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Protein

Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt-3

Gene

stt-3

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc3Man9GlcNAc2 in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-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 enzyme activity. This subunit contains the active site and the acceptor peptide and donor lipid-linked oligosaccharide (LLO) binding pockets.By similarity

Catalytic activityi

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.By similarity

Cofactori

Mg2+By similarity, Mn2+By similarity

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.By similarity
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi51ManganeseBy similarity1
Binding sitei51Target acceptor peptideBy similarity1
Sitei162Important for catalytic activityBy similarity1
Metal bindingi169ManganeseBy similarity1
Metal bindingi171ManganeseBy similarity1
Binding sitei353Target acceptor peptideBy similarity1
Binding sitei407Lipid-linked oligosaccharideBy similarity1
Binding sitei552Lipid-linked oligosaccharideBy similarity1
Binding sitei617Target acceptor peptideBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosyltransferase, Transferase
LigandMagnesium, Metal-binding

Enzyme and pathway databases

SignaLinkiP46975
UniPathwayi
UPA00378

Protein family/group databases

CAZyiGT66 Glycosyltransferase Family 66

Names & Taxonomyi

Protein namesi
Recommended name:
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt-3By similarity (EC:2.4.99.18)
Short name:
Oligosaccharyl transferase subunit stt-3By similarity
Gene namesi
Name:stt-3Imported
ORF Names:T12A2.2Imported
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome III

Organism-specific databases

WormBaseiT12A2.2 ; CE01395 ; WBGene00020437 ; stt-3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 13CytoplasmicCuratedAdd BLAST13
Transmembranei14 – 34HelicalSequence analysisAdd BLAST21
Topological domaini35 – 121LumenalCuratedAdd BLAST87
Transmembranei122 – 140HelicalBy similarityAdd BLAST19
Topological domaini141 – 142CytoplasmicCurated2
Transmembranei143 – 160HelicalBy similarityAdd BLAST18
Topological domaini161 – 171LumenalCuratedAdd BLAST11
Transmembranei172 – 191HelicalBy similarityAdd BLAST20
Topological domaini192 – 193CytoplasmicCurated2
Transmembranei194 – 208HelicalBy similarityAdd BLAST15
Topological domaini209 – 210LumenalCurated2
Transmembranei211 – 235HelicalBy similarityAdd BLAST25
Transmembranei236 – 261HelicalBy similarityAdd BLAST26
Topological domaini262 – 269LumenalCurated8
Transmembranei270 – 289HelicalBy similarityAdd BLAST20
Topological domaini290 – 299CytoplasmicCurated10
Transmembranei300 – 320HelicalSequence analysisAdd BLAST21
Topological domaini321 – 358LumenalCuratedAdd BLAST38
Transmembranei359 – 381HelicalBy similarityAdd BLAST23
Topological domaini382 – 387CytoplasmicCurated6
Transmembranei388 – 404HelicalBy similarityAdd BLAST17
Topological domaini405 – 408LumenalCurated4
Transmembranei409 – 430HelicalBy similarityAdd BLAST22
Topological domaini431 – 469CytoplasmicCuratedAdd BLAST39
Transmembranei470 – 495HelicalBy similarityAdd BLAST26
Topological domaini496 – 757LumenalCuratedAdd BLAST262

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

RNAi-mediated knock-down is mostly embryonic lethal. Embryogenesis proceeds more slowly and embryos are osmo-sensitive.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000722891 – 757Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt-3Add BLAST757

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi559N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi566N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi570N-linked (GlcNAc...) (high mannose) asparagine2 Publications1
Glycosylationi584N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiP46975
PaxDbiP46975
PeptideAtlasiP46975
PRIDEiP46975

PTM databases

iPTMnetiP46975

Expressioni

Gene expression databases

BgeeiWBGene00020437 Expressed in 5 organ(s), highest expression level in multi-cellular organism

Interactioni

Subunit structurei

Component of the oligosaccharyltransferase (OST) complex.By similarity

Protein-protein interaction databases

BioGridi41106, 1 interactor
ComplexPortaliCPX-968 Oligosaccharyl transferase complex
DIPiDIP-24951N
STRINGi6239.T12A2.2.2

Structurei

3D structure databases

ProteinModelPortaliP46975
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni547 – 549Target acceptor peptide bindingBy similarity3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi49 – 51DXD motif 1By similarity3
Motifi169 – 171DXD motif 2By similarity3
Motifi350 – 353SVSE motifBy similarity4
Motifi547 – 551WWDYG motifBy similarity5
Motifi614 – 621DK motifBy similarity8

Domaini

Despite low primary sequence conservation between eukaryotic catalytic subunits and bacterial and archaeal single subunit OSTs (ssOST), structural comparison revealed several common motifs at spatially equivalent positions, like the DXD motif 1 on the external loop 1 and the DXD motif 2 on the external loop 2 involved in binding of the metal ion cofactor and the carboxamide group of the acceptor asparagine, the conserved Glu residue of the TIXE/SVSE motif on the external loop 5 involved in catalysis, as well as the WWDYG and the DK/MI motifs in the globular domain that define the binding pocket for the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg residue was found to interact with a negatively charged side chain at the -2 position of the sequon. This Arg is conserved in bacterial enzymes and correlates with an extended sequon requirement (Asp-X-Asn-X-Ser/Thr) for bacterial N-glycosylation.By similarity

Sequence similaritiesi

Belongs to the STT3 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2292 Eukaryota
COG1287 LUCA
GeneTreeiENSGT00390000015238
HOGENOMiHOG000157471
InParanoidiP46975
KOiK07151
OMAiNYRATAY
OrthoDBiEOG091G02DB
PhylomeDBiP46975

Family and domain databases

InterProiView protein in InterPro
IPR003674 Oligo_trans_STT3
PfamiView protein in Pfam
PF02516 STT3, 1 hit

Sequencei

Sequence statusi: Complete.

P46975-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTSTTAARTA SSRVGATTLL TIVVLALAWF VGFASRLFAI VRFESIIHEF
60 70 80 90 100
DPWFNYRATH HMVQHGFYKF LNWFDERAWY PLGRIVGGTV YPGLMVTSGL
110 120 130 140 150
IHWILDSLNF HVHIREVCVF LAPTFSGLTA IATYLLTKEL WSPGAGLFAA
160 170 180 190 200
CFIAISPGYT SRSVAGSYDN EGIAIFALQF TYYLWVKSLK TGSIMWASLC
210 220 230 240 250
ALSYFYMVSA WGGYVFIINL IPLHALALII MGRYSSRLFV SYTSFYCLAT
260 270 280 290 300
ILSMQVPFVG FQPVRTSEHM PAFGVFGLLQ IVALMHYARN RITRQQFMTL
310 320 330 340 350
FVGGLTILGA LSVVVYFALV WGGYVAPFSG RFYSLWDTGY AKIHIPIIAS
360 370 380 390 400
VSEHQPTTWV SFFFDLHITA AVFPVGLWYC IKKVNDERVF IILYAVSAVY
410 420 430 440 450
FAGVMVRLML TLTPAVCVLA GIGFSYTFEK YLKDEETKER SSSQSGTTKD
460 470 480 490 500
EKLYDKAAKN VKSRNANDGD ESGVSSNVRT IISIILVIFL LMFVVHATYV
510 520 530 540 550
TSNAYSHPSV VLQSSTNNGD RIIMDDFREA YHWLRENTAD DARVMSWWDY
560 570 580 590 600
GYQIAGMANR TTLVDNNTWN NSHIALVGKA MSSNESAAYE IMTELDVDYI
610 620 630 640 650
LVIFGGVIGY SGDDINKFLW MVRIAQGEHP KDIREENYFT STGEYSTGAG
660 670 680 690 700
ASETMLNCLM YKMSYYRFGE TRVGYNQAGG FDRTRGYVIG KKDITLEYIE
710 720 730 740 750
EAYTTENWLV RIYKRKKLPN RPTVKSEEAT IPIKGKKATQ GKNKKGVIRP

APTASKA
Length:757
Mass (Da):85,122
Last modified:November 1, 1995 - v1
Checksum:iA6BF0BB019B6C4FF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO080619 Genomic DNA Translation: CCD65209.1
PIRiT34351
RefSeqiNP_498362.1, NM_065961.3
UniGeneiCel.17422

Genome annotation databases

EnsemblMetazoaiT12A2.2.1; T12A2.2.1; WBGene00020437
T12A2.2.2; T12A2.2.2; WBGene00020437
GeneIDi175886
KEGGicel:CELE_T12A2.2
UCSCiT12A2.2.2 c. elegans

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO080619 Genomic DNA Translation: CCD65209.1
PIRiT34351
RefSeqiNP_498362.1, NM_065961.3
UniGeneiCel.17422

3D structure databases

ProteinModelPortaliP46975
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi41106, 1 interactor
ComplexPortaliCPX-968 Oligosaccharyl transferase complex
DIPiDIP-24951N
STRINGi6239.T12A2.2.2

Protein family/group databases

CAZyiGT66 Glycosyltransferase Family 66

PTM databases

iPTMnetiP46975

Proteomic databases

EPDiP46975
PaxDbiP46975
PeptideAtlasiP46975
PRIDEiP46975

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiT12A2.2.1; T12A2.2.1; WBGene00020437
T12A2.2.2; T12A2.2.2; WBGene00020437
GeneIDi175886
KEGGicel:CELE_T12A2.2
UCSCiT12A2.2.2 c. elegans

Organism-specific databases

CTDi175886
WormBaseiT12A2.2 ; CE01395 ; WBGene00020437 ; stt-3

Phylogenomic databases

eggNOGiKOG2292 Eukaryota
COG1287 LUCA
GeneTreeiENSGT00390000015238
HOGENOMiHOG000157471
InParanoidiP46975
KOiK07151
OMAiNYRATAY
OrthoDBiEOG091G02DB
PhylomeDBiP46975

Enzyme and pathway databases

UniPathwayi
UPA00378

SignaLinkiP46975

Miscellaneous databases

PROiPR:P46975

Gene expression databases

BgeeiWBGene00020437 Expressed in 5 organ(s), highest expression level in multi-cellular organism

Family and domain databases

InterProiView protein in InterPro
IPR003674 Oligo_trans_STT3
PfamiView protein in Pfam
PF02516 STT3, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiSTT3_CAEEL
AccessioniPrimary (citable) accession number: P46975
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 10, 2018
This is version 126 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
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Main funding by: National Institutes of Health

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