MGAT3
entrez
4248
canonical
uniprot
Q09327
canonical
ensembl
ENSG00000128268
resolver
ensp
ENSP00000345270
resolver
ensp
ENSP00000525390
resolver
ensp
ENSP00000525391
resolver
ensp
ENSP00000525392
resolver
ensp
ENSP00000525393
resolver
ensp
ENSP00000525394
resolver
ensp
ENSP00000590290
resolver
ensp
ENSP00000590291
resolver
enst
ENST00000341184
resolver
enst
ENST00000855331
resolver
enst
ENST00000855332
resolver
enst
ENST00000855333
resolver
enst
ENST00000855334
resolver
enst
ENST00000855335
resolver
enst
ENST00000920231
resolver
enst
ENST00000920232
resolver
genesymbol
MGAT3
resolver
genesymbol_syn
GGNT3
resolver
hgnc
HGNC:7046
resolver
uniprot
A6NGD0
resolver
uniprot
Q14CK5
resolver
uniprot
Q6IC49
resolver
uniprot
Q9UH32
resolver
uniprot_entry
MGAT3_HUMAN
resolver
uniprot_sec
A6NGD0
resolver
uniprot_sec
Q14CK5
resolver
uniprot_sec
Q6IC49
resolver
uniprot_sec
Q9UH32
resolver
amino_acid_sequence
MKMRRYKLFLMFCMAGLCLISFLHFFKTLSYVTFPRELASLSPNLVSSFFWNNAPVTPQASPEPGGPDLLRTPLYSHSPLLQPLPPSKAAEELHRVDLVLPEDTTEYFVRTKAGGVCFKPGTKMLERPPPGRPEEKPEGANGSSARRPPRYLLSARERTGGRGARRKWVECVCLPGWHGPSCGVPTVVQYSNLPTKERLVPREVPRRVINAINVNHEFDLLDVRFHELGDVVDAFVVCESNFTAYGEPRPLKFREMLTNGTFEYIRHKVLYVFLDHFPPGGRQDGWIADDYLRTFLTQDGVSRLRNLRPDDVFIIDDADEIPARDGVLFLKLYDGWTEPFAFHMRKSLYGFFWKQPGTLEVVSGCTVDMLQAVYGLDGIRLRRRQYYTMPNFRQYENRTGHILVQWSLGSPLHFAGWHCSWCFTPEGIYFKLVSAQNGDFPRWGDYEDKRDLNYIRGLIRTGGWFDGTQQEYPPADPSEHMYAPKYLLKNYDRFHYLLDNPYQEPRSTAAGGWRHRGPEGRPPARGKLDEAEV
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. 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 (PubMed:19403558). Addition of bisecting N-acetylglucosamine to CDH1/E-cadherin modulates CDH1 cell membrane location (PubMed:19403558). Inhibits NeuAc-alpha-2,3-Gal-beta-1,4-GlcNAc- formation which modulates sialylation levels and plays a role in cell migration regulation (PubMed:26801611). 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 (By similarity). 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:Q10470, ECO:0000269|PubMed:19403558, ECO:0000269|PubMed:26801611, ECO:0000269|PubMed:27872474, ECO:0000269|PubMed:37632720}.
uniprot
proteins
mass_dalton
61313
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:19403558, ECO:0000269|PubMed:27872474, ECO:0000269|PubMed:37632720}.
uniprot
proteins
protein_family
Glycosyltransferase 17 family
uniprot
proteins
pubmed
10591208
uniprot
proteins
pubmed
15461802
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19403558
uniprot
proteins
pubmed
26801611
uniprot
proteins
pubmed
27872474
uniprot
proteins
pubmed
29133956
uniprot
proteins
pubmed
37632720
uniprot
proteins
pubmed
8370666
uniprot
proteins
sequence_length
533
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:29133956}; 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:0000269|PubMed:29133956}.
uniprot
proteins
transmembrane_region
TRANSMEM 8..23; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins