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Database: UniProt
Entry: A0A0N5APG5_9BILA
LinkDB: A0A0N5APG5_9BILA
Original site: A0A0N5APG5_9BILA 
ID   A0A0N5APG5_9BILA        Unreviewed;       416 AA.
AC   A0A0N5APG5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Alpha-1,3/1,6-mannosyltransferase ALG2 {ECO:0000256|RuleBase:RU367136};
DE            EC=2.4.1.132 {ECO:0000256|RuleBase:RU367136};
DE            EC=2.4.1.257 {ECO:0000256|RuleBase:RU367136};
DE   AltName: Full=GDP-Man:Man(1)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase {ECO:0000256|RuleBase:RU367136};
OS   Syphacia muris.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX   NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000654001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMUV_0000654001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- FUNCTION: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and
CC       Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol
CC       diphosphate. {ECO:0000256|ARBA:ARBA00003142,
CC       ECO:0000256|RuleBase:RU367136}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC         alpha-D-GlcNAc-diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-
CC         (1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC         alpha-D-GlcNAc-diphosphodolichol + GDP + H(+); Xref=Rhea:RHEA:29519,
CC         Rhea:RHEA-COMP:12624, Rhea:RHEA-COMP:12626, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:132510,
CC         ChEBI:CHEBI:132511; EC=2.4.1.257;
CC         Evidence={ECO:0000256|ARBA:ARBA00001514,
CC         ECO:0000256|RuleBase:RU367136};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC         diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-(1->3)-beta-D-
CC         Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol +
CC         GDP + H(+); Xref=Rhea:RHEA:29515, Rhea:RHEA-COMP:11044, Rhea:RHEA-
CC         COMP:12624, ChEBI:CHEBI:15378, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:58472, ChEBI:CHEBI:132510; EC=2.4.1.132;
CC         Evidence={ECO:0000256|ARBA:ARBA00001253,
CC         ECO:0000256|RuleBase:RU367136};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU367136}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU367136}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       {ECO:0000256|RuleBase:RU367136}.
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DR   AlphaFoldDB; A0A0N5APG5; -.
DR   STRING; 451379.A0A0N5APG5; -.
DR   WBParaSite; SMUV_0000654001-mRNA-1; SMUV_0000654001-mRNA-1; SMUV_0000654001.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000046393; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004378; F:GDP-Man:Man1GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0102704; F:GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR027054; ALG2.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR028098; Glyco_trans_4-like_N.
DR   PANTHER; PTHR45918; ALPHA-1,3/1,6-MANNOSYLTRANSFERASE ALG2; 1.
DR   PANTHER; PTHR45918:SF2; ALPHA-1,3_1,6-MANNOSYLTRANSFERASE ALG2; 1.
DR   Pfam; PF13439; Glyco_transf_4; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU367136};
KW   Transferase {ECO:0000256|RuleBase:RU367136}.
FT   DOMAIN          28..196
FT                   /note="Glycosyltransferase subfamily 4-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13439"
FT   DOMAIN          208..366
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
SQ   SEQUENCE   416 AA;  48498 MW;  3AF635B5CE2BE4E3 CRC64;
     MMQIREIVMH NRTADMLIVI IHPELWNGGS DRCNVGMIRH FLNTEHRIVW YTSWSDKYWS
     KDEFSNVELR ELKLPLHPGD WLSENVAIGW QLLFSDLNPD LIILDHSASC VPLLKWRFPK
     VKILFYCHFP QQLVTPSRFF LYRWYANLIG VYESFLFKDV DTIMVNSKFT KKKFSLVMPE
     ISKDKIMVVY PPCDVDVTEI GEKAISRMSR PKNERYTFLS LNRFWPEKRL EIVIEAAVEL
     KKKNLNPRIL LAGSVMPTIP ESKIYYTYLK EKVKEFQVSD LVEFVPSPTE YKKFALLREC
     DTVLYTPENE HFGIVPIEAL EQRRPVIVCN SGGPAETVLD GITGSKISYP DGQLLAEEME
     KHMNKPFWPA LDDDTGFEVQ RKRFDNNFSL KGFGNHLNDA IAELFSQPRS AMRDRA
//
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