STT3_DICDI
ID STT3_DICDI Reviewed; 714 AA.
AC Q54NM9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3;
DE Short=Oligosaccharyl transferase subunit STT3;
DE EC=2.4.99.18;
GN Name=stt3; ORFNames=DDB_G0285159;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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}.
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 -!- SIMILARITY: Belongs to the STT3 family. {ECO:0000305}.
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DR EMBL; AAFI02000074; EAL64892.1; -; Genomic_DNA.
DR RefSeq; XP_639887.1; XM_634795.1.
DR AlphaFoldDB; Q54NM9; -.
DR SMR; Q54NM9; -.
DR STRING; 44689.DDB0230191; -.
DR PaxDb; Q54NM9; -.
DR PRIDE; Q54NM9; -.
DR EnsemblProtists; EAL64892; EAL64892; DDB_G0285159.
DR GeneID; 8624958; -.
DR KEGG; ddi:DDB_G0285159; -.
DR dictyBase; DDB_G0285159; stt3.
DR eggNOG; KOG2292; Eukaryota.
DR HOGENOM; CLU_009279_1_0_1; -.
DR InParanoid; Q54NM9; -.
DR OMA; VAYSSWY; -.
DR PhylomeDB; Q54NM9; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q54NM9; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; ISS:dictyBase.
DR GO; GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISS:dictyBase.
DR InterPro; IPR003674; Oligo_trans_STT3.
DR PANTHER; PTHR13872; PTHR13872; 1.
DR Pfam; PF02516; STT3; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Magnesium;
KW Manganese; Membrane; Metal-binding; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..714
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit STT3"
FT /id="PRO_0000328633"
FT TOPO_DOM 1..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..143
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 144..162
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 163..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 165..182
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 183..193
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 194..213
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 214..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 216..230
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 231..235
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 236..252
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 253..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 258..283
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 284..291
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 292..311
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 312..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..380
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 381..403
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 404..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 410..426
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 427..430
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 431..452
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 453..466
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 467..489
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 490..714
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 541..543
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT MOTIF 71..73
FT /note="DXD motif 1"
FT /evidence="ECO:0000250|UniProtKB:Q5HTX9"
FT MOTIF 191..193
FT /note="DXD motif 2"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT MOTIF 372..375
FT /note="SVSE motif"
FT /evidence="ECO:0000250|UniProtKB:Q5HTX9"
FT MOTIF 541..545
FT /note="WWDYG motif"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT MOTIF 608..615
FT /note="DK motif"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT BINDING 73
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 191
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 193
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 429
FT /ligand="dolichyl diphosphooligosaccharide"
FT /ligand_id="ChEBI:CHEBI:57570"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 546
FT /ligand="dolichyl diphosphooligosaccharide"
FT /ligand_id="ChEBI:CHEBI:57570"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 73
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 184
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 375
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 611
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT CARBOHYD 553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P39007"
SQ SEQUENCE 714 AA; 80546 MW; 5C21BBCEC770B656 CRC64;
MKRSEKSSTS VVSNNKQQDV NIISSNEVGV KEENKGHQEF LLKVLILSVI YVLAFSTRLF
SVLRYESVIH EFDPYFNYRS TIYLVQEGFY NFLNWFDERA WYPLGRIVGG TIYPGLMATA
SLVHWSLNSL NITVNIRNVC VLLSPWFASN TAMVTYKFAK EVKDTQTGLV AAAMIAIVPG
YISRSVAGSF DNEGIAIFAL IFTYYCWIKS VNTGSLMWAA ICSLAYFYMA SAWGGYVFII
NLIPLHAFFL LLTGRYSHRL YIAYSTMFVI GTILSMQITF ISFQPVQSSE HLAAIGIFGL
LQLYAGLSWV KSHLTNEAFK KLQRLTVLFV LSCAAAVLVV GTLTGYISPF NGRFYSLLDP
TYARDHIPII ASVSEHQPTT WASYFFDLHI LVFLFPAGLY FCFQKLTDAN IFLILYGVTS
IYFSGVMVRL MLVLAPVACI LAAVAVSATL TTYMKKLKAP SSPSDANNSK ESGGVMVAVL
TVLLILYAFH CTWVTSEAYS SPSIVLSAKQ NDGSRVIFDD FREAYRWIGQ NTADDARIMS
WWDYGYQLSA MANRTVLVDN NTWNNSHIAQ VGKAFASTEE DAYIQMKALD VDYVLVIFGG
LTGYSSDDIN KFLWMVRIGG SCDPNIKEQD YLTNGQYRID KGASPTMLNS LMYKLSYYRF
SEVHTDYQRP TGFDRVRNVE IGNKNFDLTY LEEAFTSVHW LVRVYKVKDF DNRA
