MGT4C_CHICK
ID MGT4C_CHICK Reviewed; 464 AA.
AC Q9DGD1;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Alpha-1,6-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase;
DE EC=2.4.1.201 {ECO:0000269|PubMed:10962001, ECO:0000269|PubMed:16428802};
DE AltName: Full=N-acetylglucosaminyltransferase VI;
DE Short=GnT-VI;
GN Name=MGAT4C;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 85-107; 173-183; 358-384
RP AND 422-431, FUNCTION, ENZYME ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=10962001; DOI=10.1074/jbc.m005860200;
RA Sakamoto Y., Taguchi T., Honke K., Korekane H., Watanabe H., Tano Y.,
RA Dohmae N., Takio K., Horii A., Taniguchi N.;
RT "Molecular cloning and expression of cDNA encoding chicken UDP-N-acetyl-D-
RT glucosamine (GlcNAc): GlcNAcbeta 1-6(GlcNAcbeta 1-2)-manalpha 1-R[GlcNAc to
RT man]beta 1,4N-acetylglucosaminyltransferase VI.";
RL J. Biol. Chem. 275:36029-36034(2000).
RN [2]
RP IDENTIFICATION, AND COFACTOR.
RX PubMed=10903319; DOI=10.1074/jbc.m004673200;
RA Taguchi T., Ogawa T., Inoue S., Inoue Y., Sakamoto Y., Korekane H.,
RA Taniguchi N.;
RT "Purification and characterization of UDP-GlcNAc: GlcNAcbeta 1-6(GlcNAcbeta
RT 1-2)Manalpha 1-R [GlcNAc to Man]-beta 1, 4-N-acetylglucosaminyltransferase
RT VI from hen oviduct.";
RL J. Biol. Chem. 275:32598-32602(2000).
RN [3]
RP ENZYME ACTIVITY.
RX PubMed=16428802; DOI=10.1093/glycob/cwj079;
RA Watanabe T., Ihara H., Miyoshi E., Honke K., Taniguchi N., Taguchi T.;
RT "A specific detection of GlcNAcbeta1-6Manalpha1 branches in N-linked
RT glycoproteins based on the specificity of N-acetylglucosaminyltransferase
RT VI.";
RL Glycobiology 16:431-439(2006).
CC -!- FUNCTION: Glycosyltransferase that catalyzes the transfer of GlcNAc to
CC the Manalpha1-6 arm to form GlcNAcBeta1-4Manalpha1-6 linkage (also
CC named 'GnT-VI' activity). May also participate in the transfer of N-
CC acetylglucosamine (GlcNAc) to the core mannose residues of N-linked
CC glycans by catalyzing the formation of the GlcNAcbeta1-4 branch on the
CC GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans.
CC {ECO:0000269|PubMed:10962001}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-
CC (1->3)-[beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->6)]-alpha-D-Man-
CC (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAcl-(1->4)-beta-D-GlcNAc}-L-
CC asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) +
CC N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-
CC [beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-[beta-D-GlcNAc-(1->6)]-
CC alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-
CC GlcNAc}-L-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:19945,
CC Rhea:RHEA-COMP:14377, Rhea:RHEA-COMP:14384, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:139510,
CC ChEBI:CHEBI:139513; EC=2.4.1.201;
CC Evidence={ECO:0000269|PubMed:10962001, ECO:0000269|PubMed:16428802};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:10903319};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in oviduct, spleen, lung and
CC colon. {ECO:0000269|PubMed:10962001}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 54 family.
CC {ECO:0000305}.
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DR EMBL; AB040608; BAB16845.1; -; mRNA.
DR RefSeq; NP_990012.1; NM_204681.2.
DR AlphaFoldDB; Q9DGD1; -.
DR SMR; Q9DGD1; -.
DR STRING; 9031.ENSGALP00000000302; -.
DR CAZy; GT54; Glycosyltransferase Family 54.
DR PaxDb; Q9DGD1; -.
DR GeneID; 395415; -.
DR KEGG; gga:395415; -.
DR CTD; 25834; -.
DR VEuPathDB; HostDB:geneid_395415; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q9DGD1; -.
DR OrthoDB; 593094at2759; -.
DR PhylomeDB; Q9DGD1; -.
DR BioCyc; MetaCyc:MON-20297; -.
DR BRENDA; 2.4.1.201; 1306.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9DGD1; -.
DR Proteomes; UP000000539; Unplaced.
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:0047253; F:alpha-1,6-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR006759; Glyco_transf_54.
DR PANTHER; PTHR12062; PTHR12062; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Metal-binding; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..464
FT /note="Alpha-1,6-mannosyl-glycoprotein 4-beta-N-
FT acetylglucosaminyltransferase"
FT /id="PRO_0000288600"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..464
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 464 AA; 52820 MW; 80946781FE1A7CA8 CRC64;
MRCSPKRSLT AVIAASFLLL LLLLLLHRGS WQDPQEVQFR DLPSDAVLKI LKQGSLHILQ
DTDNLCALHN ISYHLLAGSP LPHKKFLAVG LSSVRRPRGY YLPDTLQSLF KQSSEEELQE
MVVVVHLADA DPIWNAQVAA DISHRFAHHI LLGRLVLIHT PHEFYPTLEG LKRNYNDPEE
RVKFRSKQNV DYAFLFTFAA NLSSYYLMIE DDVWSAKSFF TAIRKAVASQ EGSNWATLEF
SKLGYIGKLY RSSDLPRLAR FLLLFYQEMP CDWLLTHFRL LLTQKDVIRF KPSLFQHMGL
YSSFQGTVNR LEDDEFQADA MDLPDNPPAA LFTNMVVFEN YEPSKAYSTA RGYFWGKNPA
VGSIFSIVFH QPARVTRVRV QTGSSERPGD FLHAGVLELG RGRRADGRDC SVYTTVGTFE
KGNLEWRGLE KGMPNPVECV RIRVTQSQSE WLIIQSIGIW TAGT
