ID   Q6AXK8_DANRE            Unreviewed;       227 AA.
AC   Q6AXK8;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   04-NOV-2026, entry version 146.
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:AAH79496.1,
GN   ECO:0000313|ZFIN:ZDB-GENE-040808-45};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|EMBL:AAH79496.1};
RN   [1] {ECO:0000313|EMBL:AAH79496.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Singapore local strain {ECO:0000313|EMBL:AAH79496.1};
RC   TISSUE=Embryo {ECO:0000313|EMBL:AAH79496.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (AUG-2004) 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; BC079496; AAH79496.1; -; mRNA.
DR   RefSeq; NP_001003784.2; NM_001003784.2.
DR   PeptideAtlas; Q6AXK8; -.
DR   GeneID; 445327; -.
DR   KEGG; dre:445327; -.
DR   CTD; 29929; -.
DR   AGR; ZFIN:ZDB-GENE-040808-45; -.
DR   ZFIN; ZDB-GENE-040808-45; alg6.
DR   GeneTree; ENSGT00940000153733; -.
DR   HOGENOM; CLU_094820_0_0_1; -.
DR   OrthoDB; 4983at2759; -.
DR   UniPathway; UPA00378; -.
DR   Bgee; ENSDARG00000017617; Expressed in ovary and 27 other cell types or tissues.
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.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:ZFIN.
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   GO; GO:0046527; F:glucosyltransferase activity; ISS:ZFIN.
DR   GO; GO:0006487; P:protein N-linked glycosylation; ISS:ZFIN.
DR   AlphaFoldDB; Q6AXK8; -.
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..227
FT                   /note="Alpha-1,3-glucosyltransferase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015098167"
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"
SQ   SEQUENCE   227 AA;  25845 MW;  5F4B72A98AC83DEE CRC64;
     MENWSLISLC VLLGLTSRWA VSFHSYSGAG KPPMFGDYEA QRHWQELTYN LPVHEWYFNT
     TNNDLNYWGL DYPPLTAYHS LACAYIAKLF NPEWVELHAS RGYESHSHKL FMRATVLFAD
     ALIYIPAVLL YCFYFCDGSP KQKVATAFCI LMYPGLMLID YGHFQYNGVS LGLALWGVLG
     LGLGWDLFGS VAFVLALNYK QMELYHALPF FCYLLGKCVK HGLNGQG
//