ID V7BLF7_PHAVU Unreviewed; 438 AA.
AC V7BLF7;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase {ECO:0000256|ARBA:ARBA00014817};
DE EC=2.4.1.143 {ECO:0000256|ARBA:ARBA00012613};
DE AltName: Full=Beta-1,2-N-acetylglucosaminyltransferase II {ECO:0000256|ARBA:ARBA00032915};
DE AltName: Full=GlcNAc-T II {ECO:0000256|ARBA:ARBA00032552};
DE AltName: Full=Mannoside acetylglucosaminyltransferase 2 {ECO:0000256|ARBA:ARBA00031203};
DE AltName: Full=N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II {ECO:0000256|ARBA:ARBA00029663};
GN ORFNames=PHAVU_007G239000g {ECO:0000313|EMBL:ESW17431.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW17431.1, ECO:0000313|Proteomes:UP000000226};
RN [1] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-
CC asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) +
CC N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-
CC alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-
CC GlcNAc}-L-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:12941,
CC Rhea:RHEA-COMP:13526, Rhea:RHEA-COMP:14369, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60615,
CC ChEBI:CHEBI:60651; EC=2.4.1.143;
CC Evidence={ECO:0000256|ARBA:ARBA00000406};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004323}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 16 (GT16) protein
CC family. {ECO:0000256|ARBA:ARBA00011011}.
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DR EMBL; CM002294; ESW17431.1; -; Genomic_DNA.
DR RefSeq; XP_007145437.1; XM_007145375.1.
DR AlphaFoldDB; V7BLF7; -.
DR STRING; 3885.V7BLF7; -.
DR EnsemblPlants; ESW17431; ESW17431; PHAVU_007G239000g.
DR GeneID; 18626867; -.
DR Gramene; ESW17431; ESW17431; PHAVU_007G239000g.
DR KEGG; pvu:PHAVU_007G239000g; -.
DR eggNOG; KOG2791; Eukaryota.
DR OMA; MHHKKTC; -.
DR OrthoDB; 3676111at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000226; Chromosome 7.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; IEA:InterPro.
DR GO; GO:0008455; F:alpha-1,6-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR007754; GlcNAc_II.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR12871:SF0; ALPHA-1,6-MANNOSYL-GLYCOPROTEIN 2-BETA-N-ACETYLGLUCOSAMINYLTRANSFERASE; 1.
DR PANTHER; PTHR12871; BETA-1,2-N-ACETYLGLUCOSAMINYLTRANSFERASE II; 1.
DR Pfam; PF05060; MGAT2; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000226};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 438 AA; 49931 MW; A01F2BA032EA2D1D CRC64;
MVSSTFMAAS KRPRLRLRDV ALCRLLSVVF VTLSGVLLLI FLLASNSTPT LIVTPDIDNV
DAYHHDLKFE KWHDLPQQSD LSLRLEKING LPPRNLDLYP TLAKDHIIVV LYVHNRPQYL
KVVVESLSHV VGIGETLLIV SHDGYFKEMN KIIDGIRFCQ VKQIYAPYSP HLFSDSFPGV
SANDCKDKDD AGEKHCKGNP DQYGNHRSPK IVSLKHHWWW MMNTVWDGLR ETRDHSGHVL
FIEEDHFIFP NAYRNLQVLT SLKPKKCPDC YAANLAPSDV NSRGEGWASL IAERMGNVGY
SFNRTVWKKI HNKAREFCFF DDYNWDITMW STVYPSFGSP VYSLRGPRTS AIHFGKCGLH
QGQGENKSCM DNGMVNINVE QPDTVSNIGL DWNVHTYENQ PGYKAGFEGW GGWGDHRDRH
LCLSFAKMYQ STPTASRL
//
