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Database: UniProt
Entry: Q02527
LinkDB: Q02527
Original site: Q02527 
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   16-JAN-2019, entry version 139.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 287-297; 447-453
RP   AND 494-509.
RC   STRAIN=Donryu; TISSUE=Kidney;
RX   PubMed=1325461;
RA   Nishikawa A., Ihara Y., Hatakeyama M., Kangawa K., Taniguchi N.;
RT   "Purification, cDNA cloning, and expression of UDP-N-
RT   acetylglucosamine: beta-D-mannoside beta-1,4N-
RT   acetylglucosaminyltransferase III from rat 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
CC       the addition of N-acetylglucosamine in beta 1-4 linkage to the
CC       beta-linked mannose of the trimannosyl core of N-linked sugar
CC       chains, called bisecting N-acetylglucosamine (GlcNAc). It is one
CC       of the most important enzymes involved in the regulation of the
CC       biosynthesis of glycoprotein oligosaccharides. The addition of
CC       this bisecting GlcNAc residue alters not only the composition, but
CC       also the conformation of the N-glycan. The introduction of the
CC       bisecting GlcNAc residue results in the suppression of further
CC       processing and elongation of N-glycans, precluding the formation
CC       of beta-1,6 GlcNAc branching, catalyzed by MGAT5 since it is
CC       unable to use the bisected oligosaccharide as a substrate.
CC       Addition of bisecting N-acetylglucosamine to CDH1/E-cadherin
CC       modulates CDH1 cell membrane location. Inhibits NeuAc-alpha-2,3-
CC       Gal-beta-1,4-GlcNAc- formation which modulates sialylation levels
CC       and plays a role in cell migration regulation (By similarity). In
CC       brain, addition of bisecting N-acetylglucosamine to BACE1 blocks
CC       its lysosomal targeting in response to oxidative stress and
CC       further degradation which increases its location to early endosome
CC       and the APP cleavage (By similarity).
CC       {ECO:0000250|UniProtKB:Q09327, ECO:0000250|UniProtKB:Q10470}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-
CC         GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-
CC         GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-
CC         acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-
CC         alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->4)]-[beta-D-GlcNAc-(1->2)-
CC         alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-
CC         D-GlcNAc}-L-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:15509,
CC         Rhea:RHEA-COMP:13526, Rhea:RHEA-COMP:14371, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60651,
CC         ChEBI:CHEBI:139504; 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
CC       II membrane protein.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 17 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA01625.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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   UniGene; Rn.9803; -.
DR   STRING; 10116.ENSRNOP00000023434; -.
DR   CAZy; GT17; Glycosyltransferase Family 17.
DR   PaxDb; Q02527; -.
DR   PRIDE; Q02527; -.
DR   Ensembl; ENSRNOT00000023434; ENSRNOP00000023434; ENSRNOG00000017434.
DR   GeneID; 29582; -.
DR   KEGG; rno:29582; -.
DR   UCSC; RGD:3084; rat.
DR   CTD; 4248; -.
DR   RGD; 3084; Mgat3.
DR   eggNOG; ENOG410IEQJ; Eukaryota.
DR   eggNOG; ENOG410YQKP; LUCA.
DR   GeneTree; ENSGT00390000008221; -.
DR   HOGENOM; HOG000113579; -.
DR   HOVERGEN; HBG052468; -.
DR   InParanoid; Q02527; -.
DR   KO; K00737; -.
DR   OMA; MKMRRHK; -.
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 10 organ(s), highest expression level in brain.
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:transferase activity, transferring glycosyl groups; IBA:GO_Central.
DR   GO; GO:0050435; P:amyloid-beta metabolic process; ISS:UniProtKB.
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; IBA:GO_Central.
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   Complete proteome; Direct protein sequencing; Glycoprotein;
KW   Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN         1    538       Beta-1,4-mannosyl-glycoprotein 4-beta-N-
FT                                acetylglucosaminyltransferase.
FT                                /FTId=PRO_0000188844.
FT   TOPO_DOM      1      7       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM      8     23       Helical; Signal-anchor for type II
FT                                membrane protein. {ECO:0000255}.
FT   TOPO_DOM     24    538       Lumenal. {ECO:0000255}.
FT   COMPBIAS     35     86       Pro-rich.
FT   CARBOHYD    245    245       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    263    263       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    401    401       N-linked (GlcNAc...) asparagine.
FT                                {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
//
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