Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A

Preferred order of sections

Names and origin

Protein names

Recommended name:
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
Short name=Oligosaccharyl transferase subunit STT3A
Short name=STT3-A
EC=2.4.99.18

Alternative name(s):
Integral membrane protein 1
Protein STAUROSPORIN AND TEMPERATURE SENSITIVE 3-LIKE A

Gene names

Name:	STT3A
Ordered Locus Names:	At5g19690
ORF Names:	T29J13_110

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	779 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalytic subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor 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). SST3A seems to be involved in complex substrate specificity By similarity. Controls adaptive responses to salt/osmotic stress. Acts as a key glycosylation determinant for EFR function during plant innate immunity. Ref.4 Ref.6
Catalytic activity	Dolichyl diphosphooligosaccharide + [protein]-L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
Pathway	Protein modification; protein glycosylation.
Subunit structure	Component of the oligosaccharyltransferase (OST) complex By similarity.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein.
Tissue specificity	Expressed in the root and in the shoot. Ref.4
Disruption phenotype	Salt/osmotic sensitivity associated with root tip growth arrest and swelling and the induction of lateral roots. Ref.4
Sequence similarities	Belongs to the STT3 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein glycosylation Inferred from electronic annotation. Source: UniProtKB-UniPathway regulation of response to osmotic stress Inferred from mutant phenotype Ref.4. Source: UniProtKB response to salt stress Inferred from mutant phenotype Ref.4. Source: TAIR
Cellular_component	endoplasmic reticulum Inferred from direct assay Ref.5 Ref.7. Source: TAIR endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay PubMed 17317660. Source: TAIR
Molecular_function	oligosaccharyl transferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 779

779

Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A

PRO_0000420536

Regions

Topological domain

1 – 17

17

Cytoplasmic Potential

Transmembrane

18 – 38

21

Helical; Potential

Topological domain

39 – 119

81

Lumenal Potential

Transmembrane

120 – 140

21

Helical; Potential

Topological domain

141 – 174

34

Cytoplasmic Potential

Transmembrane

175 – 195

21

Helical; Potential

Topological domain

196 – 213

18

Lumenal Potential

Transmembrane

214 – 234

21

Helical; Potential

Topological domain

235 – 242

8

Cytoplasmic Potential

Transmembrane

243 – 263

21

Helical; Potential

Topological domain

264 – 274

11

Lumenal Potential

Transmembrane

275 – 295

21

Helical; Potential

Topological domain

296 – 305

10

Cytoplasmic Potential

Transmembrane

306 – 326

21

Helical; Potential

Topological domain

327 – 366

40

Lumenal Potential

Transmembrane

367 – 387

21

Helical; Potential

Topological domain

388 – 394

7

Cytoplasmic Potential

Transmembrane

395 – 412

18

Helical; Potential

Topological domain

413

1

Lumenal Potential

Transmembrane

414 – 434

21

Helical; Potential

Topological domain

435 – 518

84

Cytoplasmic Potential

Transmembrane

519 – 539

21

Helical; Potential

Topological domain

540 – 779

240

Lumenal Potential

Amino acid modifications

Glycosylation

597

1

N-linked (GlcNAc...) Potential

Glycosylation

604

1

N-linked (GlcNAc...) Potential

Glycosylation

608

1

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

735

1

T → K in AAK91413. Ref.3

Sequence conflict

735

1

T → K in AAL31142. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

Q93ZY3 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 74F702FF6772478B
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FASTA

779

86,113

        10         20         30         40         50         60 
MAALESPLPG TPTAMRNAFG NVLSVLILVL IGVLAFSIRL FSVIKYESVI HEFDPYFNYR 

        70         80         90        100        110        120 
VTQFLSKNGI YEFWNWFDDR TWYPLGRVIG GTVYPGLTLT AGTIWWGLNS LNIPLSVETV 

       130        140        150        160        170        180 
CVFTAPVFSA FASWATYLLT KEVKGSGAGL AAAALLAMVP SYISRSVAGS YDNEAVAIFA 

       190        200        210        220        230        240 
LIFTFYLYIK TLNTGSLFYA TLNALAYFYM VCSWGGYTFI INLIPMHVLL CIVTGRYSPR 

       250        260        270        280        290        300 
LYIAYAPLVV LGTLLAALVP VVGFNAVLTS EHFASFLVFI IIHVVALVYY IKGILSPKMF 

       310        320        330        340        350        360 
KVAVTLVVSI GMVVCFIVVA ILVALVASSP TGGWSGRSLS LLDPTYASKY IPIIASVSEH 

       370        380        390        400        410        420 
QPPTWPSYFM DINVLAFLVP AGIIACFSPL SDASSFVVLY IVMSVYFSGV MVRLMLVLAP 

       430        440        450        460        470        480 
AACIMSGIAL SQAFDVFTGS IKYQLGASSN STDDAEDNTS TNNAPKDDVS AGKTDKGEEI 

       490        500        510        520        530        540 
VKERSSKKGK KKEREPADKP SVKAKIKKKA LVLPLEASIV ALLLLIMLGA FYVIHCVWAA 

       550        560        570        580        590        600 
AEAYSAPSIV LTSQSRDGLH VFDDFRESYA WLSHNTDVDD KVASWWDYGY QTTAMANRTV 

       610        620        630        640        650        660 
IVDNNTWNNT HIATVGTAMS SPEKAAWEIF NSLDVKYVLV VFGGLIGYPS DDINKFLWMV 

       670        680        690        700        710        720 
RIGGGVFPHI KEADYLRDGQ YRIDSEATPT MLNSLMYKLS YYRFVETDGK GYDRVRRTEI 

       730        740        750        760        770 
GKKHFKLTHF EEVFTSHHWM VRLYKLKPPR NRIRGKAKKL KSKTSSGLSS KSAKKNPWV

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. Fransz P.F. Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"The STT3a subunit isoform of the Arabidopsis oligosaccharyltransferase controls adaptive responses to salt/osmotic stress." Koiwa H., Li F., McCully M.G., Mendoza I., Koizumi N., Manabe Y., Nakagawa Y., Zhu J., Rus A., Pardo J.M., Bressan R.A., Hasegawa P.M. Plant Cell 15:2273-2284(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY. Strain: cv. C24 and cv. Columbia.
[5]	"Mapping the Arabidopsis organelle proteome." Dunkley T.P.J., Hester S., Shadforth I.P., Runions J., Weimar T., Hanton S.L., Griffin J.L., Bessant C., Brandizzi F., Hawes C., Watson R.B., Dupree P., Lilley K.S. Proc. Natl. Acad. Sci. U.S.A. 103:6518-6523(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION.
[6]	"Control of the pattern-recognition receptor EFR by an ER protein complex in plant immunity." Nekrasov V., Li J., Batoux M., Roux M., Chu Z.H., Lacombe S., Rougon A., Bittel P., Kiss-Papp M., Chinchilla D., van Esse H.P., Jorda L., Schwessinger B., Nicaise V., Thomma B.P., Molina A., Jones J.D., Zipfel C. EMBO J. 28:3428-3438(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Putative glycosyltransferases and other plant Golgi apparatus proteins are revealed by LOPIT proteomics." Nikolovski N., Rubtsov D., Segura M.P., Miles G.P., Stevens T.J., Dunkley T.P., Munro S., Lilley K.S., Dupree P. Plant Physiol. 160:1037-1051(2012) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF296838 Genomic DNA. No translation available. CP002688 Genomic DNA. Translation: AED92738.1. AY050397 mRNA. Translation: AAK91413.1. AY056191 mRNA. Translation: AAL07040.1. AY059649 mRNA. Translation: AAL31142.1.
IPI	IPI00548574.
RefSeq	NP_568380.1. NM_121974.4.
UniGene	At.23388.
3D structure databases
ProteinModelPortal	Q93ZY3.
SMR	Q93ZY3. Positions 535-777.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT5G19690.1-P.
Protein family/group databases
CAZy	GT66. Glycosyltransferase Family 66.
Proteomic databases
PaxDb	Q93ZY3.
PRIDE	Q93ZY3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G19690.1; AT5G19690.1; AT5G19690.
GeneID	832089.
KEGG	ath:AT5G19690.
Organism-specific databases
TAIR	At5g19690.
Phylogenomic databases
eggNOG	COG1287.
HOGENOM	HOG000157471.
InParanoid	Q93ZY3.
KO	K07151.
OMA	SHNTDVD.
PhylomeDB	Q93ZY3.
ProtClustDB	CLSN2689799.
Enzyme and pathway databases
BRENDA	2.4.1.119. 302.
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q93ZY3.
Genevestigator	Q93ZY3.
Family and domain databases
InterPro	IPR003674. Oligo_trans_STT3. [Graphical view]
Pfam	PF02516. STT3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

STT3A_ARATH

Accession

Primary (citable) accession number: Q93ZY3
Secondary accession number(s): Q94A42

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2013
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

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

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents