Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST6 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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Q03723 (OST6_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 94. History...

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

Documents (5) |

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:
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST6
Short name=Oligosaccharyl transferase subunit OST6
EC=2.4.1.119

Alternative name(s):
Oligosaccharyl transferase 37 kDa subunit
Short name=OTase 37 kDa subunit

Gene names

Name:	OST6
Ordered Locus Names:	YML019W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	332 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Subunit of N-oligosaccharyl transferase enzyme which catalyzes the transfer of a high mannose oligosaccharide to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. Can participate in redox reactions and is able to catalyze dithiol-disulfide exchange reactions with other proteins, albeit with relatively low efficiency. May form transient disulfide bonds with nascent polypeptides in the endoplasmic reticulum and thereby promote efficient glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal oligosaccharyl transferase activity. Ref.11
Catalytic activity	Dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine.
Pathway	Protein modification; protein glycosylation.
Subunit structure	Component of the oligosaccharyl transferase (OST) complex, which apears to exist in two assemblies comprising OST1, OST2, OST4, OST5, STT3, SWP1, WPB1, and either OST3 or OST6. May interact directly with OST1, OST2, OST4, STT3, WBP1 and SWP1.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Probable.
Miscellaneous	Present with 1080 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the OST3/OST6 family.
Biophysicochemical properties	Redox potential: E₀ is -275 mV. Ref.11

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Transferase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein N-linked glycosylation via asparagine Inferred from mutant phenotype Ref.1. Source: SGD protein complex assembly Inferred from mutant phenotype Ref.1. Source: SGD
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW oligosaccharyltransferase complex Inferred from physical interaction Ref.1 Ref.7. Source: SGD
Molecular function	dolichyl-diphosphooligosaccharide-protein glycotransferase activity Inferred from physical interaction Ref.1. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
OST1	P41543	3	EBI-12696,EBI-12651

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 332

332

Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST6

PRO_0000058098

Regions

Topological domain

1 – 188

188

Lumenal Potential

Transmembrane

189 – 209

Helical; Potential

Transmembrane

217 – 237

Helical; Potential

Transmembrane

268 – 288

Helical; Potential

Transmembrane

303 – 323

Helical; Potential

Topological domain

324 – 332

Lumenal Potential

Amino acid modifications

Disulfide bond

78 ↔ 81

Redox-active Probable

Experimental info

Mutagenesis

C → S: Alters glycosyltransferase efficiency towards a subset of target proteins; when associated with S-81. Ref.11

Mutagenesis

C → S: Alters glycosyltransferase efficiency towards a subset of target proteins; when associated with S-78. Ref.11

Sequence conflict

I → T in AAT92993. Ref.4

Secondary structure

332

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q03723 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: FC7AE156BF27F1B5
Show »

FASTA

332

37,891

        10         20         30         40         50         60 
MKWCSTYIII WLAIIFHKFQ KSTATASHNI DDILQLKDDT GVITVTADNY PLLSRGVPGY 

        70         80         90        100        110        120 
FNILYITMRG TNSNGMSCQL CHDFEKTYHA VADVIRSQAP QSLNLFFTVD VNEVPQLVKD 

       130        140        150        160        170        180 
LKLQNVPHLV VYPPAESNKQ SQFEWKTSPF YQYSLVPENA ENTLQFGDFL AKILNISITV 

       190        200        210        220        230        240 
PQAFNVQEFV YYFVACMVVF IFIKKVILPK VTNKWKLFSM ILSLGILLPS ITGYKFVEMN 

       250        260        270        280        290        300 
AIPFIARDAK NRIMYFSGGS GWQFGIEIFS VSLMYIVMSA LSVLLIYVPK ISCVSEKMRG 

       310        320        330 
LLSSFLACVL FYFFSYFISC YLIKNPGYPI VF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The oligosaccharyltransferase complex from Saccharomyces cerevisiae. Isolation of the OST6 gene, its synthetic interaction with OST3, and analysis of the native complex." Knauer R., Lehle L. J. Biol. Chem. 274:17249-17256(1999) [PubMed: 10358084] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION IN THE OLIGOSACCHARYL TRANSFERASE COMPLEX.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. Barrell B.G. Nature 387:90-93(1997) [PubMed: 9169872] [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]	"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. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"The oligosaccharyltransferase complex from yeast." Knauer R., Lehle L. Biochim. Biophys. Acta 1426:259-273(1999) [PubMed: 9878773] [Abstract] Cited for: REVIEW ON OLIGOSACCHARYL TRANSFERASE.
[6]	"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].
[7]	"Yeast oligosaccharyltransferase consists of two functionally distinct sub-complexes, specified by either the Ost3p or Ost6p subunit." Schwarz M., Knauer R., Lehle L. FEBS Lett. 579:6564-6568(2005) [PubMed: 16297388] [Abstract] Cited for: COMPOSITION OF OLIGOSACCHARYL TRANSFERASE COMPLEXES.
[8]	"The 3.4-kDa Ost4 protein is required for the assembly of two distinct oligosaccharyltransferase complexes in yeast." Spirig U., Bodmer D., Wacker M., Burda P., Aebi M. Glycobiology 15:1396-1406(2005) [PubMed: 16096346] [Abstract] Cited for: COMPOSITION OF OLIGOSACCHARYL TRANSFERASE COMPLEXES.
[9]	"Two oligosaccharyl transferase complexes exist in yeast and associate with two different translocons." Yan A., Lennarz W.J. Glycobiology 15:1407-1415(2005) [PubMed: 16096345] [Abstract] Cited for: COMPOSITION OF OLIGOSACCHARYL TRANSFERASE COMPLEXES.
[10]	"Studies of yeast oligosaccharyl transferase subunits using the split-ubiquitin system: topological features and in vivo interactions." Yan A., Wu E., Lennarz W.J. Proc. Natl. Acad. Sci. U.S.A. 102:7121-7126(2005) [PubMed: 15886282] [Abstract] Cited for: TOPOLOGY, INTERACTION WITH OST1; OST2; OST4; STT3; WBP1 AND SWP1.
[11]	"Oxidoreductase activity of oligosaccharyltransferase subunits Ost3p and Ost6p defines site-specific glycosylation efficiency." Schulz B.L., Stirnimann C.U., Grimshaw J.P., Brozzo M.S., Fritsch F., Mohorko E., Capitani G., Glockshuber R., Grutter M.G., Aebi M. Proc. Natl. Acad. Sci. U.S.A. 106:11061-11066(2009) [PubMed: 19549845] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 24-188, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, REDOX POTENTIAL, MUTAGENESIS OF CYS-78 AND CYS-81.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y08606 Genomic DNA. Translation: CAA69898.1.
Z46659 Genomic DNA. Translation: CAA86636.1.
AY692974 Genomic DNA. Translation: AAT92993.1.
BK006946 Genomic DNA. Translation: DAA09879.1.

PIR

S49758.

RefSeq

NP_013693.1. NM_001182377.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3G7Y	X-ray	2.21	A	24-188	[»]
3G9B	X-ray	1.96	A	24-188	[»]
3GA4	X-ray	1.30	A	24-188	[»]

ProteinModelPortal

Q03723.

SMR

Q03723. Positions 30-185.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-3851N.

IntAct

Q03723. 8 interactions.

MINT

MINT-509989.

STRING

Q03723.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YML019W; YML019W; YML019W.

GeneID

854989.

KEGG

sce:YML019W.

NMPDR

fig|4932.3.peg.4734.

Organism-specific databases

CYGD

YML019w.

SGD

S000004481. OST6.

Phylogenomic databases

eggNOG

fuNOG09139.

HOGENOM

HBG203362.

OMA

YQFGIEV.

OrthoDB

EOG45QMPM.

Enzyme and pathway databases

BRENDA

2.4.1.119. 984.

Gene expression databases

ArrayExpress

Q03723.

Genevestigator

Q03723.

GermOnline

YML019W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR006844. Mg_transporter-1.
IPR021149. OligosaccharylTrfase_OST3/OST6.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

K12669.

PANTHER

PTHR12692. OST3_OST6. 1 hit.

Pfam

PF04756. OST3_OST6. 1 hit.
[Graphical view]

SUPFAM

SSF52833. Thiordxn-like_fd. 1 hit.

ProtoNet

Search...

Other

NextBio

978124.

Entry information

Entry name

OST6_YEAST

Accession

Primary (citable) accession number: Q03723
Secondary accession number(s): D6VZF5, E9P904

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 94 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 XIII

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction 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