ALG6_CAEEL
ID ALG6_CAEEL Reviewed; 503 AA.
AC Q09226;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase;
DE EC=2.4.1.267 {ECO:0000250|UniProtKB:Q12001};
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=algn-6 {ECO:0000312|WormBase:C08B11.8};
GN ORFNames=C08B11.8 {ECO:0000312|WormBase:C08B11.8};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Adds the first glucose residue to the lipid-linked
CC oligosaccharide precursor for N-linked glycosylation (By similarity).
CC Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the
CC lipid-linked oligosaccharide Man(9)GlcNAc(2)-PP-Dol (By similarity).
CC {ECO:0000250|UniProtKB:Q12001}.
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 Evidence={ECO:0000250|UniProtKB:Q12001};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q12001}.
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; BX284602; CAA86666.1; -; Genomic_DNA.
DR PIR; T19071; T19071.
DR RefSeq; NP_495685.1; NM_063284.1.
DR AlphaFoldDB; Q09226; -.
DR SMR; Q09226; -.
DR STRING; 6239.C08B11.8; -.
DR CAZy; GT57; Glycosyltransferase Family 57.
DR PaxDb; Q09226; -.
DR EnsemblMetazoa; C08B11.8.1; C08B11.8.1; WBGene00007435.
DR EnsemblMetazoa; C08B11.8.2; C08B11.8.2; WBGene00007435.
DR GeneID; 182392; -.
DR KEGG; cel:CELE_C08B11.8; -.
DR UCSC; C08B11.8; c. elegans.
DR CTD; 182392; -.
DR WormBase; C08B11.8; CE01478; WBGene00007435; algn-6.
DR eggNOG; KOG2575; Eukaryota.
DR GeneTree; ENSGT00940000153733; -.
DR HOGENOM; CLU_008110_3_0_1; -.
DR InParanoid; Q09226; -.
DR OMA; RQWYFNT; -.
DR OrthoDB; 595382at2759; -.
DR PhylomeDB; Q09226; -.
DR Reactome; R-CEL-446193; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q09226; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00007435; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
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 3: Inferred from homology;
KW Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..503
FT /note="Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-
FT 1,3-glucosyltransferase"
FT /id="PRO_0000174157"
FT TOPO_DOM 1..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..151
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..211
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 240..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..268
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 354..359
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 360..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 380..382
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 404..420
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 442..443
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 465..474
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 496..503
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 57907 MW; 06A5F20DE1AEFC65 CRC64;
MKERIKDKAW RPQFIKLNNP DTSKKIVSQK SKKPEIVDLS SPGNNDLVTI SILCVLLCFQ
LAISLNPHSG ESQPPMYGDY EAQRHWMEIT VNLPIEQWYL NGTHNDLLYW GLDYPPITAY
HHYLLGVISN KINKKWVELT TSRGYESIAH KLFMRLSAII PFYIFYLPPL IFYFTRSKKM
SPILYALALL YPSLLVIDNG HFQYNSISLG LFLATYMFLT KNFTIIGSIL FVAALNYKQM
ELYHALPVFV FILARSINKT QLFNSFRRIL TIGLFVVGTF LIIWLPFLLT GTAKDVIIRV
FPFNRGLYED KVASFWCAFS FILKRLPLQS VQIYISTALV LAGSAPSLLV LFLRPTEKQF
RISLTATGLS FFLFSFHVHE KTILLAAVPA LLLISEYTSL VIWFLNITNI SIFSLCVKDN
FALSLSFFFA YFVVSYAYTA PRKISHILTI LIGFAICILE LYGPSNQRFP HIYQLANAFF
SCVHFIYFLL YLSFASFEKT KKE
