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   02-SEP-2026, entry version 117.
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=MGAT6 {ECO:0000303|PubMed:25395405};
DE   AltName: Full=N-acetylglucosaminyltransferase VI {ECO:0000303|PubMed:10962001};
DE            Short=GlcNAc-TVI;
DE            Short=GnT-VI {ECO:0000303|PubMed:10962001};
DE   AltName: Full=N-glycan branching N-acetylglucosaminyltransferase VI {ECO:0000303|PubMed:25395405};
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, CATALYTIC 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   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
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   FUNCTION, AND CATALYTIC 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).
RN   [4]
RP   FUNCTION.
RX   PubMed=25395405; DOI=10.1093/glycob/cwu105;
RA   Abdel Rahman A.M., Ryczko M., Nakano M., Pawling J., Rodrigues T.,
RA   Johswich A., Taniguchi N., Dennis J.W.;
RT   "Golgi N-glycan branching N-acetylglucosaminyltransferases I, V and VI
RT   promote nutrient uptake and metabolism.";
RL   Glycobiology 25:225-240(2015).
CC   -!- FUNCTION: Catalyzes the transfer of N-acetylglucosamine (GlcNAc) with
CC       beta-(1,4) linkage from UDP-GlcNAc to the alpha-(1,6)-linked mannose
CC       (Man) of complex-type N-linked glycans (also named 'GnT-VI' activity).
CC       Displays strict substrate specificity adding a beta-(1,4)-linked GlcNAc
CC       branch to tri- and tetra-antennary asialoagalacto N-glycans having a
CC       GlcNAcbeta(1,2)[GlcNAcbeta-(1,6)] branching on the Manalpha-(1,6) arm
CC       (PubMed:10903319, PubMed:10962001, PubMed:16428802). High branching of
CC       N-linked glycans, as it occurs in birds, likely evolved to regulate
CC       metabolic rates and fitness in response to nutrient uptake
CC       (PubMed:25395405). {ECO:0000269|PubMed:10903319,
CC       ECO:0000269|PubMed:10962001, ECO:0000269|PubMed:16428802,
CC       ECO:0000269|PubMed:25395405}.
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-GlcNAc-(1->4)-beta-D-GlcNAc}-L-
CC         asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine =
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 + H(+); 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:10903319, ECO:0000305|PubMed:10962001};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19946;
CC         Evidence={ECO:0000305|PubMed:16428802};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-
CC         GlcNAc-(1->2)-[beta-D-GlcNAc-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-
CC         (1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] +
CC         UDP-N-acetyl-alpha-D-glucosamine = an N(4)-{beta-D-GlcNAc-(1->2)-
CC         alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-
CC         [beta-D-GlcNAc-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-
CC         GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP + H(+);
CC         Xref=Rhea:RHEA:84303, Rhea:RHEA-COMP:17733, Rhea:RHEA-COMP:20344,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:187874, ChEBI:CHEBI:233673;
CC         Evidence={ECO:0000269|PubMed:10903319, ECO:0000269|PubMed:16428802,
CC         ECO:0000305|PubMed:10962001};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84304;
CC         Evidence={ECO:0000305|PubMed:16428802};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000269|PubMed:10903319};
CC       Note=Mn(2+), Mg(2+), Co(2+) and Ni(2+) can act as cofactors.
CC       {ECO:0000269|PubMed:10903319};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.75. {ECO:0000269|PubMed:10903319};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000305|PubMed:16428802}.
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_990012.2; NM_204681.3.
DR   AlphaFoldDB; Q9DGD1; -.
DR   SMR; Q9DGD1; -.
DR   FunCoup; Q9DGD1; 26.
DR   STRING; 9031.ENSGALP00000066730; -.
DR   CAZy; CBM94; Carbohydrate-Binding Module Family 94.
DR   CAZy; GT54; Glycosyltransferase Family 54.
DR   GlyCosmos; Q9DGD1; 2 sites, No reported glycans.
DR   GlyGen; Q9DGD1; 2 sites.
DR   PaxDb; 9031-ENSGALP00000066730; -.
DR   GeneID; 395415; -.
DR   KEGG; gga:395415; -.
DR   CTD; 240755; -.
DR   VEuPathDB; HostDB:geneid_395415; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; Q9DGD1; -.
DR   OrthoDB; 2016523at2759; -.
DR   PhylomeDB; Q9DGD1; -.
DR   BioCyc; MetaCyc:MONOMER-20297; -.
DR   BRENDA; 2.4.1.201; 1306.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q9DGD1; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008375; F:acetylglucosaminyltransferase activity; IBA:GO_Central.
DR   GO; GO:0047253; F:alpha-1,6-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity; EXP:UniProtKB.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR   InterPro; IPR006759; Glyco_transf_54.
DR   InterPro; IPR057279; MGAT4.
DR   InterPro; IPR056576; MGAT4_A/B/C_C.
DR   PANTHER; PTHR12062:SF11; ALPHA-1,3-MANNOSYL-GLYCOPROTEIN 4-BETA-N-ACETYLGLUCOSAMINYLTRANSFERASE-LIKE PROTEIN MGAT4E; 1.
DR   PANTHER; PTHR12062; N-ACETYLGLUCOSAMINYLTRANSFERASE VI; 1.
DR   Pfam; PF04666; MGAT4_cons; 1.
DR   Pfam; PF23524; MGAT4A_C; 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
//