TM258_DROME
ID TM258_DROME Reviewed; 78 AA.
AC Q9VVA8;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Transmembrane protein 258 {ECO:0000305};
DE AltName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TMEM258;
DE Short=Oligosaccharyl transferase subunit TMEM258;
DE AltName: Full=Protein kuduk {ECO:0000305|PubMed:28716842};
DE AltName: Full=Transmembrane protein 258 homolog;
GN Name=kud {ECO:0000303|PubMed:28716842, ECO:0000312|FlyBase:FBgn0036667};
GN ORFNames=CG9669;
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 [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 [2]
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 [3]
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TOPOLOGY, FUNCTION, INTERACTION
RP WITH KLAR AND MSP300, AND SUBUNIT.
RX PubMed=28716842; DOI=10.1083/jcb.201606043;
RA Ding Z.Y., Wang Y.H., Huang Y.C., Lee M.C., Tseng M.J., Chi Y.H.,
RA Huang M.L.;
RT "Outer nuclear membrane protein Kuduk modulates the LINC complex and
RT nuclear envelope architecture.";
RL J. Cell Biol. 216:2827-2841(2017).
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). In addition may regulates nuclear
CC envelope (NE) architecture and nuclear positioning through the linker
CC of nucleoskeleton and cytoskeleton (LINC)-dependent and -independent
CC mechanisms (PubMed:28716842). {ECO:0000250|UniProtKB:P61165,
CC ECO:0000269|PubMed:28716842}.
CC -!- SUBUNIT: Homodimer (PubMed:28716842). Component of the
CC oligosaccharyltransferase (OST) complex (By similarity). Interacts with
CC klar and Msp300, components of LINC complex (PubMed:28716842).
CC {ECO:0000250|UniProtKB:P61165, ECO:0000269|PubMed:28716842}.
CC -!- SUBCELLULAR LOCATION: Nucleus outer membrane
CC {ECO:0000269|PubMed:28716842}; Multi-pass membrane protein
CC {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:28716842}. Endoplasmic
CC reticulum membrane {ECO:0000269|PubMed:28716842}.
CC -!- DISRUPTION PHENOTYPE: Homozygous mutants display growth retardation and
CC dy as larvae and show defects in ovarian follicle cells, which enwrap
CC the germ cell clusters in ovarioles. {ECO:0000269|PubMed:28716842}.
CC -!- SIMILARITY: Belongs to the OST5 family. {ECO:0000305}.
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DR EMBL; AE014296; AAF49405.1; -; Genomic_DNA.
DR RefSeq; NP_001246807.1; NM_001259878.1.
DR RefSeq; NP_648925.1; NM_140668.3.
DR AlphaFoldDB; Q9VVA8; -.
DR SMR; Q9VVA8; -.
DR BioGRID; 65181; 3.
DR DIP; DIP-22543N; -.
DR IntAct; Q9VVA8; 1.
DR STRING; 7227.FBpp0075098; -.
DR PaxDb; Q9VVA8; -.
DR EnsemblMetazoa; FBtr0075339; FBpp0075098; FBgn0036667.
DR EnsemblMetazoa; FBtr0305272; FBpp0293796; FBgn0036667.
DR GeneID; 39882; -.
DR KEGG; dme:Dmel_CG9669; -.
DR UCSC; CG9669-RA; d. melanogaster.
DR CTD; 39882; -.
DR FlyBase; FBgn0036667; CG9669.
DR VEuPathDB; VectorBase:FBgn0036667; -.
DR eggNOG; KOG4452; Eukaryota.
DR GeneTree; ENSGT00390000010089; -.
DR HOGENOM; CLU_180449_0_0_1; -.
DR InParanoid; Q9VVA8; -.
DR OMA; MERYVGP; -.
DR OrthoDB; 1627291at2759; -.
DR PhylomeDB; Q9VVA8; -.
DR BioGRID-ORCS; 39882; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 39882; -.
DR PRO; PR:Q9VVA8; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036667; Expressed in eye disc (Drosophila) and 27 other tissues.
DR ExpressionAtlas; Q9VVA8; baseline and differential.
DR Genevisible; Q9VVA8; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0031309; C:integral component of nuclear outer membrane; IDA:FlyBase.
DR GO; GO:0043227; C:membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005640; C:nuclear outer membrane; IDA:UniProtKB.
DR GO; GO:0034998; C:oligosaccharyltransferase I complex; IEA:InterPro.
DR GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
DR GO; GO:0006998; P:nuclear envelope organization; IMP:UniProtKB.
DR GO; GO:0007097; P:nuclear migration; IMP:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; IEA:InterPro.
DR InterPro; IPR007915; TMEM258/Ost5.
DR PANTHER; PTHR13636; PTHR13636; 1.
DR Pfam; PF05251; Ost5; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endoplasmic reticulum; Membrane; Nucleus; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..78
FT /note="Transmembrane protein 258"
FT /id="PRO_0000221145"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:28716842"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:28716842"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..78
FT /note="Perinuclear space"
FT /evidence="ECO:0000305|PubMed:28716842"
SQ SEQUENCE 78 AA; 8717 MW; E6CAD5AC720DE90C CRC64;
MDVMQRYVSP VNPAVFPHLA TVLLVIGTFF TAWFFIFVVS RKSSKESTLI KELLISLCAS
IFLGFGIVFL LLTVGIYV
