MGT4C_MOUSE
ID MGT4C_MOUSE Reviewed; 478 AA.
AC Q9D306; Q9D2X2;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase C;
DE EC=2.4.1.145;
DE AltName: Full=N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IVc;
DE Short=GnT-IVc;
DE Short=N-acetylglucosaminyltransferase IVc;
DE AltName: Full=UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IVc;
GN Name=Mgat4c;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum, and Colon;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Glycosyltransferase that participates in the transfer of N-
CC acetylglucosamine (GlcNAc) to the core mannose residues of N-linked
CC glycans. Catalyzes the formation of the GlcNAcbeta1-4 branch on the
CC GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans.
CC Essential for the production of tri- and tetra-antennary N-linked sugar
CC chains. Does not catalyze the transfer of GlcNAc to the Manalpha1-6 arm
CC to form GlcNAcBeta1-4Manalpha1-6 linkage ('GnT-VI' activity) (By
CC similarity). {ECO:0000250}.
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)-[beta-D-GlcNAc-
CC (1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-
CC beta-D-Man-(1->4)-beta-D-GlcNAcl-(1->4)-beta-D-GlcNAc}-L-asparaginyl-
CC [protein] + UDP; Xref=Rhea:RHEA:16057, Rhea:RHEA-COMP:13526,
CC Rhea:RHEA-COMP:14374, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:60651, ChEBI:CHEBI:139507;
CC EC=2.4.1.145;
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 54 family.
CC {ECO:0000305}.
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DR EMBL; AK018574; BAB31286.1; -; mRNA.
DR EMBL; AK018672; BAB31336.1; -; mRNA.
DR EMBL; AK033482; BAC28312.1; -; mRNA.
DR EMBL; BC046987; AAH46987.1; -; mRNA.
DR CCDS; CCDS24153.1; -.
DR RefSeq; NP_001155840.1; NM_001162368.1.
DR RefSeq; NP_001155841.1; NM_001162369.1.
DR RefSeq; NP_001192027.1; NM_001205098.1.
DR RefSeq; NP_080519.2; NM_026243.4.
DR RefSeq; XP_006514065.1; XM_006514002.1.
DR RefSeq; XP_006514066.1; XM_006514003.1.
DR RefSeq; XP_006514067.1; XM_006514004.3.
DR RefSeq; XP_006514068.1; XM_006514005.2.
DR RefSeq; XP_011241840.1; XM_011243538.2.
DR RefSeq; XP_011241841.1; XM_011243539.1.
DR AlphaFoldDB; Q9D306; -.
DR STRING; 10090.ENSMUSP00000020039; -.
DR CAZy; GT54; Glycosyltransferase Family 54.
DR GlyGen; Q9D306; 2 sites.
DR PhosphoSitePlus; Q9D306; -.
DR MaxQB; Q9D306; -.
DR PaxDb; Q9D306; -.
DR PRIDE; Q9D306; -.
DR ProteomicsDB; 295661; -.
DR Antibodypedia; 2664; 99 antibodies from 22 providers.
DR DNASU; 67569; -.
DR Ensembl; ENSMUST00000020039; ENSMUSP00000020039; ENSMUSG00000019888.
DR Ensembl; ENSMUST00000120748; ENSMUSP00000114010; ENSMUSG00000019888.
DR Ensembl; ENSMUST00000163753; ENSMUSP00000131551; ENSMUSG00000019888.
DR Ensembl; ENSMUST00000179929; ENSMUSP00000135959; ENSMUSG00000019888.
DR GeneID; 67569; -.
DR KEGG; mmu:67569; -.
DR UCSC; uc007gyc.2; mouse.
DR CTD; 25834; -.
DR MGI; MGI:1914819; Mgat4c.
DR VEuPathDB; HostDB:ENSMUSG00000019888; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000155352; -.
DR HOGENOM; CLU_027046_1_0_1; -.
DR InParanoid; Q9D306; -.
DR OMA; RQCTTYL; -.
DR OrthoDB; 593094at2759; -.
DR PhylomeDB; Q9D306; -.
DR TreeFam; TF324570; -.
DR Reactome; R-MMU-975577; N-Glycan antennae elongation.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 67569; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Mgat4c; mouse.
DR PRO; PR:Q9D306; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9D306; protein.
DR Bgee; ENSMUSG00000019888; Expressed in right colon and 56 other tissues.
DR ExpressionAtlas; Q9D306; baseline and differential.
DR Genevisible; Q9D306; MM.
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:0008375; F:acetylglucosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0008454; F:alpha-1,3-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR InterPro; IPR006759; Glyco_transf_54.
DR PANTHER; PTHR12062; PTHR12062; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..478
FT /note="Alpha-1,3-mannosyl-glycoprotein 4-beta-N-
FT acetylglucosaminyltransferase C"
FT /id="PRO_0000288598"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..43
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..478
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 478 AA; 56250 MW; EC8EC991A802F1BC CRC64;
MLKFYQMKYI FQILDKMRCL RKRSTVSFLG VLVVFLLFMN LYIEDSYVLE GDKQLIRETS
THQLNSERYV HTFKDLSNFS GTINVTYRYL AATPLQRKRY LTIGLSSVKR KKGNYLLDTI
KSIFEQSSYE ELKEISVVVH LADFNSSWRD AMVQDITQKF AHHIIAGRLM VIHAPEEYYP
VLDGLKRNYN DPEDRVRFRS KQNVDYAFLL NFCANTSDYY VMLEDDVRCS RNFLTAIKKV
IASLEGTYWV TLEFSKLGYI GKLYHSHDLP RLAHFLLMFY QEMPCDWLLT HFRGLLAQKN
VIRFKPSLFQ HMGYYSSYKG TENKLKDDDF EEESFDIPDN PPASFYTNMN VFENYEASKA
YSSVDEYFWG KSPSMGDTFV IVFENPITIK KIKVNTGTED RQNDILQHGA LDVGEKLIFS
KQIRQCDTYL RLGEFKNGYF EMSDVNQKIP FDIHCMRICV TKTQKEWLII RSISIWTS
