ALG5_DROME
ID ALG5_DROME Reviewed; 326 AA.
AC Q9VLQ1;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Dolichyl-phosphate beta-glucosyltransferase {ECO:0000250|UniProtKB:Q9Y673};
DE EC=2.4.1.117 {ECO:0000250|UniProtKB:Q9Y673};
DE AltName: Full=Wollknaeuel {ECO:0000312|EMBL:AAF52633.1};
GN Name=wol; Synonyms=alg5 {ECO:0000303|PubMed:21199819}; ORFNames=CG7870;
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] {ECO:0000312|EMBL:AAF52633.1}
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] {ECO:0000312|EMBL:AAF52633.1}
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] {ECO:0000312|EMBL:AAM11045.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Head {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP ARG-209.
RX PubMed=18403407; DOI=10.1242/dev.020891;
RA Haecker A., Bergman M., Neupert C., Moussian B., Luschnig S., Aebi M.,
RA Mannervik M.;
RT "Wollknauel is required for embryo patterning and encodes the Drosophila
RT ALG5 UDP-glucose:dolichyl-phosphate glucosyltransferase.";
RL Development 135:1745-1749(2008).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21199819; DOI=10.1093/glycob/cwq213;
RA Shaik K.S., Pabst M., Schwarz H., Altmann F., Moussian B.;
RT "The Alg5 ortholog Wollknauel is essential for correct epidermal
RT differentiation during Drosophila late embryogenesis.";
RL Glycobiology 21:743-756(2011).
CC -!- FUNCTION: Required for normal production of N-glycosylated proteins in
CC the endoplasmic reticulum (ER). Required for embryonic segmentation,
CC dorsal-ventral patterning and gastrulation. Required for chitin
CC orientation and shaping of the apical and lateral plasma membranes of
CC epidermal cells during cuticle differentiation. Also required for
CC correctly shaping apical membrane topology of the epithelia of other
CC organs such as the midgut and the hindgut.
CC {ECO:0000269|PubMed:18403407, ECO:0000269|PubMed:21199819}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl phosphate + UDP-alpha-D-glucose = a dolichyl beta-
CC D-glucosyl phosphate + UDP; Xref=Rhea:RHEA:15401, Rhea:RHEA-
CC COMP:9517, Rhea:RHEA-COMP:9528, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.117;
CC Evidence={ECO:0000250|UniProtKB:Q9Y673};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q9Y673}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21199819}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:21199819}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally and zygotically. In
CC cellularizing embryos, maternal expression is ubiquitous. At embryonic
CC stage 11, zygotic expression begins in salivary gland precursor cells.
CC In stage 16 embryos, strong expression in salivary glands and part of
CC the proventriculus is detected. {ECO:0000269|PubMed:18403407}.
CC -!- DISRUPTION PHENOTYPE: Larval lethality. Embryos lacking maternal and
CC zygotic wol activity show segmentation, dorso-ventral patterning and
CC gastrulation defects. As a result, germband elongation does not proceed
CC normally and mesoderm invagination is disturbed. In these embryos,
CC protein glycosylation is reduced by 25 percent, the ER tubules are
CC smooth and the unfolded protein response (UPR), a transcriptional
CC response which up-regulates genes that enable cells to cope with
CC misfolded, endoplasmic reticulum-retained proteins, is activated.
CC Larvae lacking maternal wol present patterning and morphological
CC defects, including the failure to form a normal head skeleton, a
CC discontinuous cuticle and irregular body contours. Larvae lacking both
CC maternal and zygotic wol show severe reduction in cuticle deposition, a
CC complete failure of denticle formation and melanization, loss of chitin
CC orientation in the procuticle and dislocation of proteins of the lower
CC electron-dense portion of the epicuticle into the upper electron-lucid
CC sublayer. In addition, the midgut microvilli are separated from each
CC other by large gaps and the apical plasma membrane of the hindgut is
CC highly irregular. {ECO:0000269|PubMed:18403407,
CC ECO:0000269|PubMed:21199819}.
CC -!- MISCELLANEOUS: 'Wollknaeuel' means 'ball of wool' in German.
CC {ECO:0000303|PubMed:18403407}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC {ECO:0000250|UniProtKB:Q9Y673}.
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DR EMBL; AE014134; AAF52633.1; -; Genomic_DNA.
DR EMBL; AY094692; AAM11045.1; -; mRNA.
DR RefSeq; NP_609202.1; NM_135358.2.
DR AlphaFoldDB; Q9VLQ1; -.
DR SMR; Q9VLQ1; -.
DR STRING; 7227.FBpp0079234; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; Q9VLQ1; -.
DR PRIDE; Q9VLQ1; -.
DR DNASU; 34134; -.
DR EnsemblMetazoa; FBtr0079614; FBpp0079234; FBgn0261020.
DR GeneID; 34134; -.
DR KEGG; dme:Dmel_CG7870; -.
DR UCSC; CG7870-RA; d. melanogaster.
DR CTD; 34134; -.
DR FlyBase; FBgn0261020; wol.
DR VEuPathDB; VectorBase:FBgn0261020; -.
DR eggNOG; KOG2977; Eukaryota.
DR GeneTree; ENSGT00940000153481; -.
DR HOGENOM; CLU_033536_9_1_1; -.
DR InParanoid; Q9VLQ1; -.
DR OMA; MVNTDAV; -.
DR OrthoDB; 1107630at2759; -.
DR PhylomeDB; Q9VLQ1; -.
DR Reactome; R-DME-480985; Synthesis of dolichyl-phosphate-glucose.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 34134; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34134; -.
DR PRO; PR:Q9VLQ1; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0261020; Expressed in saliva-secreting gland and 20 other tissues.
DR Genevisible; Q9VLQ1; DM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004581; F:dolichyl-phosphate beta-glucosyltransferase activity; IMP:FlyBase.
DR GO; GO:0040003; P:chitin-based cuticle development; IMP:FlyBase.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:UniProtKB.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:FlyBase.
DR GO; GO:0010004; P:gastrulation involving germ band extension; IMP:UniProtKB.
DR GO; GO:0007509; P:mesoderm migration involved in gastrulation; IMP:UniProtKB.
DR GO; GO:0007009; P:plasma membrane organization; IMP:FlyBase.
DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:FlyBase.
DR GO; GO:0006493; P:protein O-linked glycosylation; IMP:FlyBase.
DR GO; GO:0007379; P:segment specification; HMP:FlyBase.
DR GO; GO:0019991; P:septate junction assembly; IMP:FlyBase.
DR CDD; cd04188; DPG_synthase; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR035518; DPG_synthase.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..326
FT /note="Dolichyl-phosphate beta-glucosyltransferase"
FT /id="PRO_0000423515"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..326
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT MUTAGEN 209
FT /note="R->W: Fails to rescue glycosylation and growth
FT phenotypes in yeast."
FT /evidence="ECO:0000269|PubMed:18403407"
SQ SEQUENCE 326 AA; 37081 MW; 810782B5835D4E69 CRC64;
MWTCLCQLCF YLLSTLAVAA LSIAALVLYK TKPYPNIKRH KDEETFLDPH TIKTVTFPSL
EDSPSLELSV IVPAYNEEQR LPSMLDECLA FLEQKSAGTP NFTYEVIVVS DGSQDATVSV
ALGYSKKHGA EKVRVLELIE NRGKGGAVRM GMLSARGRNL LFADADGATK FPDYDKLEVA
LKQLAPEWRD DGIAIGSRAH LENDAIATRS FFRTILMHGF HFLVWLFAVR SIRDTQCGFK
LFTRTTARKL FTSLHVERWA FDVELLYLAE NLKLPMSEVA VRWTEIDGSK LTPFWSWLQM
GRDLFMIWVR YLVGAWRIAS IQKKEK
