ALG8_DEBHA
ID ALG8_DEBHA Reviewed; 559 AA.
AC Q6BRE5;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase;
DE EC=2.4.1.265;
DE AltName: Full=Asparagine-linked glycosylation protein 8;
DE AltName: Full=Dol-P-Glc:Glc(1)Man(9)GlcNAc(2)-PP-dolichyl alpha-1,3-glucosyltransferase;
DE AltName: Full=Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl glucosyltransferase;
GN Name=ALG8; OrderedLocusNames=DEHA2D17028g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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).
CC {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ALG6/ALG8 glucosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; CR382136; CAG87397.1; -; Genomic_DNA.
DR RefSeq; XP_459225.1; XM_459225.1.
DR AlphaFoldDB; Q6BRE5; -.
DR SMR; Q6BRE5; -.
DR STRING; 4959.XP_459225.1; -.
DR CAZy; GT57; Glycosyltransferase Family 57.
DR EnsemblFungi; CAG87397; CAG87397; DEHA2D17028g.
DR GeneID; 2901619; -.
DR KEGG; dha:DEHA2D17028g; -.
DR eggNOG; KOG2576; Eukaryota.
DR HOGENOM; CLU_022045_1_1_1; -.
DR InParanoid; Q6BRE5; -.
DR OMA; WDTFVGA; -.
DR OrthoDB; 595382at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000599; Chromosome D.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..559
FT /note="Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-
FT glucosyltransferase"
FT /id="PRO_0000278332"
FT TOPO_DOM 1..24
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..122
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..203
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..286
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 385..394
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..426
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 448..449
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471..493
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 515..526
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 548..559
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 559 AA; 65129 MW; 537489B40080F635 CRC64;
MSKKSFVKGP SGLPKELNND KQWNYSLVNI WVASLALKLL LSVGYHSTDF DVHRNWLAIT
YNLPISKWYI ENTSQWTLDY PPFFAYFEWV LASFVPDFVK RDGCLKIVEK GLYSLPTVLF
QRLSVIVSEV VLFVSLQWYI NSSKTHTEAK RAFVVASSLV LSPGLLIIDH IHFQYNGMLY
GILVLMINSA RLKKYLMCGF WFSILICFKH IYLYLAPAVF IFLLRAYCLN LNFGKTKSSN
ILKIVRWKNL FKLSSIVIAV FSIAFGPFIY YEVMPQLIER LFPFNRGLTH AYWAPNVWAI
YSAIDRLLIQ IYYRIPISRP ILLKIFKFNP QYLWDTKLVN KTTRGLIGDV EFLILPTITS
QLTFFLTLFY QVMALIPLFL QPTFRRFMGS LTLCGFASFL FGWHVHEKAV LVVIFPMTFL
VSRDRDLLGP FNLLVSCAYI SLFPLIFTCD EWLIKITYML LWYIVYYFSL KKVVRLPKTN
GGYGKVILDR VNNGYILGLV PVITIVSLID LFEHKFEILR KLQFMKLLII SVYCGIGIIS
SWNGFSWLYF VDESIWTDE
