ALG10_ASHGO
ID ALG10_ASHGO Reviewed; 509 AA.
AC Q75AQ8;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase;
DE EC=2.4.1.256;
DE AltName: Full=Alpha-1,2-glucosyltransferase ALG10-A;
DE AltName: Full=Alpha-2-glucosyltransferase ALG10;
DE AltName: Full=Asparagine-linked glycosylation protein 10;
DE AltName: Full=Dolichyl-phosphoglucose-dependent glucosyltransferase ALG10;
GN Name=ALG10; OrderedLocusNames=ADL138C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 204.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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.
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 -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- SIMILARITY: Belongs to the ALG10 glucosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AE016817; AAS51782.2; -; Genomic_DNA.
DR RefSeq; NP_983958.2; NM_209311.2.
DR AlphaFoldDB; Q75AQ8; -.
DR SMR; Q75AQ8; -.
DR STRING; 33169.AAS51782; -.
DR CAZy; GT59; Glycosyltransferase Family 59.
DR EnsemblFungi; AAS51782; AAS51782; AGOS_ADL138C.
DR GeneID; 4620100; -.
DR KEGG; ago:AGOS_ADL138C; -.
DR eggNOG; KOG2642; Eukaryota.
DR HOGENOM; CLU_017053_1_0_1; -.
DR InParanoid; Q75AQ8; -.
DR OMA; FNCGNLY; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000591; Chromosome IV.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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:0106073; F:dolichyl pyrophosphate Glc2Man9GlcNAc2 alpha-1,2-glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR InterPro; IPR016900; Alg10.
DR PANTHER; PTHR12989; PTHR12989; 1.
DR Pfam; PF04922; DIE2_ALG10; 1.
DR PIRSF; PIRSF028810; Alpha1_2_glucosyltferase_Alg10; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..509
FT /note="Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-
FT glucosyltransferase"
FT /id="PRO_0000215450"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 509 AA; 59118 MW; 7F2658F4D5504E3F CRC64;
MGGEATASEK ELQEREDQLS QQIQDEIVMG CVVNLALWPV LLGAAAYVAY KYNCSWVPYP
FIDEKFHVGQ TVRYLAGRWR EWDSKITTPP GLYVIGWAVQ RTVGLLVGWN TLSLLRLSNV
IGGLVVWPWF VLRPLYFFNA LAFWPATLSV FPLLTSYYFL YYTDVWSTIL IVGSLTLAVT
VPFGERASIW ASAICGLLSC LFRQTNIVWN AFVLVVVLER RTMIHKGFNS LRINNYLKLI
IHGIENWNSL VLPYAVNFAL FLIFLLYNGS VTLGDKSSHV AGFHLVQMFY CLLFITFFSV
PVWFCRSFLL NYVSRTVVYP IWTIFEILGI MMIIRFFTVV HPYLLADNRH IAFYLFKKLI
GRNRFLKYFV MAPIYHFSTF VYLEAVRPTV FFFHPILPIE VKSPVDLPLQ FTHISWSALI
ICTLLTVVPS PLFEPRYYIL PYIFWRIFLL VSPEPFFAVP TEMTYRFGNT RRLAVEFLWF
ILINAITIVI FATNAFAWET EASLQRIIW
