Q10470
uniprot
Q10470
canonical
amino_acid_sequence
MKMRRYKLFLMFCMAGLCLISFLHFFKTLSYVTFPRELASLSPNLISSFFWNNAPVTPQASPEPGDPDLLRTPLYSHSPLLQPLSPSKATEELHRVDFVLPEDTTEYFVRTKAGGVCFKPGTRMLEKPSPGRTEEKTEVSEGSSARGPARRPMRHVLSSRERLGSRGTRRKWVECVCLPGWHGPSCGVPTVVQYSNLPTKERLVPREVPRRVINAININHEFDLLDVRFHELGDVVDAFVVCDSNFTAYGEPRPLKFREMLTNGTFEYIRHKVLYVFLDHFPPGGRQDGWIADDYLRTFLTQDGVSRLRNLRPDDVFIIDDADEIPARDGVLFLKLYDGWTEPFAFHMRKSLYGFFWKQPGTLEVVSGCTMDMLQAVYGLDGIRLRRRQYYTMPNFRQYENRTGHILVQWSLGSPLHFAGWHCSWCFTPEGIYFKLVSAQNGDFPRWGDYEDKRDLNYIRSLIRTGGWFDGTQQEYPPADPSEHMYAPKYLLKNYDQFRYLLENPYREPKSTVEGGRQNQGSDGRSSAVRGKLDTAEG
uniprot
proteins
ec_number
2.4.1.144
uniprot
proteins
function
FUNCTION: It is involved in the regulation of the biosynthesis and biological function of glycoprotein oligosaccharides. Catalyzes the addition of N-acetylglucosamine in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-linked sugar chains, called bisecting N-acetylglucosamine (GlcNAc). It is one of the most important enzymes involved in the regulation of the biosynthesis of glycoprotein oligosaccharides (PubMed:11986323, PubMed:25592972). The addition of this bisecting GlcNAc residue alters not only the composition, but also the conformation of the N-glycan. The introduction of the bisecting GlcNAc residue results in the suppression of further processing and elongation of N-glycans, precluding the formation of beta-1,6 GlcNAc branching, catalyzed by MGAT5 since it is unable to use the bisected oligosaccharide as a substrate (By similarity). Addition of bisecting N-acetylglucosamine to CDH1/E-cadherin modulates CDH1 cell membrane location. Inhibits NeuAc-alpha-2,3-Gal-beta-1,4-GlcNAc- formation which modulates sialylation levels and plays a role in cell migration regulation (By similarity). In brain, addition of bisecting N-acetylglucosamine to BACE1 blocks its lysosomal targeting in response to oxidative stress and further degradation which increases its location to early endosome and the APP cleavage (PubMed:25592972, PubMed:26467158). Adds bisecting GlcNAc residue to complex-type N-linked-glycans attached on fragment crystallizable (Fc) of IgGs. Readily converts fucosylated and non-fucosylated core glycoforms with terminal GlcNAcs on both antennae. Prior galactosylation of GlcNAc on the alpha(1->3) Man branch prevents N-glycan bisection, whereas galactosylation of GlcNAc on the alpha(1->6) Man branch is permissive. {ECO:0000250|UniProtKB:Q09327, ECO:0000269|PubMed:11986323, ECO:0000269|PubMed:25592972, ECO:0000269|PubMed:26467158}.
uniprot
proteins
mass_dalton
62003
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein glycosylation. {ECO:0000305|PubMed:25592972}.
uniprot
proteins
protein_family
Glycosyltransferase 17 family
uniprot
proteins
pubmed
11986323
uniprot
proteins
pubmed
16537539
uniprot
proteins
pubmed
20805325
uniprot
proteins
pubmed
25592972
uniprot
proteins
pubmed
26467158
uniprot
proteins
pubmed
7590346
uniprot
proteins
pubmed
9061364
uniprot
proteins
sequence_length
538
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q09327}; Single-pass type II membrane protein {ECO:0000255}. Note=Colocalizes with ST6GAL1 and B4GALT1 in the Golgi stacks of cisternae, including the cis-part of the Golgi stacks. {ECO:0000250|UniProtKB:Q09327}.
uniprot
proteins
transmembrane_region
TRANSMEM 8..23; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins