STT3_SCHPO
ID STT3_SCHPO Reviewed; 752 AA.
AC O94335; Q8WZK7;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=SPBC1271.02;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10234787;
RX DOI=10.1002/(sici)1097-0061(199904)15:6<497::aid-yea375>3.0.co;2-u;
RA Yoshida S., Matsuura A., Merregaert J., Anraku Y.;
RT "Schizosaccharomyces pombe stt3+ is a functional homologue of Saccharomyces
RT cerevisiae STT3 which regulates oligosaccharyltransferase activity.";
RL Yeast 15:497-505(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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:P39007}.
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; AB015232; BAA76479.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA22192.1; -; Genomic_DNA.
DR PIR; T39338; T39338.
DR PIR; T43370; T43370.
DR RefSeq; NP_595148.1; NM_001021056.2.
DR AlphaFoldDB; O94335; -.
DR SMR; O94335; -.
DR BioGRID; 276723; 1.
DR STRING; 4896.SPBC1271.02.1; -.
DR CAZy; GT66; Glycosyltransferase Family 66.
DR MaxQB; O94335; -.
DR PaxDb; O94335; -.
DR EnsemblFungi; SPBC1271.02.1; SPBC1271.02.1:pep; SPBC1271.02.
DR GeneID; 2540190; -.
DR KEGG; spo:SPBC1271.02; -.
DR PomBase; SPBC1271.02; stt3.
DR VEuPathDB; FungiDB:SPBC1271.02; -.
DR eggNOG; KOG2292; Eukaryota.
DR HOGENOM; CLU_009279_1_0_1; -.
DR InParanoid; O94335; -.
DR OMA; VAYSSWY; -.
DR PhylomeDB; O94335; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:O94335; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IGI:PomBase.
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:0043687; P:post-translational protein modification; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IGI:PomBase.
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 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..752
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit stt3"
FT /id="PRO_0000072292"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..125
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 126..144
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 145..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 147..164
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 165..175
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 176..195
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 196..197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 198..212
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 213..217
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 218..234
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 235..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 240..265
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 266..273
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 274..293
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 294..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..362
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 363..385
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 386..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 392..408
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 409..412
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 413..434
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT TOPO_DOM 435..482
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..752
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 550..552
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT MOTIF 53..55
FT /note="DXD motif 1"
FT /evidence="ECO:0000250|UniProtKB:Q5HTX9"
FT MOTIF 173..175
FT /note="DXD motif 2"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT MOTIF 354..357
FT /note="SVSE motif"
FT /evidence="ECO:0000250|UniProtKB:Q5HTX9"
FT MOTIF 550..554
FT /note="WWDYG motif"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT MOTIF 617..624
FT /note="DK motif"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT BINDING 55
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 173
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 175
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 411
FT /ligand="dolichyl diphosphooligosaccharide"
FT /ligand_id="ChEBI:CHEBI:57570"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT BINDING 555
FT /ligand="dolichyl diphosphooligosaccharide"
FT /ligand_id="ChEBI:CHEBI:57570"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 55
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 166
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 357
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT SITE 620
FT /note="Interacts with target acceptor peptide in protein
FT substrate"
FT /evidence="ECO:0000250|UniProtKB:B9KDD4"
FT CARBOHYD 569
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P39007"
FT CONFLICT 399
FT /note="S -> P (in Ref. 1; BAA76479)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="F -> S (in Ref. 1; BAA76479)"
FT /evidence="ECO:0000305"
FT CONFLICT 739..752
FT /note="LRRPAKTNEIPLRV -> SAVLQKLTKFL (in Ref. 1; BAA76479)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 752 AA; 84974 MW; 2ACB97DFE82B10B8 CRC64;
MANSATITSK KGVKSHQKDW KIPLKVLILI CIAVASVSSR LFSVIRYESI IHEFDPWFNF
RASKILVEQG FYNFLNWFDE RSWYPLGRVA GGTLYPGLMV TSGIIFKVLH LLRINVNIRD
VCVLLAPAFS GITAIATYYL ARELKSDACG LLAAAFMGIA PGYTSRSVAG SYDNEAIAIT
LLMSTFALWI KAVKSGSSFW GACTGLLYFY MVTAWGGYVF ITNMIPLHVF VLLLMGRYTS
KLYIAYTTYY VIGTLASMQV PFVGFQPVST SEHMSALGVF GLLQLFAFYN YVKGLVSSKQ
FQILIRFALV CLVGLATVVL FALSSTGVIA PWTGRFYSLW DTNYAKIHIP IIASVSEHQP
PTWSSLFFDL QFLIWLLPVG VYLCFKELRN EHVFIIIYSV LGTYFCGVMV RLVLTLTPCV
CIAAAVAIST LLDTYMGPEV EEDKVSEEAA SAKSKNKKGI FSILSFFTSG SKNIGIYSLL
SRVLVISSTA YFLIMFVYHS SWVTSNAYSS PTVVLSTVLN DGSLMYIDDF REAYDWLRRN
TPYDTKVMSW WDYGYQIAGM ADRITLVDNN TWNNTHIATV GKAMSSPEEK AYPILRKHDV
DYILIIYGGT LGYSSDDMNK FLWMIRISQG LWPDEIVERN FFTPNGEYRT DDAATPTMRE
SLLYKMSYHG AWKLFPPNQG YDRARNQKLP SKDPQLFTIE EAFTTVHHLV RLYKVKKPDT
LGRDLKQVTL FEEGKRKKLR RPAKTNEIPL RV
