ALG8_CAEEL
ID ALG8_CAEEL Reviewed; 766 AA.
AC P52887; Q5WRQ2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase;
DE EC=2.4.1.265;
DE AltName: Full=Asparagine-linked glycosylation protein 8 homolog;
DE AltName: Full=Dol-P-Glc:Glc(1)Man(9)GlcNAc(2)-PP-dolichyl alpha-1,3-glucosyltransferase;
DE AltName: Full=Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl glucosyltransferase;
GN Name=algn-8 {ECO:0000312|WormBase:C08H9.3a};
GN ORFNames=C08H9.3 {ECO:0000312|WormBase:C08H9.3a};
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 second 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(1)Man(9)GlcNAc(2)-PP-Dol (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-
CC Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-
CC Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-
CC Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+);
CC Xref=Rhea:RHEA:31307, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9528,
CC Rhea:RHEA-COMP:12632, Rhea:RHEA-COMP:12633, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57525, ChEBI:CHEBI:57683, ChEBI:CHEBI:132521,
CC ChEBI:CHEBI:132522; EC=2.4.1.265;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:C08H9.3a};
CC IsoId=P52887-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:C08H9.3a};
CC IsoId=P52887-2; Sequence=VSP_012307, VSP_012308;
CC -!- SIMILARITY: Belongs to the ALG6/ALG8 glucosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; BX284602; CAA91145.3; -; Genomic_DNA.
DR EMBL; BX284602; CAH60747.1; -; Genomic_DNA.
DR PIR; T19107; T19107.
DR RefSeq; NP_001021940.2; NM_001026769.3. [P52887-1]
DR RefSeq; NP_001021941.1; NM_001026770.3.
DR AlphaFoldDB; P52887; -.
DR SMR; P52887; -.
DR BioGRID; 39864; 1.
DR STRING; 6239.C08H9.3a; -.
DR CAZy; GT57; Glycosyltransferase Family 57.
DR EPD; P52887; -.
DR PaxDb; P52887; -.
DR PeptideAtlas; P52887; -.
DR EnsemblMetazoa; C08H9.3a.1; C08H9.3a.1; WBGene00007464. [P52887-1]
DR EnsemblMetazoa; C08H9.3b.1; C08H9.3b.1; WBGene00007464. [P52887-2]
DR GeneID; 174542; -.
DR KEGG; cel:CELE_C08H9.3; -.
DR UCSC; C08H9.3a; c. elegans. [P52887-1]
DR CTD; 174542; -.
DR WormBase; C08H9.3a; CE47030; WBGene00007464; algn-8. [P52887-1]
DR WormBase; C08H9.3b; CE37608; WBGene00007464; algn-8. [P52887-2]
DR eggNOG; KOG2576; Eukaryota.
DR eggNOG; KOG4417; Eukaryota.
DR GeneTree; ENSGT00940000153733; -.
DR HOGENOM; CLU_398629_0_0_1; -.
DR InParanoid; P52887; -.
DR OMA; CALYSFR; -.
DR OrthoDB; 595382at2759; -.
DR PhylomeDB; P52887; -.
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:P52887; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00007464; 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:0042283; F:dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; 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 CDD; cd06559; Endonuclease_V; 1.
DR InterPro; IPR039487; ALG8.
DR InterPro; IPR021173; C08H9.3-like.
DR InterPro; IPR007581; Endonuclease-V.
DR InterPro; IPR004856; Glyco_trans_ALG6/ALG8.
DR PANTHER; PTHR12413; PTHR12413; 1.
DR PANTHER; PTHR12413:SF2; PTHR12413:SF2; 1.
DR Pfam; PF03155; Alg6_Alg8; 1.
DR Pfam; PF04493; Endonuclease_5; 1.
DR PIRSF; PIRSF037345; Dolichyl-P-Glc/endonucV; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Endoplasmic reticulum; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..766
FT /note="Probable dolichyl pyrophosphate Glc1Man9GlcNAc2
FT alpha-1,3-glucosyltransferase"
FT /id="PRO_0000174164"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 111..123
FT /note="YIAVCALYSFRSP -> LLSALYTPSALHV (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_012307"
FT VAR_SEQ 124..766
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_012308"
SQ SEQUENCE 766 AA; 86870 MW; B335E2AD83D90934 CRC64;
MGEVQLVLAV TAILISFKCL LIPAYVSTDF EVHRNWMAVT WQRPLCEWYT EATSEWTLDY
PPFFAYFELG LASVAHFFGF DECLVISKTP RFSRRILIFQ RFSVIFCDIL YIAVCALYSF
RSPRLVSRIP KKLQQNGREA CFVLLASLQA LIICDSIHFQ YNSMLTAIFL MSLFFIDTER
YLMAALSYSI LLNFKHIYVY YALGYVFYYL VNYFQFSGNV LLANTPKAIS LAIALLIPFC
ASIFPFIHAS GVQGLQNIAT RLFPVSRGLT HAYWAPNFWA LYNFADLCLY RVLSLLKIGK
FDAPTYTSGL VQEYSHSVLP NVSPMGTLCL VVISSMIVLT GLVIRRKDSA DFSLFAVFSA
FCFFYFGYHV HEKAIILVTV PMTVFAIKNP KYHSILIHLT CIASFSLFPL LFTPFETLLK
YAICVSYFFI QLVFLKRVTL MPLSDLIPTR HVASWLLMGM VEVYNTFLHK WLWTSRLPFA
PLMAISILTA IELTGLIGAL IWSTFGDGIF EIWWAKATCQ IRERLIRDST YSVQAVEDLD
DVKLVAGIDT SAAKLNSDMV YISVSFWTYP DLKHVATISD TRMLELPYIP QYLAVREAEV
MADFLKSVIT ERPELRPDVI LCDGFGEFHS RGCGMACHVG ALSGIASIGV AKNLTLHHTY
ETIGMENKSK VDSFVEHCRE VYKNNKTSPG FIPFDIVEPV VLNILRMGSS MNGVFVSAGY
GIDLELSTEI CSQLLLNNTT IEPIRAADLE SRRLVRENFD GNEKLE
