Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A

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P46978 (STT3A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 86. History...

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

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
Short name=Oligosaccharyl transferase subunit STT3A
Short name=STT3-A
EC=2.4.1.119

Alternative name(s):
B5
Integral membrane protein 1

Gene names

Name:	Stt3a
Synonyms:	Itm1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	705 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the N-oligosaccharyl transferase enzyme 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.
Catalytic activity	Dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-glycosyl linkage to protein L-asparagine.
Subunit structure	Component of the oligosaccharyltransferase (OST) complex. OST seems to exist in different forms which contain at least RPN1, RPN2, OST48, DAD1, OSTC, KRTCAP2 and either STT3A or STT3B. OST can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes By similarity.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the STT3 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Transferase
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	protein N-linked glycosylation via asparagine Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane fraction Inferred from direct assay. Source: MGI oligosaccharyltransferase complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	dolichyl-diphosphooligosaccharide-protein glycotransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 705

705

Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A

PRO_0000072291

Regions

Topological domain

1 – 17

Cytoplasmic Potential

Transmembrane

18 – 38

Helical; Potential

Topological domain

39 – 114

Lumenal Potential

Transmembrane

115 – 135

Helical; Potential

Topological domain

136 – 169

Cytoplasmic Potential

Transmembrane

170 – 190

Helical; Potential

Topological domain

191 – 208

Lumenal Potential

Transmembrane

209 – 229

Helical; Potential

Topological domain

230 – 235

Cytoplasmic Potential

Transmembrane

236 – 259

Helical; Potential

Topological domain

260 – 300

Lumenal Potential

Transmembrane

301 – 321

Helical; Potential

Topological domain

322 – 359

Cytoplasmic Potential

Transmembrane

360 – 380

Helical; Potential

Topological domain

381 – 383

Lumenal Potential

Transmembrane

384 – 404

Helical; Potential

Topological domain

405

Cytoplasmic Potential

Transmembrane

406 – 426

Helical; Potential

Topological domain

427 – 453

Lumenal Potential

Transmembrane

454 – 474

Helical; Potential

Topological domain

475 – 705

231

Lumenal Potential

Amino acid modifications

Glycosylation

381

N-linked (GlcNAc...) Potential

Glycosylation

537

N-linked (GlcNAc...) Potential

Glycosylation

544

N-linked (GlcNAc...) Potential

Glycosylation

548

N-linked (GlcNAc...) Ref.6

Sequences

Sequence

Length

Mass (Da)

Tools

P46978 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: CD1D796D0479F321
Show »

FASTA

705

80,598

        10         20         30         40         50         60 
MTKLGFLRLS YEKQDTLLKL LILSMAAVLS FSTRLFAVLR FESVIHEFDP YFNYRTTRFL 

        70         80         90        100        110        120 
AEEGFYKFHN WFDDRAWYPL GRIIGGTIYP GLMITSAAIY HVLHFFHITI DIRNVCVFLA 

       130        140        150        160        170        180 
PLFSSFTTIV TYHLTKELKD AGAGLLAAAM IAVVPGYISR SVAGSYDNEG IAIFCMLLTY 

       190        200        210        220        230        240 
YMWIKAVKTG SIYWAAKCAL AYFYMVSSWG GYVFLINLIP LHVLVLMLTG RFSHRIYVAY 

       250        260        270        280        290        300 
CTVYCLGTIL SMQISFVGFQ PVLSSEHMAA FGVFGLCQIH AFVDYLRSKL NPQQFEVLFR 

       310        320        330        340        350        360 
SVISLVGFVL LTVGALLMLT GKISPWTGRF YSLLDPSYAK NNIPIIASVS EHQPTTWSSY 

       370        380        390        400        410        420 
YFDLQLLVFM FPVGLYYCFS NLSDARIFII MYGVTSMYFS AVMVRLMLVL APVMCILSGI 

       430        440        450        460        470        480 
GVSQVLSTYM KNLDISRPDK KSKKQQDSTY PIKNEVASGM ILVMAFFLIT YTFHSTWVTS 

       490        500        510        520        530        540 
EAYSSPSIVL SARGGDGSRI IFDDFREAYY WLRHNTPEDA KVMSWWDYGY QITAMANRTI 

       550        560        570        580        590        600 
LVDNNTWNNT HISRVGQAMA STEEKAYEIM RELDVSYVLV IFGGLTGYSS DDINKFLWMV 

       610        620        630        640        650        660 
RIGGSTETGR HIKENDYYTP TGEFRVDREG SPVLLNCLMY KMCYYRFGQV YTEAKRPPGF 

       670        680        690        700 
DRVRNAEIGN KDFELDVLEE AYTTEHWLVR IYKVKDLDNR GLSRT

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of a highly conserved mouse and human integral membrane protein (Itm1) and genetic mapping to mouse chromosome 9." Hong G., Deleersnjider W., Kozak C.A., van Marck E., Tylzanowski P., Merregaert J. Genomics 31:295-300(1996) [PubMed: 8838310] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Mandibular condyle.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary gland.
[3]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 696-704, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
[4]	"Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties." Kelleher D.J., Karaoglu D., Mandon E.C., Gilmore R. Mol. Cell 12:101-111(2003) [PubMed: 12887896] [Abstract] Cited for: TISSUE SPECIFICITY.
[5]	"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.
[6]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed: 19349973] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-548, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L34260 mRNA. Translation: AAB47775.1. BC037612 mRNA. Translation: AAH37612.1.
IPI	IPI00109108.
RefSeq	NP_032434.3. NM_008408.4.
UniGene	Mm.2863.
3D structure databases
ProteinModelPortal	P46978.
SMR	P46978. Positions 503-608.
ModBase	Search...
Protein-protein interaction databases
STRING	P46978.
Protein family/group databases
CAZy	GT66. Glycosyltransferase Family 66.
Proteomic databases
PRIDE	P46978.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000120381; ENSMUSP00000113116; ENSMUSG00000032116.
GeneID	16430.
KEGG	mmu:16430.
Organism-specific databases
CTD	3703.
MGI	MGI:105124. Stt3a.
Phylogenomic databases
eggNOG	roNOG05020.
HOVERGEN	HBG010606.
InParanoid	P46978.
OrthoDB	EOG4SF95B.
Gene expression databases
ArrayExpress	P46978.
Bgee	P46978.
Genevestigator	P46978.
GermOnline	ENSMUSG00000032116. Mus musculus.
Family and domain databases
InterPro	IPR003674. Oligo_trans_STT3. [Graphical view]
KO	K07151.
Pfam	PF02516. STT3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	289661.
SOURCE	Search...

Entry information

Entry name

STT3A_MOUSE

Accession

Primary (citable) accession number: P46978

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	December 14, 2011
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

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

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents