ID   Q60GL7_DROME            Unreviewed;       458 AA.
AC   Q60GL7;
DT   03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2006, sequence version 1.
DT   04-NOV-2026, entry version 163.
DE   RecName: Full=Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase {ECO:0000256|ARBA:ARBA00038949, ECO:0000256|RuleBase:RU368119};
DE            Short=GNT-I {ECO:0000256|RuleBase:RU368119};
DE            Short=GlcNAc-T I {ECO:0000256|RuleBase:RU368119};
DE            EC=2.4.1.101 {ECO:0000256|ARBA:ARBA00038949, ECO:0000256|RuleBase:RU368119};
DE   AltName: Full=N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I {ECO:0000256|ARBA:ARBA00041712, ECO:0000256|RuleBase:RU368119};
GN   Name=Mgat1 {ECO:0000313|FlyBase:FBgn0034521};
GN   Synonyms=CG13431-RA {ECO:0000313|EMBL:ACD81852.1}, MGAT1
GN   {ECO:0000313|EMBL:BAD54756.1}, Mgat1-RA {ECO:0000313|EMBL:ADF59567.1};
GN   ORFNames=CG13431 {ECO:0000313|FlyBase:FBgn0034521};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000313|EMBL:BAD54756.1};
RN   [1] {ECO:0000313|EMBL:BAD54756.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15271988; DOI=10.1074/jbc.M404900200;
RA   Ichimiya T., Manya H., Ohmae Y., Yoshida H., Takahashi K., Ueda R.,
RA   Endo T., Nishihara S.;
RT   "The twisted abdomen phenotype of Drosophila POMT1 and POMT2 mutants
RT   coincides with their heterophilic protein O-mannosyltransferase activity.";
RL   J. Biol. Chem. 279:42638-42647(2004).
RN   [2] {ECO:0000313|EMBL:ACD81852.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Berkeley {ECO:0000313|EMBL:ACD81852.1};
RA   Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ADF59567.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Carlson J., Booth B., Frise E., Sandler J., Wan K., Yu C., Celniker S.;
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Initiates complex N-linked carbohydrate formation. Essential
CC       for the conversion of high-mannose to hybrid and complex N-glycans.
CC       {ECO:0000256|ARBA:ARBA00037706, ECO:0000256|RuleBase:RU368119}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-
CC         (1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC         beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer
CC         5A1,2) + UDP-N-acetyl-alpha-D-glucosamine = N(4)-{beta-D-GlcNAc-
CC         (1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-
CC         alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-
CC         GlcNAc}-L-asparaginyl-[protein] + UDP + H(+); Xref=Rhea:RHEA:11456,
CC         Rhea:RHEA-COMP:14367, Rhea:RHEA-COMP:14368, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:59087,
CC         ChEBI:CHEBI:60625; EC=2.4.1.101;
CC         Evidence={ECO:0000256|RuleBase:RU368119};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU368119};
CC       Note=The cofactor is mostly bound to the substrate.
CC       {ECO:0000256|RuleBase:RU368119};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU368119}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000256|ARBA:ARBA00004556}. Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU368119}; Single-
CC       pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323,
CC       ECO:0000256|RuleBase:RU368119}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 13 family.
CC       {ECO:0000256|ARBA:ARBA00006492, ECO:0000256|RuleBase:RU368119}.
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DR   EMBL; BT032838; ACD81852.1; -; mRNA.
DR   EMBL; BT124781; ADF59567.1; -; mRNA.
DR   EMBL; AB176552; BAD54756.1; -; mRNA.
DR   RefSeq; NP_525117.2; NM_080378.4.
DR   AlphaFoldDB; Q60GL7; -.
DR   SMR; Q60GL7; -.
DR   STRING; 7227.FBpp0085571; -.
DR   CAZy; GT13; Glycosyltransferase Family 13.
DR   PaxDb; 7227-FBpp0085571; -.
DR   PeptideAtlas; Q60GL7; -.
DR   DNASU; 37323; -.
DR   GeneID; 37323; -.
DR   KEGG; dme:Dmel_CG13431; -.
DR   UCSC; CG13431-RA; d. melanogaster.
DR   AGR; FB:FBgn0034521; -.
DR   CTD; 4245; -.
DR   FlyBase; FBgn0034521; Mgat1.
DR   VEuPathDB; VectorBase:FBgn0034521; -.
DR   eggNOG; KOG1413; Eukaryota.
DR   HOGENOM; CLU_022150_0_0_1; -.
DR   OMA; AAFFDDW; -.
DR   OrthoDB; 440755at2759; -.
DR   Reactome; R-DME-964739; N-glycan trimming and elongation in the cis-Golgi.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 37323; 0 hits in 1 CRISPR screen.
DR   Bgee; FBgn0034521; Expressed in male accessory gland main cell (Drosophila) in male reproductive gland and 33 other cell types or tissues.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:1990675; C:Golgi medial cisterna membrane; IDA:FlyBase.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003827; F:alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity; IDA:FlyBase.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:FlyBase.
DR   GO; GO:0035284; P:brain segmentation; IMP:BHF-UCL.
DR   GO; GO:0035010; P:encapsulation of foreign target; IMP:FlyBase.
DR   GO; GO:1904381; P:Golgi apparatus N-glycan mannose trimming; IDA:FlyBase.
DR   GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
DR   GO; GO:0006491; P:N-glycan processing; IDA:FlyBase.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR   CDD; cd02514; GT13_GLCNAC-TI; 1.
DR   FunFam; 3.10.180.20:FF:000001; alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase; 1.
DR   FunFam; 3.90.550.10:FF:000055; Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase; 1.
DR   Gene3D; 3.10.180.20; N-Acetylglucosaminyltransferase I, Domain 2; 1.
DR   Gene3D; 3.90.550.10; Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A; 1.
DR   InterPro; IPR004139; Glyco_trans_13.
DR   InterPro; IPR052261; Glycosyltransferase_13.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR10468:SF0; ALPHA-1,3-MANNOSYL-GLYCOPROTEIN 2-BETA-N-ACETYLGLUCOSAMINYLTRANSFERASE; 1.
DR   PANTHER; PTHR10468; PROTEIN O-LINKED-MANNOSE BETA-1,2-N-ACETYLGLUCOSAMINYLTRANSFERASE 1/ALPHA-1,3-MANNOSYL-GLYCOPROTEIN 2-BETA-N-ACETYLGLUCOSAMINYLTRANSFERASE; 1.
DR   Pfam; PF03071; GNT-I; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU368119};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW   ECO:0000256|RuleBase:RU368119};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|RuleBase:RU368119};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU368119};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968,
KW   ECO:0000256|RuleBase:RU368119};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAD54756.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ   SEQUENCE   458 AA;  53193 MW;  6E5CB2B7B3C41CD1 CRC64;
     MRTRKVLLVI GFLVTWTYAT YYLLLRQTGI HTSRHQSLQA YKLNSQARDA NMQSHHLAKN
     VFEFVKLKYL EKQPPSVAST PQISIIAAEI SAELPEQHVA KSATARIPTK TYLANGEPVF
     PVVVFACNRV SVKKCIDNLV QYRPSVEQFP IIVSQDCGDE PTKEAILSYG KQVTLIEQPD
     LSDITVLPKE KKFKGYYKIA RHYGWALNTT FAVGFEFVII VEDDLNVAPD FFEYFLGTHK
     LLKQDPSLWC VSAWNDNGKA AVVDAAQPEL LYRTDFFPGL GWMLTKDLWA ELSVKWPKSF
     WDDWIRHPAQ RKDRVCIRPE ISRTRTFGKI GVSNGLFFDK YLKHIKLSED FVQFTKINMS
     YLLKDNYDNT FLRRVYTYPI VTYDELRRNL IRIEGPVRIQ YTTREQYKRT TKMLGLMDDF
     KSGVPRTAYH GIVSFYYNKR RVHLAPNANW KGYELSWS
//