVGGFWIFPN LFEDCGVLES FKPLYGFGEK DTYSYKKKLK
260 270
RMKKKQAKRE SNKKKAINEK AEQN
Length:274
Mass (Da):31,347
Last modified:July 11, 2006 - v2
Checksum:i2B2BA0DAAF3ACCA1
GO

Sequence cautioni

The sequence AAB68205.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAB56541.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51666 Genomic DNA. Translation: CAB56541.1. Different initiation.
U43281 Genomic DNA. Translation: AAB68205.1. Different initiation.
BK006949 Genomic DNA. Translation: DAA11339.1.
PIRiA33617.
RefSeqiNP_015231.2. NM_001183908.1.

Genome annotation databases

EnsemblFungiiYPL094C; YPL094C; YPL094C.
GeneIDi856011.
KEGGisce:YPL094C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51666 Genomic DNA. Translation: CAB56541.1. Different initiation.
U43281 Genomic DNA. Translation: AAB68205.1. Different initiation.
BK006949 Genomic DNA. Translation: DAA11339.1.
PIRiA33617.
RefSeqiNP_015231.2. NM_001183908.1.

3D structure databases

ProteinModelPortaliP21825.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36087. 88 interactions.
DIPiDIP-3827N.
IntActiP21825. 41 interactions.
MINTiMINT-495147.

Protein family/group databases

TCDBi1.A.15.1.1. the non-selective cation channel-2 (nscc2) family.

PTM databases

iPTMnetiP21825.

Proteomic databases

MaxQBiP21825.

Protocols and materials databases

DNASUi856011.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL094C; YPL094C; YPL094C.
GeneIDi856011.
KEGGisce:YPL094C.

Organism-specific databases

EuPathDBiFungiDB:YPL094C.
SGDiS000006015. SEC62.

Phylogenomic databases

GeneTreeiENSGT00390000002757.
HOGENOMiHOG000248588.
InParanoidiP21825.
KOiK12275.
OMAiIVRLIIY.
OrthoDBiEOG7PK9B1.

Enzyme and pathway databases

BioCyciYEAST:G3O-33998-MONOMER.
ReactomeiR-SCE-381038. XBP1(S) activates chaperone genes.

Miscellaneous databases

PROiP21825.

Family and domain databases

InterProiIPR004728. Sec62.
IPR011553. Sec62_asco.
[Graphical view]
PANTHERiPTHR12443. PTHR12443. 1 hit.
PfamiPF03839. Sec62. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00869. sec62. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "SEC62 encodes a putative membrane protein required for protein translocation into the yeast endoplasmic reticulum."
    Deshaies R.J., Schekman R.
    J. Cell Biol. 109:2653-2664(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(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. "Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex."
    Deshaies R.J., Sanders S.L., Feldheim D.A., Schekman R.
    Nature 349:806-808(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SEC62/63 COMPLEX.
  5. "Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p."
    Panzner S., Dreier L., Hartmann E., Kostka S., Rapoport T.A.
    Cell 81:561-570(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION OF THE SEC62/63 COMPLEX WITH THE SEC61 COMPLEX.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "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.
  8. "Identification of novel protein-protein interactions at the cytosolic surface of the Sec63 complex in the yeast ER membrane."
    Willer M., Jermy A.J., Young B.P., Stirling C.J.
    Yeast 20:133-148(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF N-TERMINUS, INTERACTION WITH SEC63.
  9. "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.
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSEC62_YEAST
AccessioniPrimary (citable) accession number: P21825
Secondary accession number(s): D6W3S3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: July 11, 2006
Last modified: June 8, 2016
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 16500 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: 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.