GLY2_CAEEL
ID GLY2_CAEEL Reviewed; 669 AA.
AC Q9NDH7; Q962C0;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase;
DE EC=2.4.1.155;
DE AltName: Full=GlcNAc-TV;
DE AltName: Full=Glycosylation-related protein 2;
DE AltName: Full=N-acetylglucosaminyltransferase gly-2;
GN Name=gly-2; ORFNames=C55B7.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND MUTAGENESIS OF LEU-116.
RC STRAIN=Bristol N2;
RX PubMed=11937505; DOI=10.1074/jbc.m201390200;
RA Warren C.E., Krizus A., Roy P.J., Culotti J.G., Dennis J.W.;
RT "The Caenorhabditis elegans gene, gly-2, can rescue the N-
RT acetylglucosaminyltransferase V mutation of Lec4 cells.";
RL J. Biol. Chem. 277:22829-22838(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Catalyzes the addition of N-acetylglucosamine (GlcNAc) in
CC beta 1-6 linkage to the alpha-linked mannose of biantennary N-linked
CC oligosaccharides. {ECO:0000269|PubMed:11937505}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-
CC (1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAcl-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-
CC acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-
CC D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-[beta-D-
CC GlcNAc-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAcl-
CC (1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP;
CC Xref=Rhea:RHEA:16921, Rhea:RHEA-COMP:14374, Rhea:RHEA-COMP:14377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:139507, ChEBI:CHEBI:139510; EC=2.4.1.155;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in a complex subset of neurons in larvae
CC and in the spermathecal and pharyngeal-intestinal valves and certain
CC vulval cells of adults. {ECO:0000269|PubMed:11937505}.
CC -!- DEVELOPMENTAL STAGE: In embryos, expressed from the late comma stage.
CC {ECO:0000269|PubMed:11937505}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 18 family.
CC {ECO:0000305}.
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DR EMBL; AF154122; AAF74523.1; -; mRNA.
DR EMBL; AY037800; AAK94765.1; -; mRNA.
DR EMBL; AY037802; AAK94767.1; -; mRNA.
DR EMBL; FO080958; CCD68089.1; -; Genomic_DNA.
DR RefSeq; NP_491874.1; NM_059473.6.
DR AlphaFoldDB; Q9NDH7; -.
DR SMR; Q9NDH7; -.
DR BioGRID; 37811; 1.
DR STRING; 6239.C55B7.2; -.
DR CAZy; GT18; Glycosyltransferase Family 18.
DR PaxDb; Q9NDH7; -.
DR PRIDE; Q9NDH7; -.
DR EnsemblMetazoa; C55B7.2.1; C55B7.2.1; WBGene00001627.
DR GeneID; 172360; -.
DR KEGG; cel:CELE_C55B7.2; -.
DR UCSC; C55B7.2.1; c. elegans.
DR CTD; 172360; -.
DR WormBase; C55B7.2; CE27887; WBGene00001627; gly-2.
DR eggNOG; ENOG502QTNG; Eukaryota.
DR GeneTree; ENSGT00940000153470; -.
DR HOGENOM; CLU_016749_1_0_1; -.
DR InParanoid; Q9NDH7; -.
DR OMA; IGHHLEV; -.
DR OrthoDB; 179031at2759; -.
DR PhylomeDB; Q9NDH7; -.
DR Reactome; R-CEL-975577; N-Glycan antennae elongation.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9NDH7; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001627; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; TAS:WormBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0030144; F:alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IPI:WormBase.
DR GO; GO:0016758; F:hexosyltransferase activity; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:WormBase.
DR InterPro; IPR026116; GlyclTrfase_18.
DR Pfam; PF15024; Glyco_transf_18; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..669
FT /note="Alpha-1,6-mannosylglycoprotein 6-beta-N-
FT acetylglucosaminyltransferase"
FT /id="PRO_0000288613"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..669
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 116
FT /note="L->R: Loss of function."
FT /evidence="ECO:0000269|PubMed:11937505"
SQ SEQUENCE 669 AA; 77835 MW; 783CFC8B131769D9 CRC64;
MRRRHRCVAL LFIFSAFITP LGFFYYTISN ESKRYSEESE KNYGYQTLEF TESPEEISVD
FDKYSQSECS RFPSNVEIEY PECLNKMKWI KNGWKTHHCY IENHIDGSEC SFRYYLSQVE
NYCPPMEHHG KRKGLAKISP SIRRLLPIFE SIPHYMKTRI NRLWKKWKEG AHEVMQKYPK
SMIERRKLNV LVFIGFLANE QKLNMAKKSD HGGPLGELLQ WSDLLATLSV IGHHLEVSTN
KNTLRNIVWK YMSRGPCQYV NNFRQQLDII FTDIMGFNIL RQHHRQFLLS NRCRIRLLDS
FGTHAEFTTK TYFVQNKKSL SGPFSQRNPW GGHGLDLRQH WTFYPHSDDN TFLGFVVDTE
GIDKKNNQMI PSALVYGKEQ YMWRDAEKPI DVLKRIVTVH STVADLDLKD SNISSIFKKV
QNHGFLNSEE ISQLLDNITI FFGLGFPLEG PAPLEAMAHG AVFINAKFKE PKSRLNYKFL
AEKPTLRKWT SQNPYMEKIG EPHVITVDIF NELELEEAIK RAISLKPKHF VPFEFTPAGM
LHRVALLLEK QELCDKIAYS KRWPPIDQMK IFRTLNADDS CETICHSKQL LCEPSYFPII
NSSPLLRREN LCSSTTSDSS PFAPFNCTIQ QSAFLFSCAS SPPISFEINR LCPCRDYIPE
QHAICKKCL
