OST48_DROME
ID OST48_DROME Reviewed; 449 AA.
AC Q24319; Q24355; Q9W382;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit;
DE Short=DDOST 48 kDa subunit;
DE Short=Oligosaccharyl transferase 48 kDa subunit;
DE AltName: Full=DmOST50;
DE Short=DrOST;
DE AltName: Full=OST5OP;
DE Flags: Precursor;
GN Name=Ost48; Synonyms=OST50; ORFNames=CG9022;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7607543; DOI=10.1016/0378-1119(95)00172-3;
RA Stagljar I., Te Heesen S., Aebi M.;
RT "PCR-mediated cloning and sequencing of the DmOST50 gene, a
RT WBP1/AvOST50/OST48 homologue, from Drosophila melanogaster.";
RL Gene 158:209-212(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 119-449.
RX PubMed=7557364; DOI=10.1139/g95-075;
RA Akhmanova A.S., Bindels P.S.T., Xu J., Miedema K., Kremer H., Hennig W.;
RT "Structure and expression of histone H3.3 genes in Drosophila melanogaster
RT and Drosophila hydei.";
RL Genome 38:586-600(1995).
CC -!- FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that
CC 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 (By similarity). Required for the assembly of both
CC SST3A- and SS3B-containing OST complexes (By similarity).
CC {ECO:0000250|UniProtKB:P39656, ECO:0000250|UniProtKB:Q05052}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC {ECO:0000250|UniProtKB:Q05052}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DDOST 48 kDa subunit family. {ECO:0000305}.
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DR EMBL; X81999; CAA57525.1; -; mRNA.
DR EMBL; AE014298; AAF46453.1; -; Genomic_DNA.
DR EMBL; BT010050; AAQ22519.1; -; mRNA.
DR EMBL; X81207; CAA57079.1; -; Genomic_DNA.
DR PIR; JC4132; JC4132.
DR RefSeq; NP_511096.2; NM_078541.4.
DR AlphaFoldDB; Q24319; -.
DR SMR; Q24319; -.
DR BioGRID; 58304; 78.
DR STRING; 7227.FBpp0071279; -.
DR PaxDb; Q24319; -.
DR PRIDE; Q24319; -.
DR DNASU; 31849; -.
DR EnsemblMetazoa; FBtr0071344; FBpp0071279; FBgn0014868.
DR GeneID; 31849; -.
DR KEGG; dme:Dmel_CG9022; -.
DR CTD; 31849; -.
DR FlyBase; FBgn0014868; Ost48.
DR VEuPathDB; VectorBase:FBgn0014868; -.
DR eggNOG; KOG2754; Eukaryota.
DR GeneTree; ENSGT00390000017294; -.
DR HOGENOM; CLU_031804_0_0_1; -.
DR InParanoid; Q24319; -.
DR OMA; YQFKVDY; -.
DR OrthoDB; 975158at2759; -.
DR PhylomeDB; Q24319; -.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 31849; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 31849; -.
DR PRO; PR:Q24319; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0014868; Expressed in embryonic/larval hemocyte (Drosophila) and 50 other tissues.
DR Genevisible; Q24319; DM.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IBA:GO_Central.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
DR InterPro; IPR005013; DDOST_48_kDa_subunit.
DR PANTHER; PTHR10830; PTHR10830; 1.
DR Pfam; PF03345; DDOST_48kD; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..449
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase 48 kDa subunit"
FT /id="PRO_0000021956"
FT TOPO_DOM 19..412
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 434..449
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 94
FT /note="R -> A (in Ref. 1; CAA57525)"
FT /evidence="ECO:0000305"
FT CONFLICT 148..149
FT /note="EH -> DD (in Ref. 5; CAA57079)"
FT /evidence="ECO:0000305"
FT CONFLICT 175..176
FT /note="AA -> R (in Ref. 5; CAA57079)"
FT /evidence="ECO:0000305"
FT CONFLICT 225..226
FT /note="LL -> VV (in Ref. 5; CAA57079)"
FT /evidence="ECO:0000305"
FT CONFLICT 287..289
FT /note="RLR -> QVG (in Ref. 5; CAA57079)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="R -> V (in Ref. 1; CAA57525)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="P -> T (in Ref. 5; CAA57079)"
FT /evidence="ECO:0000305"
FT CONFLICT 329..330
FT /note="RA -> AR (in Ref. 1; CAA57525)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="D -> A (in Ref. 5; CAA57079)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 449 AA; 49981 MW; E4BC30AF376DCCD9 CRC64;
MMWKALLIAV LAIAHCQAVL ETDANTLVLL DNLAIRETHS IFFKSLQDRG FKLTYKLADD
SSLLLSKYGE YLYKNVIIFA PSVEEFGGDV SVERLAQFVD DGGNVLVAGS EKSGDALREF
ASECGFELDE ENAAVIDHLH YDVSDAGEHT TILTSAKNLI QADTIVGKAN RQADAAPLLY
RGTGLIADKE NPLVLKLLTA ESTAYSYNPE ASVSDYPHAV GRGTLLIAAL QARNNARVVF
SGSLLFFSDE SFTTAVQYAQ SGVFHKLAGN RDVAESISKW VFGETGRLRV ASVQHHKEGE
LLPPDQAYTI TDPVVYTIGI EELVQGEWRA FKASDIQLEF VRIDPFVRTY LKQTNTGAYQ
AKFKIPDVYG VYQFKVDYNR VGYTHLYSTT QVSVRPLEHT QYERFIPSAF PYYTSAFSMM
IGVFVFSFVF LHFKDEPVGR AAKEDKKSQ
