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Database: UniProt
Entry: A0A453CX67_AEGTS
LinkDB: A0A453CX67_AEGTS
Original site: A0A453CX67_AEGTS 
ID   A0A453CX67_AEGTS        Unreviewed;       479 AA.
AC   A0A453CX67;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
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   Aegilops tauschii subsp. strangulata (Goatgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX   NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET2Gv20996300.2, ECO:0000313|Proteomes:UP000015105};
RN   [1] {ECO:0000313|Proteomes:UP000015105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX   PubMed=25035499; DOI=10.1126/science.1250092;
RG   International Wheat Genome Sequencing Consortium,;
RA   Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA   Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT   "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL   Science 345:1250092-1250092(2014).
RN   [2] {ECO:0000313|Proteomes:UP000015105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX   PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA   Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA   Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT   "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL   Nat. Plants 3:946-955(2017).
RN   [3] {ECO:0000313|EnsemblPlants:AET2Gv20996300.2}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2019) 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; A0A453CX67; -.
DR   STRING; 200361.A0A453CX67; -.
DR   EnsemblPlants; AET2Gv20996300.2; AET2Gv20996300.2; AET2Gv20996300.
DR   Gramene; AET2Gv20996300.2; AET2Gv20996300.2; AET2Gv20996300.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000015105; Chromosome 2D.
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   CDD; cd03805; GT4_ALG2-like; 1.
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:SF1; 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|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU367136}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015105};
KW   Transferase {ECO:0000256|RuleBase:RU367136};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          92..251
FT                   /note="Glycosyltransferase subfamily 4-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13439"
FT   DOMAIN          281..451
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
FT   REGION          16..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   479 AA;  52837 MW;  6A5A1BE557FF6EB7 CRC64;
     TPSLFPWPAG LLLRRQSSAL PSADRPQHPT GPPQLDPSLP TISSARPRPA LPSPAGPPSL
     EAMAAAAGVA GESSGTKTRK LKVAVIHPDL GIGGAERLIV DAACQLAAHG HDVHVFTSHH
     DRNRCFEETV SGPFPVTVYG DFLPRHVFYR FHAVCAYLRC IFVALCVLLW WPSFDVILVD
     QVSVVIPLLK LKASSKTIFY CHFPDMLLAQ HTTLLRRLYR KPIDMIEEAT TGMADLILVN
     SKFTEATFAR TFCGLHARGI EPGVLYPAVS VEQFHEPHDY KLNFLSINRF ERKKNLGLAI
     SAFALLRSVV SKQPGDALRE ASLTVAGGYD KRLKENVEYL EELKRLAATE GVSEHVKFVT
     SCSSSERNEL LSNCLCVLYT PKDEHFGIVP LEAMAAYKPV IACNSGGPVE TVVNEATGFL
     CDPSPIEFSK AMLKFVSDHD LAVRMGKQAR DRVVQKFSTK TFGDLLNSYV LNVYHQRME
//
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