Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3

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Reviewed, UniProtKB/Swiss-Prot P39007 (STT3_YEAST)

Last modified November 3, 2009. Version 84. History...

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

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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:
    Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3
      Short name=Oligosaccharyl transferase subunit STT3
    EC=2.4.1.119

Gene names

Name:	STT3
Ordered Locus Names:	YGL022W

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	718 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	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. 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 enzyme activity. Ref.7
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 oligosaccharyltransferase (OST) complex, which apears to exist in two assemblies comprising OST1, OST2, OST4, OST5, STT3, SWP1, WPB1, and either OST3 or OST6. OST3, OST4 and STT3 probably form a subcomplex. May interact directly with OST3, OST4, OST6, WBP1 and SWP1. Interacts with SEC61. Ref.6 Ref.13 Ref.14
Subcellular location	Membrane; Multi-pass membrane protein.
Miscellaneous	Present with 3000 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the STT3 family.

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Ontologies

Keywords
Cellular component	Membrane
Domain	Transmembrane
Molecular function	Transferase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein amino acid N-linked glycosylation Ref.4 Inferred from physical interaction. Source: SGD
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell oligosaccharyltransferase complex Ref.4 Ref.9 Inferred from physical interaction. Source: SGD
Molecular function	dolichyl-diphosphooligosaccharide-protein glycotransferase activity Ref.4 Inferred from physical interaction. Source: SGD identical protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
itself		1	EBI-18447,EBI-18447
OST3	P48439	1	EBI-18447,EBI-12680
OST4	Q99380	1	EBI-18447,EBI-12689
SBH1	P52870	1	EBI-18447,EBI-16410
SEC61	P32915	1	EBI-18447,EBI-16400
WBP1	P33767	2	EBI-18447,EBI-12658

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 718

718

Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3

PRO_0000072293

Regions

Topological domain

1 – 8

Cytoplasmic Potential

Transmembrane

9 – 29

Potential

Topological domain

30 – 113

Lumenal Potential

Transmembrane

114 – 134

Potential

Topological domain

135 – 162

Cytoplasmic Potential

Transmembrane

163 – 183

Potential

Topological domain

184 – 207

Lumenal Potential

Transmembrane

208 – 228

Potential

Topological domain

229 – 240

Cytoplasmic Potential

Transmembrane

241 – 261

Potential

Topological domain

262 – 266

Lumenal Potential

Transmembrane

267 – 287

Potential

Topological domain

288 – 295

Cytoplasmic Potential

Transmembrane

296 – 316

Potential

Topological domain

317 – 358

Lumenal Potential

Transmembrane

359 – 379

Potential

Topological domain

380 – 382

Cytoplasmic Potential

Transmembrane

383 – 403

Potential

Topological domain

404

Lumenal Potential

Transmembrane

405 – 425

Potential

Topological domain

426 – 443

Cytoplasmic Potential

Transmembrane

444 – 464

Potential

Topological domain

465 – 718

254

Lumenal Potential

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

535

N-linked (GlcNAc...) Potential

Glycosylation

539

N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis

159

R → A: Temperature sensitive and staurosporine sensitive. Ref.12

Mutagenesis

160

S → A: Temperature sensitive and staurosporine sensitive. Ref.12

Mutagenesis

163

G → R: Temperature sensitive and staurosporine sensitive.

Mutagenesis

164

S → A: Temperature sensitive and staurosporine sensitive. Ref.12

Mutagenesis

208

W → A: Lethal; abolishes interaction with OST1 and WBP1. Ref.12

Mutagenesis

210

G → D: Temperature sensitive and staurosporine sensitive. Ref.12

Mutagenesis

393

V → I: Staurosporine sensitive. Ref.12

Mutagenesis

404

R → A: Lethal; abolishes interaction with OST1 and WBP1. Ref.12

Mutagenesis

516 – 519

WWDY → AAAA: Lethal; greatly reduces amount of OST1 in complex. Ref.7

Mutagenesis

516

W → A: Temperature-sensitive. Ref.7

Mutagenesis

517

W → A: Lethal. Ref.7

Mutagenesis

518

D → A: Lethal. Ref.7

Mutagenesis

519

Y → A: Temperature-sensitive. Ref.7

Mutagenesis

520

G → D: Temperature-sensitive. Ref.7

Mutagenesis

554 – 556

EEK → AAA: Temperature-sensitive; reduces amount of OST1 in complex.

Mutagenesis

592 – 594

RIS → AAA: Lethal; reduces glycosylation; greatly reduces amount of OST1 in complex.

Mutagenesis

593

I → D: Temperature-sensitive. Ref.7

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Sequences

Sequence

Length

Mass (Da)

Tools

P39007-1 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: D00B8FF7B2B11B9F
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FASTA

718

81,529

        10         20         30         40         50         60 
MGSDRSCVLS VFQTILKLVI FVAIFGAAIS SRLFAVIKFE SIIHEFDPWF NYRATKYLVN 

        70         80         90        100        110        120 
NSFYKFLNWF DDRTWYPLGR VTGGTLYPGL MTTSAFIWHA LRNWLGLPID IRNVCVLFAP 

       130        140        150        160        170        180 
LFSGVTAWAT YEFTKEIKDA SAGLLAAGFI AIVPGYISRS VAGSYDNEAI AITLLMVTFM 

       190        200        210        220        230        240 
FWIKAQKTGS IMHATCAALF YFYMVSAWGG YVFITNLIPL HVFLLILMGR YSSKLYSAYT 

       250        260        270        280        290        300 
TWYAIGTVAS MQIPFVGFLP IRSNDHMAAL GVFGLIQIVA FGDFVKGQIS TAKFKVIMMV 

       310        320        330        340        350        360 
SLFLILVLGV VGLSALTYMG LIAPWTGRFY SLWDTNYAKI HIPIIASVSE HQPVSWPAFF 

       370        380        390        400        410        420 
FDTHFLIWLF PAGVFLLFLD LKDEHVFVIA YSVLCSYFAG VMVRLMLTLT PVICVSAAVA 

       430        440        450        460        470        480 
LSKIFDIYLD FKTSDRKYAI KPAALLAKLI VSGSFIFYLY LFVFHSTWVT RTAYSSPSVV 

       490        500        510        520        530        540 
LPSQTPDGKL ALIDDFREAY YWLRMNSDED SKVAAWWDYG YQIGGMADRT TLVDNNTWNN 

       550        560        570        580        590        600 
THIAIVGKAM ASPEEKSYEI LKEHDVDYVL VIFGGLIGFG GDDINKFLWM IRISEGIWPE 

       610        620        630        640        650        660 
EIKERDFYTA EGEYRVDARA SETMRNSLLY KMSYKDFPQL FNGGQATDRV RQQMITPLDV 

       670        680        690        700        710 
PPLDYFDEVF TSENWMVRIY QLKKDDAQGR TLRDVGELTR SSTKTRRSIK RPELGLRV

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"STT3, a novel essential gene related to the PKC1/STT1 protein kinase pathway, is involved in protein glycosylation in yeast." Yoshida S., Ohya Y., Nakano A., Anraku Y. Gene 164:167-172(1995) [PubMed: 7590309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"STT3, a highly conserved protein required for yeast oligosaccharyl transferase activity in vivo." Zufferey R., Knauer R., Burda P., Stagljar I., Te Heesen S., Lehle L., Aebi M. EMBO J. 14:4949-4960(1995) [PubMed: 7588624] [Abstract] Cited for: CHARACTERIZATION.
[4]	"The highly conserved Stt3 protein is a subunit of the yeast oligosaccharyltransferase and forms a subcomplex with Ost3p and Ost4p." Karaoglu D., Kelleher D.J., Gilmore R. J. Biol. Chem. 272:32513-32520(1997) [PubMed: 9405463] [Abstract] Cited for: IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE COMPLEX.
[5]	"The STT3 protein is a component of the yeast oligosaccharyltransferase complex." Spirig U., Glavas M., Bodmer D., Reiss G., Burda P., Lippuner V., te Heesen S., Aebi M. Mol. Gen. Genet. 256:628-637(1997) [PubMed: 9435788] [Abstract] Cited for: IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE COMPLEX.
[6]	"Studies on the role of the hydrophobic domain of Ost4p in interactions with other subunits of yeast oligosaccharyl transferase." Kim H., Park H., Montalvo L., Lennarz W.J. Proc. Natl. Acad. Sci. U.S.A. 97:1516-1520(2000) [PubMed: 10677492] [Abstract] Cited for: INTERACTION WITH OST3 AND OST4.
[7]	"Studies on the function of oligosaccharyl transferase subunits. Stt3p is directly involved in the glycosylation process." Yan Q., Lennarz W.J. J. Biol. Chem. 277:47692-47700(2002) [PubMed: 12359722] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF TRP-516; TRP-517; ASP-518; TYR-519; GLY-520 AND ILE-593.
[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]	"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 OLIGOSACCHARYLTRANSFERASE COMPLEXES.
[10]	"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 OLIGOSACCHARYLTRANSFERASE COMPLEXES.
[11]	"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 OLIGOSACCHARYLTRANSFERASE COMPLEXES.
[12]	"Membrane topology of the STT3 subunit of the oligosaccharyl transferase complex." Kim H., von Heijne G., Nilsson I. J. Biol. Chem. 280:20261-20267(2005) [PubMed: 15781470] [Abstract] Cited for: TOPOLOGY, MUTAGENESIS OF ARG-159; SER-160; SER-164; TRP-208; GLY-210; VAL-393 AND ARG-404.
[13]	"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 SEC61.
[14]	"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 OST3; OST4; OST6; WBP1 AND SWP1.
[15]	"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
	D28952 Genomic DNA. Translation: BAA06079.1. Z72544 Genomic DNA. Translation: CAA96722.1.
PIR	S64024.
RefSeq	NP_011493.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2459N.
IntAct	P39007. 10 interactions.
STRING	P39007.
Protein family/group databases
CAZy	GT66. Glycosyltransferase Family 66.
Proteomic databases
PeptideAtlas	P39007.
Genome annotation databases
Ensembl	YGL022W; YGL022W; YGL022W; Saccharomyces cerevisiae. [Genome view]
GeneID	852862.
GenomeReviews	Gene locus YGL022W in contig Y13135_GR.
KEGG	sce:YGL022W.
NMPDR	fig\|4932.3.peg.2600.
Organism-specific databases
CYGD	YGL022w.
SGD	S000002990. STT3.
Phylogenomic databases
HOGENOM	P39007.
OMA	SKLYSAY.
Enzyme and pathway databases
BRENDA	2.4.1.119. 250.
Gene expression databases
ArrayExpress	P39007.
Genevestigator	P39007.
GermOnline	YGL022W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR003674. Oligo_trans_STT3. [Graphical view]
Pfam	PF02516. STT3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	972472.

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Entry information

Entry name

STT3_YEAST

Accession

Primary (citable) accession number: P39007

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	October 1, 1996
Last modified:	November 3, 2009
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome VII

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

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

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

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents