ALG5C_TRIVA
ID ALG5C_TRIVA Reviewed; 337 AA.
AC A2ELE6;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Dolichyl-phosphate beta-glucosyltransferase ALG5C {ECO:0000303|PubMed:18552282};
DE Short=DolP-glucosyltransferase;
DE EC=2.4.1.117 {ECO:0000269|PubMed:18552282};
GN Name=ALG5C {ECO:0000303|PubMed:18552282};
GN ORFNames=TVAG_358380 {ECO:0000303|PubMed:17218520};
OS Trichomonas vaginalis.
OC Eukaryota; Metamonada; Parabasalia; Trichomonadida; Trichomonadidae;
OC Trichomonas.
OX NCBI_TaxID=5722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC PRA-98 / G3;
RX PubMed=17218520; DOI=10.1126/science.1132894;
RA Carlton J.M., Hirt R.P., Silva J.C., Delcher A.L., Schatz M., Zhao Q.,
RA Wortman J.R., Bidwell S.L., Alsmark U.C.M., Besteiro S.,
RA Sicheritz-Ponten T., Noel C.J., Dacks J.B., Foster P.G., Simillion C.,
RA Van de Peer Y., Miranda-Saavedra D., Barton G.J., Westrop G.D., Mueller S.,
RA Dessi D., Fiori P.L., Ren Q., Paulsen I., Zhang H., Bastida-Corcuera F.D.,
RA Simoes-Barbosa A., Brown M.T., Hayes R.D., Mukherjee M., Okumura C.Y.,
RA Schneider R., Smith A.J., Vanacova S., Villalvazo M., Haas B.J., Pertea M.,
RA Feldblyum T.V., Utterback T.R., Shu C.L., Osoegawa K., de Jong P.J.,
RA Hrdy I., Horvathova L., Zubacova Z., Dolezal P., Malik S.B.,
RA Logsdon J.M. Jr., Henze K., Gupta A., Wang C.C., Dunne R.L., Upcroft J.A.,
RA Upcroft P., White O., Salzberg S.L., Tang P., Chiu C.-H., Lee Y.-S.,
RA Embley T.M., Coombs G.H., Mottram J.C., Tachezy J., Fraser-Liggett C.M.,
RA Johnson P.J.;
RT "Draft genome sequence of the sexually transmitted pathogen Trichomonas
RT vaginalis.";
RL Science 315:207-212(2007).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18552282; DOI=10.1128/ec.00061-08;
RA Grabinska K.A., Ghosh S.K., Guan Z., Cui J., Raetz C.R., Robbins P.W.,
RA Samuelson J.;
RT "Dolichyl-phosphate-glucose is used to make O-glycans on glycoproteins of
RT Trichomonas vaginalis.";
RL Eukaryot. Cell 7:1344-1351(2008).
CC -!- FUNCTION: Dolichyl-phosphate beta-glucosyltransferase involved in the
CC glycosylation of glycoproteins through the synthesis of dolichyl beta-
CC D-glucosyl phosphate which serves as a sugar donor for transfer of
CC three glucose residues to the Man-9-GlcNAc-2-PP-dolichol precursor to
CC N-glycans. {ECO:0000269|PubMed:18552282}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl phosphate + UDP-alpha-D-glucose = a dolichyl beta-
CC D-glucosyl phosphate + UDP; Xref=Rhea:RHEA:15401, Rhea:RHEA-
CC COMP:9517, Rhea:RHEA-COMP:9528, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.117;
CC Evidence={ECO:0000269|PubMed:18552282};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:18552282}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P40350}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; DS113421; EAY06548.1; -; Genomic_DNA.
DR RefSeq; XP_001318771.1; XM_001318736.1.
DR AlphaFoldDB; A2ELE6; -.
DR SMR; A2ELE6; -.
DR STRING; 5722.XP_001318771.1; -.
DR GeneID; 4764425; -.
DR KEGG; tva:TVAG_358380; -.
DR VEuPathDB; TrichDB:TVAG_358380; -.
DR eggNOG; KOG2977; Eukaryota.
DR InParanoid; A2ELE6; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001542; Unassembled WGS sequence.
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:0004581; F:dolichyl-phosphate beta-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR CDD; cd04188; DPG_synthase; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR035518; DPG_synthase.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..337
FT /note="Dolichyl-phosphate beta-glucosyltransferase ALG5C"
FT /id="PRO_0000431407"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..337
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 337 AA; 38118 MW; 93E9416936208047 CRC64;
MNDLPPIANL ISNILFVLLI ITFLYALCSR FVSDKTLYDY TILPTNDPEK INYYIEPSPS
PKEKIPFPTV FSPSEVYTTF VVPAYNESKR ITPMLDETVA YLERRASENP EFTWEIIVVN
DGSKDNTAEI VTNYAFKHPQ IRLLNQPKNM GKGAAVQAGC LHSRGELILM VDADGATKID
EFEELEKKIK SLTTINKEAI VVGSRAHLEG AEKANRTPLR KFLGLGFHML ITIAGVHGIK
DTQCGFKLFT REAARWLFPN QHVQRWCFDP ELLVIAQSRQ MEVAEVPVEW NEIGDSKMKI
SGMIKMAIDL VQIAIYFRAG LWTVKDKADT PISDFEV
