ID   A4RXM8_OSTLU            Unreviewed;       743 AA.
AC   A4RXM8;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   02-SEP-2026, entry version 91.
DE   RecName: Full=dolichyl-diphosphooligosaccharide--protein glycotransferase {ECO:0000256|ARBA:ARBA00012605};
DE            EC=2.4.99.18 {ECO:0000256|ARBA:ARBA00012605};
GN   ORFNames=OSTLU_49512 {ECO:0000313|EMBL:ABO96075.1};
OS   Ostreococcus lucimarinus (strain CCE9901).
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Ostreococcus.
OX   NCBI_TaxID=436017 {ECO:0000313|EMBL:ABO96075.1, ECO:0000313|Proteomes:UP000001568};
RN   [1] {ECO:0000313|EMBL:ABO96075.1, ECO:0000313|Proteomes:UP000001568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCE9901 {ECO:0000313|EMBL:ABO96075.1,
RC   ECO:0000313|Proteomes:UP000001568};
RX   PubMed=17460045; DOI=10.1073/pnas.0611046104;
RA   Palenik B., Grimwood J., Aerts A., Rouze P., Salamov A., Putnam N.,
RA   Dupont C., Jorgensen R., Derelle E., Rombauts S., Zhou K., Otillar R.,
RA   Merchant S.S., Podell S., Gaasterland T., Napoli C., Gendler K.,
RA   Manuell A., Tai V., Vallon O., Piganeau G., Jancek S., Heijde M.,
RA   Jabbari K., Bowler C., Lohr M., Robbens S., Werner G., Dubchak I.,
RA   Pazour G.J., Ren Q., Paulsen I., Delwiche C., Schmutz J., Rokhsar D.,
RA   Van de Peer Y., Moreau H., Grigoriev I.V.;
RT   "The tiny eukaryote Ostreococcus provides genomic insights into the paradox
RT   of plankton speciation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7705-7710(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a di-trans,poly-cis-dolichyl diphosphooligosaccharide + L-
CC         asparaginyl-[protein] = N(4)-(oligosaccharide-(1->4)-N-acetyl-beta-D-
CC         glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)-L-asparaginyl-
CC         [protein] + a di-trans,poly-cis-dolichyl diphosphate + H(+);
CC         Xref=Rhea:RHEA:22980, Rhea:RHEA-COMP:12804, Rhea:RHEA-COMP:12805,
CC         Rhea:RHEA-COMP:19506, Rhea:RHEA-COMP:19509, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:50347, ChEBI:CHEBI:57497, ChEBI:CHEBI:57570,
CC         ChEBI:CHEBI:132529; EC=2.4.99.18;
CC         Evidence={ECO:0000256|ARBA:ARBA00048829};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
CC   -!- SUBCELLULAR LOCATION: Endomembrane system
CC       {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004127}.
CC   -!- SIMILARITY: Belongs to the STT3 family.
CC       {ECO:0000256|ARBA:ARBA00010810}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000585; ABO96075.1; -; Genomic_DNA.
DR   RefSeq; XP_001417782.1; XM_001417745.1.
DR   AlphaFoldDB; A4RXM8; -.
DR   SMR; A4RXM8; -.
DR   STRING; 436017.A4RXM8; -.
DR   GeneID; 5001872; -.
DR   Gramene; ABO96075; ABO96075; OSTLU_49512.
DR   KEGG; olu:OSTLU_49512; -.
DR   eggNOG; KOG2292; Eukaryota.
DR   HOGENOM; CLU_009279_0_0_1; -.
DR   OMA; MMRIYRV; -.
DR   OrthoDB; 10261066at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000001568; Chromosome 5.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009101; P:glycoprotein biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.12610; -; 1.
DR   InterPro; IPR003674; Oligo_trans_STT3.
DR   InterPro; IPR048999; STT3-PglB_core.
DR   InterPro; IPR048307; STT3_N.
DR   PANTHER; PTHR13872; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE SUBUNIT; 1.
DR   PANTHER; PTHR13872:SF1; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE SUBUNIT STT3B; 1.
DR   Pfam; PF02516; STT3; 1.
DR   Pfam; PF21436; STT3-PglB_core; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001568};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        79..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        110..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        135..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        204..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        238..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        301..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        368..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        409..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          15..413
FT                   /note="Oligosaccharyl transferase STT3 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02516"
FT   DOMAIN          527..582
FT                   /note="STT3/PglB/AglB core"
FT                   /evidence="ECO:0000259|Pfam:PF21436"
FT   REGION          444..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   743 AA;  82273 MW;  A24581E6C16FAED4 CRC64;
     MQRLIDLSLG GFVRAIALAI AVYAAVDIRL YAVRDYGRII HEFDPWFNYR ATVYLADNGW
     SKFKTWFDYM SWYPLGRPVG TTIYPGMQIT AVFLWRVFNA IGLKMSLNDV CVFFPAYFAA
     VATFLVALLT KECSGSGTGA VVAALVMAIV PAHTMRSVAG GYDNESLAVT AMCLTFYTWC
     RALRTPKSWW VGGLAGLAYT YMVAAWGGYT FVLNMVGLHA AVLVLYKRYS SSLYKAYSLF
     FVVGTIGALQ FPVVGTLPFT SAEQLGPMGV FLGFQVLEFV ERTMKPGMES REKWQRRIRM
     YTLAFAAAIG AITVLSATGV YNINGLSVRV KSLFIKHTKT GNPLVDSVAE HQPGNADSYY
     RFLHFNYFIA PIGFCFSVVH FMFDGSAGAL FLPLYGLVAY YFANRMVRLI IFLGPVAACL
     VGVCIGYAIE DALSIMRNDD IEQAETPSET ETPKSAKKKS KQAAYKKPEP LSVTVKRDMT
     KWWMSSTGMS QPSIMFKGQL NDGRTVMVKD YVEAYDWLRT QTPEDARVMA WWDYGYQITG
     IGNRTSIADG NTWNHEHIAN LARMLTSDEA KAHKVIRHLA DYVLVWAGGG GDDMAKSPHL
     FRIGASIGSG RATAVEMEKI TSTFGVDRSG RPTPKMASSL LFKLVSPQGS VSPEHFREVY
     TSKYRKVRIY EVVNVDEGSK AWVADPANRM CDNADGTGFC PGAYPPALKK FPSIIKPAYK
     VPAWIKAKRA AAKSAKSAAK DEL
//