ALG10_DROME
ID ALG10_DROME Reviewed; 449 AA.
AC Q8T8L8; Q8MQM2; Q9VTG3;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Putative Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase {ECO:0000250|UniProtKB:P50076};
DE EC=2.4.1.256 {ECO:0000250|UniProtKB:P50076};
DE AltName: Full=Alpha-2-glucosyltransferase ALG10 {ECO:0000303|PubMed:12200473};
GN Name=Alg10; ORFNames=CG32076;
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:CAD24126.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12200473; DOI=10.1093/oxfordjournals.molbev.a004208;
RA Oriol R., Martinez-Duncker I., Chantret I., Mollicone R., Codogno P.;
RT "Common origin and evolution of glycosyltransferases using Dol-P-
RT monosaccharides as donor substrate.";
RL Mol. Biol. Evol. 19:1451-1463(2002).
RN [2] {ECO:0000312|EMBL:AAF50086.2}
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] {ECO:0000312|EMBL:AAF50086.2}
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 [4] {ECO:0000312|EMBL:AAM75090.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM75090.1};
RC TISSUE=Head {ECO:0000312|EMBL:AAM75090.1};
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).
CC -!- FUNCTION: Adds the third glucose residue to the lipid-linked
CC oligosaccharide precursor for N-linked glycosylation. Transfers glucose
CC from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked
CC oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol (By similarity).
CC {ECO:0000250|UniProtKB:P50076}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-
CC alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-
CC GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate
CC + alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-
CC Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-
CC Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol + H(+); Xref=Rhea:RHEA:29543, Rhea:RHEA-COMP:9517,
CC Rhea:RHEA-COMP:9528, Rhea:RHEA-COMP:12633, Rhea:RHEA-COMP:12634,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:132522, ChEBI:CHEBI:132523; EC=2.4.1.256;
CC Evidence={ECO:0000250|UniProtKB:P50076};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P50076}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P50076}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P50076}.
CC -!- SIMILARITY: Belongs to the ALG10 glucosyltransferase family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM75090.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ431376; CAD24126.1; -; mRNA.
DR EMBL; AE014296; AAF50086.2; -; Genomic_DNA.
DR EMBL; AY128497; AAM75090.1; ALT_INIT; mRNA.
DR RefSeq; NP_729680.1; NM_168449.2.
DR AlphaFoldDB; Q8T8L8; -.
DR IntAct; Q8T8L8; 1.
DR STRING; 7227.FBpp0075946; -.
DR CAZy; GT59; Glycosyltransferase Family 59.
DR GlyGen; Q8T8L8; 1 site.
DR PaxDb; Q8T8L8; -.
DR PRIDE; Q8T8L8; -.
DR EnsemblMetazoa; FBtr0076217; FBpp0075946; FBgn0052076.
DR GeneID; 326193; -.
DR KEGG; dme:Dmel_CG32076; -.
DR UCSC; CG32076-RA; d. melanogaster.
DR CTD; 84920; -.
DR FlyBase; FBgn0052076; Alg10.
DR VEuPathDB; VectorBase:FBgn0052076; -.
DR eggNOG; KOG2642; Eukaryota.
DR HOGENOM; CLU_017053_1_0_1; -.
DR InParanoid; Q8T8L8; -.
DR OMA; FNCGNLY; -.
DR OrthoDB; 476469at2759; -.
DR PhylomeDB; Q8T8L8; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 326193; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 326193; -.
DR PRO; PR:Q8T8L8; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0052076; Expressed in eye disc (Drosophila) and 20 other tissues.
DR ExpressionAtlas; Q8T8L8; baseline and differential.
DR Genevisible; Q8T8L8; DM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0106073; F:dolichyl pyrophosphate Glc2Man9GlcNAc2 alpha-1,2-glucosyltransferase activity; ISS:FlyBase.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISS:FlyBase.
DR InterPro; IPR016900; Alg10.
DR PANTHER; PTHR12989; PTHR12989; 1.
DR Pfam; PF04922; DIE2_ALG10; 1.
DR PIRSF; PIRSF028810; Alpha1_2_glucosyltferase_Alg10; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..449
FT /note="Putative Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol
FT alpha-1,2-glucosyltransferase"
FT /id="PRO_0000413533"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 190
FT /note="Q -> R (in Ref. 4; AAM75090)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="V -> I (in Ref. 4; AAM75090)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 449 AA; 51783 MW; 879E231B5D047BB7 CRC64;
MNGSWKLILP VGFVLYSLPL FLRVNGTSDY VIDEEFHIPQ GLAFCRKEFD VWDPKITTFP
GLYLIALLLN PLSLCTVTGL RMLSLAGAGI NILLLYKIRR RILAGSGGNS YAAHEAITMS
VLPPLYFFSH LYYTDTLSLT MVLLFYNYWQ QEAHLPAAVF GAASVLMRQT NIVWVCMATG
MTVLDTLVNQ CARTGRVPKE NVRLMGKELW LQLVSSPQLL CNCILSILAK CCFYASIILP
FVGFLFINGS IVVGDKSAHE ASLHVPQLFY FAIFAAGFGI SNTIRQFRPA AELIRRNRVL
SLLALLLILV VVHLNTEVHP YLLADNRHYT FYIWSRLYGR FWWFRYAMAP AYLLSICVLF
CGLRHMPESF KLMFPLSLFL VLCFQRLLEL RYFLVPYILF RLNTRHTRKG YAEWLELGAH
LLLNVATFYV YFTKEFYWKN YRTPQRIIW
