ID   Q0VC15_BOVIN            Unreviewed;       289 AA.
AC   Q0VC15;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   10-JUN-2026, entry version 85.
DE   RecName: Full=Alpha-1,3-glucosyltransferase {ECO:0000256|RuleBase:RU363110};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU363110};
GN   Name=ALG6 {ECO:0000313|EMBL:AAI20397.1};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|EMBL:AAI20397.1};
RN   [1] {ECO:0000313|EMBL:AAI20397.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=L1 Hereford {ECO:0000313|EMBL:AAI20397.1};
RC   TISSUE=Basal ganglia {ECO:0000313|EMBL:AAI20397.1};
RA   Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA   Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA   Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA   Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA   Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA   Holt R., Jones S.J., Marra M.A.;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-
CC       glucosyltransferase that operates in the biosynthetic pathway of
CC       dolichol-linked oligosaccharides, the glycan precursors employed in
CC       protein asparagine (N)-glycosylation. The assembly of dolichol-linked
CC       oligosaccharides begins on the cytosolic side of the endoplasmic
CC       reticulum membrane and finishes in its lumen. The sequential addition
CC       of sugars to dolichol pyrophosphate produces dolichol-linked
CC       oligosaccharides containing fourteen sugars, including two GlcNAcs,
CC       nine mannoses and three glucoses. Once assembled, the oligosaccharide
CC       is transferred from the lipid to nascent proteins by
CC       oligosaccharyltransferases. In the lumen of the endoplasmic reticulum,
CC       adds the first glucose residue from dolichyl phosphate glucose (Dol-P-
CC       Glc) onto the lipid-linked oligosaccharide intermediate
CC       Man(9)GlcNAc(2)-PP-Dol to produce Glc(1)Man(9)GlcNAc(2)-PP-Dol.
CC       Glc(1)Man(9)GlcNAc(2)-PP-Dol is a substrate for ALG8, the following
CC       enzyme in the biosynthetic pathway. {ECO:0000256|ARBA:ARBA00044720}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC         [alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-
CC         Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-
CC         (1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + a di-
CC         trans,poly-cis-dolichyl beta-D-glucosyl phosphate = an alpha-D-Glc-
CC         (1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC         [alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-
CC         Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-
CC         (1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + a di-
CC         trans,poly-cis-dolichyl phosphate + H(+); Xref=Rhea:RHEA:30635,
CC         Rhea:RHEA-COMP:19498, Rhea:RHEA-COMP:19502, Rhea:RHEA-COMP:19520,
CC         Rhea:RHEA-COMP:19521, ChEBI:CHEBI:15378, ChEBI:CHEBI:57525,
CC         ChEBI:CHEBI:57683, ChEBI:CHEBI:132520, ChEBI:CHEBI:132521;
CC         EC=2.4.1.267; Evidence={ECO:0000256|ARBA:ARBA00048950};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30636;
CC         Evidence={ECO:0000256|ARBA:ARBA00048950};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU363110}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363110}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC       ECO:0000256|RuleBase:RU363110}.
CC   -!- SIMILARITY: Belongs to the ALG6/ALG8 glucosyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00008715, ECO:0000256|RuleBase:RU363110}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU363110}.
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DR   EMBL; BC120396; AAI20397.1; -; mRNA.
DR   AlphaFoldDB; Q0VC15; -.
DR   OrthoDB; 4983at2759; -.
DR   UniPathway; UPA00378; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042281; F:dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR004856; Glyco_trans_ALG6/ALG8.
DR   PANTHER; PTHR12413; DOLICHYL GLYCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR12413:SF1; DOLICHYL PYROPHOSPHATE MAN9GLCNAC2 ALPHA-1,3-GLUCOSYLTRANSFERASE; 1.
DR   Pfam; PF03155; Alg6_Alg8; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|RuleBase:RU363110};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU363110};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363110};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363110};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU363110};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU363110}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..289
FT                   /note="Alpha-1,3-glucosyltransferase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004178575"
FT   TRANSMEM        110..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363110"
FT   TRANSMEM        144..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363110"
FT   TRANSMEM        173..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363110"
FT   TRANSMEM        227..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363110"
SQ   SEQUENCE   289 AA;  33023 MW;  B97AB6E2C9D99B40 CRC64;
     MEKWYLMTAA VLLGLTVRWT VSLNSYSGAG KPPMFGDYEA QRHWQEITFN LPIKQWYFNS
     SDNNLQYWGL DYPPLTAYHS FLCAYVAKFI NPDWIALHSS RGYESQAHKL FMRATVLIAD
     LLIYIPAVVL YCCCLKEIST KKKIATALCI LLYPGLILID YGHFQYNSVS LGFALWGILG
     VSYDWDLLGS LAFCLAINYK QMELYHSLPF FCFLLGKCFK KGLKGKGLVL LIKLACTVVA
     SFILCWLPFF TEREQTLQVL RRLFPVDRGL FEACLRTFLS LPSVTGLSL
//