STT3_CAEEL
ID STT3_CAEEL Reviewed; 757 AA.
AC P46975;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt-3 {ECO:0000250|UniProtKB:Q8TCJ2};
DE Short=Oligosaccharyl transferase subunit stt-3 {ECO:0000250|UniProtKB:Q8TCJ2};
DE EC=2.4.99.18;
GN Name=stt-3 {ECO:0000312|WormBase:T12A2.2};
GN ORFNames=T12A2.2 {ECO:0000312|WormBase:T12A2.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-559 AND ASN-570, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.;
RT "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT elegans.";
RL Glycobiology 15:952-964(2005).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-559 AND ASN-570, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=23691084; DOI=10.1371/journal.pone.0063687;
RA Stevens J., Spang A.;
RT "N-glycosylation is required for secretion and mitosis in C. elegans.";
RL PLoS ONE 8:E63687-E63687(2013).
CC -!- FUNCTION: Catalytic subunit of the oligosaccharyl transferase (OST)
CC complex that catalyzes the initial transfer of a defined glycan
CC (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-
CC pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr
CC consensus motif in nascent polypeptide chains, the first step in
CC protein N-glycosylation. N-glycosylation occurs cotranslationally and
CC the complex associates with the Sec61 complex at the channel-forming
CC translocon complex that mediates protein translocation across the
CC endoplasmic reticulum (ER). All subunits are required for a maximal
CC enzyme activity. This subunit contains the active site and the acceptor
CC peptide and donor lipid-linked oligosaccharide (LLO) binding pockets.
CC {ECO:0000250|UniProtKB:P39007}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl diphosphooligosaccharide + L-asparaginyl-[protein]
CC = a dolichyl diphosphate + H(+) + N(4)-(oligosaccharide-(1->4)-N-
CC acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)-L-
CC asparaginy-[protein]; Xref=Rhea:RHEA:22980, Rhea:RHEA-COMP:9529,
CC Rhea:RHEA-COMP:12635, Rhea:RHEA-COMP:12804, Rhea:RHEA-COMP:12805,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:50347, ChEBI:CHEBI:57497,
CC ChEBI:CHEBI:57570, ChEBI:CHEBI:132529; EC=2.4.99.18;
CC Evidence={ECO:0000250|UniProtKB:P39007};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:B9KDD4};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:B9KDD4};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P39007}.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC {ECO:0000250|UniProtKB:Q8TCJ2}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P46978}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P39007}.
CC -!- DOMAIN: Despite low primary sequence conservation between eukaryotic
CC catalytic subunits and bacterial and archaeal single subunit OSTs
CC (ssOST), structural comparison revealed several common motifs at
CC spatially equivalent positions, like the DXD motif 1 on the external
CC loop 1 and the DXD motif 2 on the external loop 2 involved in binding
CC of the metal ion cofactor and the carboxamide group of the acceptor
CC asparagine, the conserved Glu residue of the TIXE/SVSE motif on the
CC external loop 5 involved in catalysis, as well as the WWDYG and the
CC DK/MI motifs in the globular domain that define the binding pocket for
CC the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg
CC residue was found to interact with a negatively charged side chain at
CC the -2 position of the sequon. This Arg is conserved in bacterial
CC enzymes and correlates with an extended sequon requirement (Asp-X-Asn-
CC X-Ser/Thr) for bacterial N-glycosylation.
CC {ECO:0000250|UniProtKB:P39007}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knock-down is mostly embryonic
CC lethal. Embryogenesis proceeds more slowly and embryos are osmo-
CC sensitive. {ECO:0000269|PubMed:23691084}.
CC -!- SIMILARITY: Belongs to the STT3 family. {ECO:0000305}.
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DR EMBL; FO080619; CCD65209.1; -; Genomic_DNA.
DR PIR; T34351; T34351.
DR RefSeq; NP_498362.1; NM_065961.3.
DR AlphaFoldDB; P46975; -.
DR SMR; P46975; -.
DR BioGRID; 41106; 17.
DR ComplexPortal; CPX-968; Oligosaccharyl transferase complex.
DR DIP; DIP-24951N; -.
DR STRING; 6239.T12A2.2.3; -.
DR CAZy; GT66; Glycosyltransferase Family 66.
DR iPTMnet; P46975; -.
DR EPD; P46975; -.
DR PaxDb; P46975; -.
DR PeptideAtlas; P46975; -.
DR PRIDE; P46975; -.
DR EnsemblMetazoa; T12A2.2.1; T12A2.2.1; WBGene00020437.
DR EnsemblMetazoa; T12A2.2.2; T12A2.2.2; WBGene00020437.
DR GeneID; 175886; -.
DR KEGG; cel:CELE_T12A2.2; -.
DR UCSC; T12A2.2.2; c. elegans.
DR CTD; 175886; -.
DR WormBase; T12A2.2; CE01395; WBGene00020437; stt-3.
DR eggNOG; KOG2292; Eukaryota.
DR GeneTree; ENSGT00940000155488; -.
DR HOGENOM; CLU_009279_1_0_1; -.
DR InParanoid; P46975; -.
DR OMA; TKELWSP; -.
DR OrthoDB; 187775at2759; -.
DR PhylomeDB; P46975; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:P46975; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00020437; Expressed in embryo and 4 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IC:ComplexPortal.
DR GO; GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043687; P:post-translational protein modification; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IC:ComplexPortal.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
DR InterPro; IPR003674; Oligo_trans_STT3.
DR PANTHER; PTHR13872; PTHR13872; 1.
DR Pfam; PF02516; STT3; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Magnesium;
KW Manganese; Membrane; Metal-binding; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..757
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit stt-3"
FT /id="PRO_0000072289"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..121
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 122..140
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 141..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 143..160
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 161..171
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 172..191
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 192..193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 194..208
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 209..210
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 211..235
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TRANSMEM 236..261
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 262..269
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 270..289
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 290..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..358
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 359..381
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 382..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 388..404
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 405..408
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 409..430
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 431..469
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 470..495
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 496..757
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 547..549
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT REGION 721..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 49..51
FT /note="DXD motif 1"
FT /evidence="ECO:0000250|UniProtKB:Q5HTX9"
FT MOTIF 169..171
FT /note="DXD motif 2"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT MOTIF 350..353
FT /note="SVSE motif"
FT /evidence="ECO:0000250|UniProtKB:Q5HTX9"
FT MOTIF 547..551
FT /note="WWDYG motif"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT MOTIF 614..621
FT /note="DK motif"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT BINDING 51
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 169
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 171
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 407
FT /ligand="dolichyl diphosphooligosaccharide"
FT /ligand_id="ChEBI:CHEBI:57570"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 552
FT /ligand="dolichyl diphosphooligosaccharide"
FT /ligand_id="ChEBI:CHEBI:57570"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 51
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 162
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 353
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 617
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT CARBOHYD 559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 570
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 757 AA; 85122 MW; A6BF0BB019B6C4FF CRC64;
MTSTTAARTA SSRVGATTLL TIVVLALAWF VGFASRLFAI VRFESIIHEF DPWFNYRATH
HMVQHGFYKF LNWFDERAWY PLGRIVGGTV YPGLMVTSGL IHWILDSLNF HVHIREVCVF
LAPTFSGLTA IATYLLTKEL WSPGAGLFAA CFIAISPGYT SRSVAGSYDN EGIAIFALQF
TYYLWVKSLK TGSIMWASLC ALSYFYMVSA WGGYVFIINL IPLHALALII MGRYSSRLFV
SYTSFYCLAT ILSMQVPFVG FQPVRTSEHM PAFGVFGLLQ IVALMHYARN RITRQQFMTL
FVGGLTILGA LSVVVYFALV WGGYVAPFSG RFYSLWDTGY AKIHIPIIAS VSEHQPTTWV
SFFFDLHITA AVFPVGLWYC IKKVNDERVF IILYAVSAVY FAGVMVRLML TLTPAVCVLA
GIGFSYTFEK YLKDEETKER SSSQSGTTKD EKLYDKAAKN VKSRNANDGD ESGVSSNVRT
IISIILVIFL LMFVVHATYV TSNAYSHPSV VLQSSTNNGD RIIMDDFREA YHWLRENTAD
DARVMSWWDY GYQIAGMANR TTLVDNNTWN NSHIALVGKA MSSNESAAYE IMTELDVDYI
LVIFGGVIGY SGDDINKFLW MVRIAQGEHP KDIREENYFT STGEYSTGAG ASETMLNCLM
YKMSYYRFGE TRVGYNQAGG FDRTRGYVIG KKDITLEYIE EAYTTENWLV RIYKRKKLPN
RPTVKSEEAT IPIKGKKATQ GKNKKGVIRP APTASKA
