MGAT3_RAT
ID MGAT3_RAT Reviewed; 538 AA.
AC Q02527;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase;
DE EC=2.4.1.144;
DE AltName: Full=N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III;
DE Short=GNT-III;
DE Short=GlcNAc-T III;
DE Short=N-acetylglucosaminyltransferase III;
GN Name=Mgat3; Synonyms=Gnt3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 287-297; 447-453 AND
RP 494-509.
RC STRAIN=Donryu; TISSUE=Kidney;
RX PubMed=1325461; DOI=10.1016/s0021-9258(19)37172-8;
RA Nishikawa A., Ihara Y., Hatakeyama M., Kangawa K., Taniguchi N.;
RT "Purification, cDNA cloning, and expression of UDP-N-acetylglucosamine:
RT beta-D-mannoside beta-1,4N-acetylglucosaminyltransferase III from rat
RT kidney.";
RL J. Biol. Chem. 267:18199-18204(1992).
CC -!- FUNCTION: It is involved in the regulation of the biosynthesis and
CC biological function of glycoprotein oligosaccharides. Catalyzes the
CC addition of N-acetylglucosamine in beta 1-4 linkage to the beta-linked
CC mannose of the trimannosyl core of N-linked sugar chains, called
CC bisecting N-acetylglucosamine (GlcNAc). It is one of the most important
CC enzymes involved in the regulation of the biosynthesis of glycoprotein
CC oligosaccharides. The addition of this bisecting GlcNAc residue alters
CC not only the composition, but also the conformation of the N-glycan.
CC The introduction of the bisecting GlcNAc residue results in the
CC suppression of further processing and elongation of N-glycans,
CC precluding the formation of beta-1,6 GlcNAc branching, catalyzed by
CC MGAT5 since it is unable to use the bisected oligosaccharide as a
CC substrate. Addition of bisecting N-acetylglucosamine to CDH1/E-cadherin
CC modulates CDH1 cell membrane location. Inhibits NeuAc-alpha-2,3-Gal-
CC beta-1,4-GlcNAc- formation which modulates sialylation levels and plays
CC a role in cell migration regulation (By similarity). In brain, addition
CC of bisecting N-acetylglucosamine to BACE1 blocks its lysosomal
CC targeting in response to oxidative stress and further degradation which
CC increases its location to early endosome and the APP cleavage (By
CC similarity). {ECO:0000250|UniProtKB:Q09327,
CC ECO:0000250|UniProtKB:Q10470}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-
CC (1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-
CC glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-
CC [beta-D-GlcNAc-(1->4)]-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-
CC beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-
CC [protein] + UDP; Xref=Rhea:RHEA:15509, Rhea:RHEA-COMP:13526,
CC Rhea:RHEA-COMP:14371, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:60651, ChEBI:CHEBI:139504;
CC EC=2.4.1.144;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Interacts with MGAT4D. {ECO:0000250|UniProtKB:Q10470}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II
CC membrane protein.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 17 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA01625.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D10852; BAA01625.1; ALT_INIT; mRNA.
DR PIR; A43415; A43415.
DR RefSeq; NP_062112.2; NM_019239.2.
DR RefSeq; XP_006242134.1; XM_006242072.2.
DR RefSeq; XP_006242135.1; XM_006242073.3.
DR RefSeq; XP_006242136.1; XM_006242074.3.
DR RefSeq; XP_017450192.1; XM_017594703.1.
DR AlphaFoldDB; Q02527; -.
DR STRING; 10116.ENSRNOP00000023434; -.
DR CAZy; GT17; Glycosyltransferase Family 17.
DR GlyGen; Q02527; 3 sites.
DR PaxDb; Q02527; -.
DR PRIDE; Q02527; -.
DR Ensembl; ENSRNOT00000023434; ENSRNOP00000023434; ENSRNOG00000017434.
DR Ensembl; ENSRNOT00000095447; ENSRNOP00000093292; ENSRNOG00000017434.
DR Ensembl; ENSRNOT00000097844; ENSRNOP00000080479; ENSRNOG00000017434.
DR Ensembl; ENSRNOT00000098313; ENSRNOP00000076545; ENSRNOG00000017434.
DR Ensembl; ENSRNOT00000103460; ENSRNOP00000082492; ENSRNOG00000017434.
DR Ensembl; ENSRNOT00000105515; ENSRNOP00000076485; ENSRNOG00000017434.
DR Ensembl; ENSRNOT00000109650; ENSRNOP00000082287; ENSRNOG00000017434.
DR Ensembl; ENSRNOT00000113053; ENSRNOP00000097179; ENSRNOG00000017434.
DR Ensembl; ENSRNOT00000117804; ENSRNOP00000077338; ENSRNOG00000017434.
DR Ensembl; ENSRNOT00000117832; ENSRNOP00000086583; ENSRNOG00000017434.
DR GeneID; 29582; -.
DR KEGG; rno:29582; -.
DR UCSC; RGD:3084; rat.
DR CTD; 4248; -.
DR RGD; 3084; Mgat3.
DR eggNOG; ENOG502QUBY; Eukaryota.
DR GeneTree; ENSGT00390000008221; -.
DR HOGENOM; CLU_029534_0_0_1; -.
DR InParanoid; Q02527; -.
DR OMA; DTRNAHI; -.
DR OrthoDB; 886866at2759; -.
DR PhylomeDB; Q02527; -.
DR TreeFam; TF323781; -.
DR BRENDA; 2.4.1.144; 5301.
DR Reactome; R-RNO-975574; Reactions specific to the hybrid N-glycan synthesis pathway.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q02527; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000017434; Expressed in stomach and 17 other tissues.
DR Genevisible; Q02527; RN.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003830; F:beta-1,4-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016757; F:glycosyltransferase activity; ISO:RGD.
DR GO; GO:0050435; P:amyloid-beta metabolic process; ISS:UniProtKB.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0050890; P:cognition; ISS:UniProtKB.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; ISO:RGD.
DR GO; GO:1905166; P:negative regulation of lysosomal protein catabolic process; ISS:UniProtKB.
DR GO; GO:1902966; P:positive regulation of protein localization to early endosome; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; ISS:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR InterPro; IPR006813; Glyco_trans_17.
DR PANTHER; PTHR12224; PTHR12224; 1.
DR Pfam; PF04724; Glyco_transf_17; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..538
FT /note="Beta-1,4-mannosyl-glycoprotein 4-beta-N-
FT acetylglucosaminyltransferase"
FT /id="PRO_0000188844"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..23
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..538
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 121..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 538 AA; 62022 MW; 9DCBE619284D7438 CRC64;
MKMRRYKLFL MFCMAGLCLI SFLHFFKTLS YVTFPRELAS LSPNLISSFF WNNAPVTPQA
SPEPGDPDLL RTPLYSHSPL LQPLSPSKAT EELHRVDFVL PEDTTEYFVR TKAGGVCFKP
GTRMLEKPSP GRTEEKTKVA EGSSVRGPAR RPMRHVLSAR ERLGGRGTRR KWVECVCLPG
WHGPSCGVPT VVQYSNLPTK ERLVPREVPR RVINAININH EFDLLDVRFH ELGDVVDAFV
VCESNFTAYG EPRPLKFREM LTNGTFEYIR HKVLYVFLDH FPPGGRQDGW IADDYLRTFL
TQDGVSRLRN LRPDDVFIID DADEIPARDG VLFLKLYDGW TEPFAFHMRK SLYGFFWKQP
GTLEVVSGCT IDMLQAVYGL DGIRLRRRQY YTMPNFRQYE NRTGHILVQW SLGSPLHFAG
WHCSWCFTPE GIYFKLVSAQ NGDFPRWGDY EDKRDLNYIR SLIRTGGWFD GTQQEYPPAD
PSEHMYAPKY LLKNYDQFRY LLENPYREPK STVEGGRRNQ GSDGRSSAVR GKLDTTEG
