ALG8_DROME
ID ALG8_DROME Reviewed; 511 AA.
AC Q9W3V8; Q058Z6;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase;
DE Short=Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl glucosyltransferase;
DE EC=2.4.1.265;
DE AltName: Full=Asparagine-linked glycosylation protein 8 homolog;
DE AltName: Full=Dol-P-Glc:Glc(1)Man(9)GlcNAc(2)-PP-dolichyl alpha-1,3-glucosyltransferase;
DE AltName: Full=Protein xiantuan {ECO:0000312|FlyBase:FBgn0029906};
GN Name=xit {ECO:0000312|FlyBase:FBgn0029906};
GN ORFNames=CG4542 {ECO:0000312|FlyBase:FBgn0029906};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24681004; DOI=10.1016/j.ydbio.2014.03.007;
RA Zhang Y., Kong D., Reichl L., Vogt N., Wolf F., Grosshans J.;
RT "The glucosyltransferase Xiantuan of the endoplasmic reticulum specifically
RT affects E-Cadherin expression and is required for gastrulation movements in
RT Drosophila.";
RL Dev. Biol. 390:208-220(2014).
CC -!- FUNCTION: Adds the second 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(1)Man(9)GlcNAc(2)-PP-Dol (By similarity). Functions
CC in developmental processes such as germband extension, the apical
CC constriction of mesoderm precursor cells and ventral furrow formation
CC in early embryogenesis prior to gastrulation (PubMed:24681004).
CC Involved in the glycosylation and intracellular distribution of shg (E-
CC cadherin) (PubMed:24681004). Function in cell intercalation in the
CC lateral epidermis during germband extension may be due to its effect on
CC shg (PubMed:24681004). {ECO:0000250|UniProtKB:P40351,
CC ECO:0000269|PubMed:24681004}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-
CC Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-
CC Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-
CC Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+);
CC Xref=Rhea:RHEA:31307, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9528,
CC Rhea:RHEA-COMP:12632, Rhea:RHEA-COMP:12633, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57525, ChEBI:CHEBI:57683, ChEBI:CHEBI:132521,
CC ChEBI:CHEBI:132522; EC=2.4.1.265;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:24681004}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:24681004}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P40351}.
CC -!- SIMILARITY: Belongs to the ALG6/ALG8 glucosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AE014298; AAF46205.1; -; Genomic_DNA.
DR EMBL; AY069662; AAL39807.1; -; mRNA.
DR RefSeq; NP_572355.1; NM_132127.4.
DR AlphaFoldDB; Q9W3V8; -.
DR SMR; Q9W3V8; -.
DR STRING; 7227.FBpp0070931; -.
DR CAZy; GT57; Glycosyltransferase Family 57.
DR PaxDb; Q9W3V8; -.
DR PRIDE; Q9W3V8; -.
DR DNASU; 31623; -.
DR EnsemblMetazoa; FBtr0070970; FBpp0070931; FBgn0029906.
DR GeneID; 31623; -.
DR KEGG; dme:Dmel_CG4542; -.
DR UCSC; CG4542-RA; d. melanogaster.
DR CTD; 31623; -.
DR FlyBase; FBgn0029906; xit.
DR VEuPathDB; VectorBase:FBgn0029906; -.
DR eggNOG; KOG2576; Eukaryota.
DR GeneTree; ENSGT00940000153733; -.
DR HOGENOM; CLU_022045_2_0_1; -.
DR InParanoid; Q9W3V8; -.
DR OMA; FWHLVGI; -.
DR OrthoDB; 595382at2759; -.
DR PhylomeDB; Q9W3V8; -.
DR Reactome; R-DME-446193; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 31623; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 31623; -.
DR PRO; PR:Q9W3V8; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0029906; Expressed in embryonic/larval hemocyte (Drosophila) and 20 other tissues.
DR Genevisible; Q9W3V8; DM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase.
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:0042283; F:dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase activity; ISS:FlyBase.
DR GO; GO:0003384; P:apical constriction involved in gastrulation; IMP:FlyBase.
DR GO; GO:0007377; P:germ-band extension; IMP:FlyBase.
DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; ISS:FlyBase.
DR GO; GO:0006486; P:protein glycosylation; IMP:FlyBase.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISS:FlyBase.
DR InterPro; IPR039487; ALG8.
DR InterPro; IPR004856; Glyco_trans_ALG6/ALG8.
DR PANTHER; PTHR12413; PTHR12413; 1.
DR PANTHER; PTHR12413:SF2; PTHR12413:SF2; 1.
DR Pfam; PF03155; Alg6_Alg8; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..511
FT /note="Probable dolichyl pyrophosphate Glc1Man9GlcNAc2
FT alpha-1,3-glucosyltransferase"
FT /id="PRO_0000174165"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 469..491
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 511 AA; 57945 MW; BD8C5A20CB3D6A0F CRC64;
MKDLFWHLVG IATGLKILLI PAYHSTDFEV HRNWLAITHS LPLNQWYVDA TSEWTLDYPP
FFAYFEWLLS QVAKYVDPRM LVVDNLNYES KATVYFQRLS VIVTDLVYVL GVRSCLGSLG
LGRDTQQFFA ASMLLLLNVG LIFVDHIHFQ YNGLLFGILL LSIGSLIRQR FLWSAFAFAV
LLNFKHIFLY MAPAFGVYLL RFYCLEQASV VSAVGAVVKL LVVGLTPFAV SFGPFWQQLP
QVLSRLFPFK RGLTHAYWAP NFWALYNAAD KLAAGVLKVQ DGGASTTSGL VQEVRHSVLP
AITPPVTFAL TALFMLPILV KLFRSAKKQS PLVFLRAVVL CGCSSFVFGW HVHEKAILMV
LLPLCLLTLV NREDARYAYV LGIAGYFSLF PLLFDADLYI PRYSLYMSYV AMMYGQLYRI
FPGFRGFHTL EWLYMLGFMA IPLYEHLLSF LLHLDQRLPF LPLLLTSVYS ALGVLYFFGA
YYLYALGISW GKVPIASSTS AAAVKRKRKT K
