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Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase (EC 2.4.1.155) (GlcNAc-TV) (Glycosylation-related protein 2) (N-acetylglucosaminyltransferase gly-2)

 GLY2_CAEEL              Reviewed;         669 AA.
Q9NDH7; Q962C0;
29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
05-DEC-2018, entry version 111.
RecName: Full=Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase;
EC=2.4.1.155;
AltName: Full=GlcNAc-TV;
AltName: Full=Glycosylation-related protein 2;
AltName: Full=N-acetylglucosaminyltransferase gly-2;
Name=gly-2; ORFNames=C55B7.2;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, AND MUTAGENESIS OF LEU-116.
STRAIN=Bristol N2;
PubMed=11937505; DOI=10.1074/jbc.M201390200;
Warren C.E., Krizus A., Roy P.J., Culotti J.G., Dennis J.W.;
"The Caenorhabditis elegans gene, gly-2, can rescue the N-
acetylglucosaminyltransferase V mutation of Lec4 cells.";
J. Biol. Chem. 277:22829-22838(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
-!- FUNCTION: Catalyzes the addition of N-acetylglucosamine (GlcNAc)
in beta 1-6 linkage to the alpha-linked mannose of biantennary N-
linked oligosaccharides. {ECO:0000269|PubMed:11937505}.
-!- CATALYTIC ACTIVITY:
Reaction=N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-
D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-
Man-(1->4)-beta-D-GlcNAcl-(1->4)-beta-D-GlcNAc}-L-asparaginyl-
[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) +
N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-
(1->3)-[beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->6)]-alpha-D-Man-
(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAcl-(1->4)-beta-D-GlcNAc}-
L-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:16921, Rhea:RHEA-
COMP:14374, Rhea:RHEA-COMP:14377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:139507,
ChEBI:CHEBI:139510; EC=2.4.1.155;
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
Single-pass type II membrane protein {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in a complex subset of neurons in
larvae and in the spermathecal and pharyngeal-intestinal valves
and certain vulval cells of adults. {ECO:0000269|PubMed:11937505}.
-!- DEVELOPMENTAL STAGE: In embryos, expressed from the late comma
stage. {ECO:0000269|PubMed:11937505}.
-!- SIMILARITY: Belongs to the glycosyltransferase 18 family.
{ECO:0000305}.
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EMBL; AF154122; AAF74523.1; -; mRNA.
EMBL; AY037800; AAK94765.1; -; mRNA.
EMBL; AY037802; AAK94767.1; -; mRNA.
EMBL; FO080958; CCD68089.1; -; Genomic_DNA.
RefSeq; NP_491874.1; NM_059473.6.
UniGene; Cel.17900; -.
SMR; Q9NDH7; -.
STRING; 6239.C55B7.2; -.
CAZy; GT18; Glycosyltransferase Family 18.
PaxDb; Q9NDH7; -.
EnsemblMetazoa; C55B7.2; C55B7.2; WBGene00001627.
GeneID; 172360; -.
KEGG; cel:CELE_C55B7.2; -.
UCSC; C55B7.2.1; c. elegans.
CTD; 172360; -.
WormBase; C55B7.2; CE27887; WBGene00001627; gly-2.
eggNOG; ENOG410IDYS; Eukaryota.
eggNOG; ENOG410XTV7; LUCA.
GeneTree; ENSGT00940000155430; -.
HOGENOM; HOG000019790; -.
InParanoid; Q9NDH7; -.
KO; K00744; -.
OMA; IAQNMSD; -.
OrthoDB; EOG091G044F; -.
PhylomeDB; Q9NDH7; -.
Reactome; R-CEL-975577; N-Glycan antennae elongation.
UniPathway; UPA00378; -.
PRO; PR:Q9NDH7; -.
Proteomes; UP000001940; Chromosome I.
Bgee; WBGene00001627; Expressed in 4 organ(s), highest expression level in pharyngeal muscle cell (C elegans).
GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0005795; C:Golgi stack; TAS:WormBase.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IDA:WormBase.
GO; GO:0030144; F:alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase activity; IBA:GO_Central.
GO; GO:0005516; F:calmodulin binding; IPI:WormBase.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016758; F:transferase activity, transferring hexosyl groups; IDA:WormBase.
GO; GO:0006487; P:protein N-linked glycosylation; IDA:WormBase.
InterPro; IPR026116; GlyclTrfase_18.
Pfam; PF15024; Glyco_transf_18; 1.
1: Evidence at protein level;
Complete proteome; Glycoprotein; Glycosyltransferase; Golgi apparatus;
Membrane; Metal-binding; Reference proteome; Signal-anchor;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 669 Alpha-1,6-mannosylglycoprotein 6-beta-N-
acetylglucosaminyltransferase.
/FTId=PRO_0000288613.
TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.
TRANSMEM 8 28 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 29 669 Lumenal. {ECO:0000255}.
CARBOHYD 30 30 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 412 412 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 437 437 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 626 626 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 116 116 L->R: Loss of function.
{ECO:0000269|PubMed:11937505}.
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


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