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Database: UniProt
Entry: Q09327
LinkDB: Q09327
Original site: Q09327 
ID   MGAT3_HUMAN             Reviewed;         533 AA.
AC   Q09327; A6NGD0; Q14CK5; Q6IC49; Q9UH32;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 3.
DT   13-FEB-2019, entry version 157.
DE   RecName: Full=Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase {ECO:0000305};
DE            EC=2.4.1.144 {ECO:0000305|PubMed:19403558};
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 {ECO:0000312|HGNC:HGNC:7046}; Synonyms=GGNT3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8370666; DOI=10.1093/oxfordjournals.jbchem.a124105;
RA   Ihara Y., Nishikawa A., Toma T., Soejima H., Niikawa N., Taniguchi N.;
RT   "cDNA cloning, expression, and chromosomal localization of human N-
RT   acetylglucosaminyltransferase III (GnT-III).";
RL   J. Biochem. 113:692-698(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA   Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA   Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA   Beare D.M., Dunham I.;
RT   "A genome annotation-driven approach to cloning the human ORFeome.";
RL   Genome Biol. 5:R84.1-R84.11(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA   Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA   Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA   Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA   Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA   Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA   Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA   Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA   Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA   Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA   Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA   Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA   Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA   Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA   Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA   Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA   Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA   Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA   Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA   Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA   Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA   Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA   Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA   Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA   Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA   Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA   Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA   Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA   Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA   Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA   Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA   Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA   O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA   Khan A.S., Lane L., Tilahun Y., Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cerebellum, and Fetal brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, AND INDUCTION BY E-CADHERIN.
RX   PubMed=19403558; DOI=10.1093/hmg/ddp194;
RA   Pinho S.S., Reis C.A., Paredes J., Magalhaes A.M., Ferreira A.C.,
RA   Figueiredo J., Xiaogang W., Carneiro F., Gaertner F., Seruca R.;
RT   "The role of N-acetylglucosaminyltransferase III and V in the post-
RT   transcriptional modifications of E-cadherin.";
RL   Hum. Mol. Genet. 18:2599-2608(2009).
RN   [6]
RP   FUNCTION.
RX   PubMed=26801611; DOI=10.1074/jbc.M115.712836;
RA   Lu J., Isaji T., Im S., Fukuda T., Kameyama A., Gu J.;
RT   "Expression of N-Acetylglucosaminyltransferase III Suppresses
RT   alpha2,3-Sialylation, and Its Distinctive Functions in Cell Migration
RT   Are Attributed to alpha2,6-Sialylation Levels.";
RL   J. Biol. Chem. 291:5708-5720(2016).
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       (PubMed:19403558). Addition of bisecting N-acetylglucosamine to
CC       CDH1/E-cadherin modulates CDH1 cell membrane location
CC       (PubMed:19403558). Inhibits NeuAc-alpha-2,3-Gal-beta-1,4-
CC       GlcNAc- formation which modulates sialylation levels and plays a
CC       role in cell migration regulation (PubMed:26801611). In brain,
CC       addition of bisecting N-acetylglucosamine to BACE1 blocks its
CC       lysosomal targeting in response to oxidative stress and further
CC       degradation which increases its location to early endosome and the
CC       APP cleavage (By similarity). {ECO:0000250|UniProtKB:Q10470,
CC       ECO:0000269|PubMed:19403558, ECO:0000269|PubMed:26801611}.
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         Evidence={ECO:0000305|PubMed:19403558};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000305|PubMed:19403558}.
CC   -!- SUBUNIT: Interacts with MGAT4D. {ECO:0000250|UniProtKB:Q10470}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type
CC       II membrane protein {ECO:0000305}.
CC   -!- INDUCTION: Expression is up-regulated by CDH1/E-cadherin-mediated
CC       cell-cell interaction. {ECO:0000269|PubMed:19403558}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 17 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA02937.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC       Note=Beta-1,4-mannosyl-glycoprotein 4-beta-N-
CC       acetylglucosaminyltransferase;
CC       URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_540";
DR   EMBL; D13789; BAA02937.1; ALT_INIT; mRNA.
DR   EMBL; CR456519; CAG30405.1; -; mRNA.
DR   EMBL; AL022312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC075025; AAH75025.1; -; mRNA.
DR   EMBL; BC075026; AAH75026.1; -; mRNA.
DR   EMBL; BC113383; AAI13384.1; -; mRNA.
DR   EMBL; BC113718; AAI13719.1; -; mRNA.
DR   CCDS; CCDS13994.2; -.
DR   PIR; JN0586; JN0586.
DR   RefSeq; NP_001091740.1; NM_001098270.1.
DR   RefSeq; NP_002400.3; NM_002409.4.
DR   RefSeq; XP_005261666.1; XM_005261609.2.
DR   RefSeq; XP_011528486.1; XM_011530184.2.
DR   RefSeq; XP_011528487.1; XM_011530185.2.
DR   RefSeq; XP_011528488.1; XM_011530186.2.
DR   RefSeq; XP_011528489.1; XM_011530187.2.
DR   RefSeq; XP_011528490.1; XM_011530188.2.
DR   RefSeq; XP_011528491.1; XM_011530189.2.
DR   RefSeq; XP_011528492.1; XM_011530190.2.
DR   RefSeq; XP_011528493.1; XM_011530191.2.
DR   RefSeq; XP_011528494.1; XM_011530192.2.
DR   RefSeq; XP_011528496.1; XM_011530194.2.
DR   RefSeq; XP_016884291.1; XM_017028802.1.
DR   UniGene; Hs.276808; -.
DR   ProteinModelPortal; Q09327; -.
DR   BioGrid; 110404; 1.
DR   IntAct; Q09327; 1.
DR   STRING; 9606.ENSP00000345270; -.
DR   BindingDB; Q09327; -.
DR   ChEMBL; CHEMBL2375206; -.
DR   CAZy; GT17; Glycosyltransferase Family 17.
DR   iPTMnet; Q09327; -.
DR   PhosphoSitePlus; Q09327; -.
DR   BioMuta; MGAT3; -.
DR   DMDM; 61252497; -.
DR   jPOST; Q09327; -.
DR   PaxDb; Q09327; -.
DR   PeptideAtlas; Q09327; -.
DR   PRIDE; Q09327; -.
DR   ProteomicsDB; 58718; -.
DR   DNASU; 4248; -.
DR   Ensembl; ENST00000341184; ENSP00000345270; ENSG00000128268.
DR   GeneID; 4248; -.
DR   KEGG; hsa:4248; -.
DR   UCSC; uc003axv.6; human.
DR   CTD; 4248; -.
DR   DisGeNET; 4248; -.
DR   EuPathDB; HostDB:ENSG00000128268.11; -.
DR   GeneCards; MGAT3; -.
DR   HGNC; HGNC:7046; MGAT3.
DR   HPA; HPA017598; -.
DR   MIM; 604621; gene.
DR   neXtProt; NX_Q09327; -.
DR   OpenTargets; ENSG00000128268; -.
DR   PharmGKB; PA30781; -.
DR   eggNOG; ENOG410IEQJ; Eukaryota.
DR   eggNOG; ENOG410YQKP; LUCA.
DR   GeneTree; ENSGT00390000008221; -.
DR   HOGENOM; HOG000113579; -.
DR   HOVERGEN; HBG052468; -.
DR   InParanoid; Q09327; -.
DR   KO; K00737; -.
DR   OMA; MKMRRHK; -.
DR   OrthoDB; 886866at2759; -.
DR   PhylomeDB; Q09327; -.
DR   TreeFam; TF323781; -.
DR   BioCyc; MetaCyc:HS05168-MONOMER; -.
DR   Reactome; R-HSA-975574; Reactions specific to the hybrid N-glycan synthesis pathway.
DR   UniPathway; UPA00378; -.
DR   ChiTaRS; MGAT3; human.
DR   GeneWiki; MGAT3; -.
DR   GenomeRNAi; 4248; -.
DR   PRO; PR:Q09327; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   Bgee; ENSG00000128268; Expressed in 210 organ(s), highest expression level in anterior cingulate cortex.
DR   ExpressionAtlas; Q09327; baseline and differential.
DR   Genevisible; Q09327; HS.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR   GO; GO:0003830; F:beta-1,4-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity; IMP: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; IMP:UniProtKB.
DR   GO; GO:0006487; P:protein N-linked glycosylation; ISS:UniProtKB.
DR   GO; GO:0030334; P:regulation of cell migration; IDA:UniProtKB.
DR   InterPro; IPR006813; Glyco_trans_17.
DR   PANTHER; PTHR12224; PTHR12224; 1.
DR   Pfam; PF04724; Glyco_transf_17; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW   Membrane; Reference proteome; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    533       Beta-1,4-mannosyl-glycoprotein 4-beta-N-
FT                                acetylglucosaminyltransferase.
FT                                /FTId=PRO_0000188842.
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    533       Lumenal. {ECO:0000255}.
FT   COMPBIAS     35     86       Pro-rich.
FT   CARBOHYD    141    141       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    241    241       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    259    259       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    397    397       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CONFLICT    346    346       K -> T (in Ref. 1; BAA02937).
FT                                {ECO:0000305}.
SQ   SEQUENCE   533 AA;  61313 MW;  11F56C44A6B173AB CRC64;
     MKMRRYKLFL MFCMAGLCLI SFLHFFKTLS YVTFPRELAS LSPNLVSSFF WNNAPVTPQA
     SPEPGGPDLL RTPLYSHSPL LQPLPPSKAA EELHRVDLVL PEDTTEYFVR TKAGGVCFKP
     GTKMLERPPP GRPEEKPEGA NGSSARRPPR YLLSARERTG GRGARRKWVE CVCLPGWHGP
     SCGVPTVVQY SNLPTKERLV PREVPRRVIN AINVNHEFDL LDVRFHELGD VVDAFVVCES
     NFTAYGEPRP LKFREMLTNG TFEYIRHKVL YVFLDHFPPG GRQDGWIADD YLRTFLTQDG
     VSRLRNLRPD DVFIIDDADE IPARDGVLFL KLYDGWTEPF AFHMRKSLYG FFWKQPGTLE
     VVSGCTVDML QAVYGLDGIR LRRRQYYTMP NFRQYENRTG HILVQWSLGS PLHFAGWHCS
     WCFTPEGIYF KLVSAQNGDF PRWGDYEDKR DLNYIRGLIR TGGWFDGTQQ EYPPADPSEH
     MYAPKYLLKN YDRFHYLLDN PYQEPRSTAA GGWRHRGPEG RPPARGKLDE AEV
//
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