ID   ALG6_PONAB              Reviewed;         507 AA.
AC   Q5NVS8;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase;
DE            EC=2.4.1.267;
DE   AltName: Full=Asparagine-linked glycosylation protein 6 homolog;
DE   AltName: Full=Dol-P-Glc:Man(9)GlcNAc(2)-PP-Dol alpha-1,3-glucosyltransferase;
DE   AltName: Full=Dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase;
GN   Name=ALG6;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Adds the first 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 Man(9)GlcNAc(2)-PP-Dol (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dolichyl beta-D-glucosyl phosphate + alpha-D-Man-(1->2)-
CC         alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-
CC         Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-
CC         (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC         diphosphodolichol = a dolichyl phosphate + alpha-D-Glc-(1->3)-alpha-
CC         D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC         (1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-
CC         alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-
CC         GlcNAc-diphosphodolichol + H(+); Xref=Rhea:RHEA:30635, Rhea:RHEA-
CC         COMP:9517, Rhea:RHEA-COMP:9528, Rhea:RHEA-COMP:12631, Rhea:RHEA-
CC         COMP:12632, ChEBI:CHEBI:15378, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683,
CC         ChEBI:CHEBI:132520, ChEBI:CHEBI:132521; EC=2.4.1.267;
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Multi-pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ALG6/ALG8 glucosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; CR925922; CAI29585.1; -; mRNA.
DR   RefSeq; NP_001127060.1; NM_001133588.1.
DR   AlphaFoldDB; Q5NVS8; -.
DR   SMR; Q5NVS8; -.
DR   STRING; 9601.ENSPPYP00000001490; -.
DR   CAZy; GT57; Glycosyltransferase Family 57.
DR   GeneID; 100174089; -.
DR   KEGG; pon:100174089; -.
DR   CTD; 29929; -.
DR   eggNOG; KOG2575; Eukaryota.
DR   InParanoid; Q5NVS8; -.
DR   OrthoDB; 595382at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000001595; Unplaced.
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:0042281; F:dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
DR   InterPro; IPR039488; ALG6.
DR   InterPro; IPR004856; Glyco_trans_ALG6/ALG8.
DR   PANTHER; PTHR12413; PTHR12413; 1.
DR   PANTHER; PTHR12413:SF1; PTHR12413:SF1; 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..507
FT                   /note="Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-
FT                   glucosyltransferase"
FT                   /id="PRO_0000284131"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        227..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        298..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        324..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        362..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        388..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        438..458
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        473..493
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   507 AA;  58075 MW;  ADF072D16671D9B9 CRC64;
     MEKWYLMTVV VLIGLTVRWT VSLNSYSGAG KPPMFGDYEA QRHWQEITFN LPVKQWYFNS
     SDNNLQYWGL DYPPPTAYHS LLCAYVAKFI NPDWIALHTS RGYESQAHKL FMRTTVLIAD
     LLIYIPAVVL YCCCLKEIST KKKIANALCI LLYPGLILID YGHFQYNSVS LGFALWGVLG
     ISCDCDLLGS LAFCLAINYK QMELYHALPF FCFLLGKCFK KGLKGKGFVL LVKLACIVVA
     SFVLCWLPFF TEREQTLQVL RRLFPVDRGL FEDKVANIWC SFNVFLKIKD ILPRHIQLIM
     SFCFTFLSLL PACIKLILQP SSKGFKFTLV SCALSFFLFS FQVHEKSILL VSLPVCLVLS
     EIPFMSTWFL LVSTFSMLPL LLKDELLMPS VVTTMAFFIA CVTSFSIFEK TSEEELQLKS
     FSISVRKYLP CFTFLSRIIQ YLFLISVITM VLLTLMTVTL GPPQKLPDLF SVLVCFVSCL
     NFLFFLVYFN IIIVWDSKSG RNQKKIS