MGT4C_HUMAN
ID MGT4C_HUMAN Reviewed; 478 AA.
AC Q9UBM8; B4DRH2; Q4G199; Q9UIU5;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase C;
DE EC=2.4.1.145;
DE AltName: Full=N-acetylglucosaminyltransferase IV homolog;
DE Short=hGnT-IV-H;
DE AltName: Full=N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IVc;
DE Short=GlcNAc-T 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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
RP AND VARIANT SER-428.
RX PubMed=10570912; DOI=10.1007/s100380050186;
RA Furukawa T., Youssef E.M., Yatsuoka T., Yokoyama T., Makino N., Inoue H.,
RA Fukushige S., Hoshi M., Hayashi Y., Sunamura M., Horii A.;
RT "Cloning and characterization of the human UDP-N-acetylglucosamine: alpha-
RT 1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IV-homologue
RT (hGnT-IV-H) gene.";
RL J. Hum. Genet. 44:397-401(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-428.
RC TISSUE=Testis;
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).
RN [5]
RP FUNCTION.
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).
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 (By similarity). Does not catalyze the transfer of GlcNAc to the
CC Manalpha1-6 arm to form GlcNAcBeta1-4Manalpha1-6 linkage ('GnT-VI'
CC activity). {ECO:0000250, ECO:0000269|PubMed:10962001}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UBM8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UBM8-2; Sequence=VSP_056096;
CC -!- TISSUE SPECIFICITY: Expressed in heart, adrenal gland, testis, liver,
CC brain and fetal brain. Not expressed in pancreas.
CC {ECO:0000269|PubMed:10570912}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 54 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26068.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AB024729; BAA83074.1; -; mRNA.
DR EMBL; AB024730; BAA83075.1; -; mRNA.
DR EMBL; AB024911; BAA83087.1; -; Genomic_DNA.
DR EMBL; AK299253; BAG61284.1; -; mRNA.
DR EMBL; AC010196; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016993; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079596; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079865; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087887; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093122; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC128681; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC139663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC139697; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026068; AAH26068.1; ALT_SEQ; mRNA.
DR EMBL; BC064141; AAH64141.1; -; mRNA.
DR CCDS; CCDS9030.1; -. [Q9UBM8-1]
DR RefSeq; NP_037376.2; NM_013244.3. [Q9UBM8-1]
DR RefSeq; XP_005268833.1; XM_005268776.4.
DR RefSeq; XP_005268836.1; XM_005268779.3.
DR RefSeq; XP_011536458.1; XM_011538156.2.
DR RefSeq; XP_011536459.1; XM_011538157.2.
DR RefSeq; XP_016874634.1; XM_017019145.1.
DR RefSeq; XP_016874635.1; XM_017019146.1. [Q9UBM8-2]
DR RefSeq; XP_016874636.1; XM_017019147.1.
DR RefSeq; XP_016874637.1; XM_017019148.1.
DR RefSeq; XP_016874638.1; XM_017019149.1.
DR RefSeq; XP_016874639.1; XM_017019150.1.
DR AlphaFoldDB; Q9UBM8; -.
DR BioGRID; 117362; 39.
DR IntAct; Q9UBM8; 37.
DR STRING; 9606.ENSP00000481096; -.
DR CAZy; GT54; Glycosyltransferase Family 54.
DR GlyGen; Q9UBM8; 2 sites.
DR iPTMnet; Q9UBM8; -.
DR PhosphoSitePlus; Q9UBM8; -.
DR BioMuta; MGAT4C; -.
DR DMDM; 296437368; -.
DR jPOST; Q9UBM8; -.
DR MassIVE; Q9UBM8; -.
DR PaxDb; Q9UBM8; -.
DR PRIDE; Q9UBM8; -.
DR ProteomicsDB; 84010; -. [Q9UBM8-1]
DR Antibodypedia; 2664; 99 antibodies from 22 providers.
DR DNASU; 25834; -.
DR Ensembl; ENST00000548651.6; ENSP00000447253.1; ENSG00000182050.14. [Q9UBM8-1]
DR Ensembl; ENST00000552808.7; ENSP00000446647.1; ENSG00000182050.14. [Q9UBM8-1]
DR Ensembl; ENST00000611864.5; ENSP00000481096.1; ENSG00000182050.14. [Q9UBM8-1]
DR Ensembl; ENST00000620241.5; ENSP00000477650.1; ENSG00000182050.14. [Q9UBM8-1]
DR Ensembl; ENST00000621808.5; ENSP00000478300.1; ENSG00000182050.14. [Q9UBM8-1]
DR Ensembl; ENST00000636211.1; ENSP00000489618.1; ENSG00000283530.1. [Q9UBM8-1]
DR Ensembl; ENST00000636626.1; ENSP00000490784.1; ENSG00000283530.1. [Q9UBM8-1]
DR Ensembl; ENST00000637362.1; ENSP00000490416.1; ENSG00000283530.1. [Q9UBM8-1]
DR Ensembl; ENST00000637661.1; ENSP00000489751.1; ENSG00000283530.1. [Q9UBM8-1]
DR Ensembl; ENST00000638103.1; ENSP00000490547.1; ENSG00000283530.1. [Q9UBM8-1]
DR Ensembl; ENST00000643295.2; ENSP00000495724.1; ENSG00000285137.2. [Q9UBM8-1]
DR Ensembl; ENST00000644829.1; ENSP00000496716.1; ENSG00000285137.2. [Q9UBM8-1]
DR Ensembl; ENST00000645144.1; ENSP00000494369.1; ENSG00000285137.2. [Q9UBM8-1]
DR Ensembl; ENST00000646486.1; ENSP00000495039.1; ENSG00000285137.2. [Q9UBM8-1]
DR Ensembl; ENST00000646655.1; ENSP00000494764.1; ENSG00000285137.2. [Q9UBM8-1]
DR GeneID; 25834; -.
DR KEGG; hsa:25834; -.
DR MANE-Select; ENST00000611864.5; ENSP00000481096.1; NM_001351288.2; NP_001338217.1.
DR UCSC; uc001tai.5; human. [Q9UBM8-1]
DR CTD; 25834; -.
DR DisGeNET; 25834; -.
DR GeneCards; MGAT4C; -.
DR HGNC; HGNC:30871; MGAT4C.
DR HPA; ENSG00000182050; Tissue enhanced (epididymis, pituitary gland, testis, thyroid gland).
DR MIM; 607385; gene.
DR neXtProt; NX_Q9UBM8; -.
DR OpenTargets; ENSG00000182050; -.
DR PharmGKB; PA143485535; -.
DR VEuPathDB; HostDB:ENSG00000182050; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000155352; -.
DR InParanoid; Q9UBM8; -.
DR OMA; RQCTTYL; -.
DR OrthoDB; 593094at2759; -.
DR PhylomeDB; Q9UBM8; -.
DR TreeFam; TF324570; -.
DR BioCyc; MetaCyc:HS00017-MON; -.
DR PathwayCommons; Q9UBM8; -.
DR Reactome; R-HSA-9694548; Maturation of spike protein.
DR Reactome; R-HSA-975577; N-Glycan antennae elongation.
DR SignaLink; Q9UBM8; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 25834; 7 hits in 1063 CRISPR screens.
DR ChiTaRS; MGAT4C; human.
DR GenomeRNAi; 25834; -.
DR Pharos; Q9UBM8; Tdark.
DR PRO; PR:Q9UBM8; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9UBM8; protein.
DR Bgee; ENSG00000182050; Expressed in ventricular zone and 87 other tissues.
DR ExpressionAtlas; Q9UBM8; baseline and differential.
DR Genevisible; Q9UBM8; HS.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
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; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0019082; P:viral protein processing; TAS:Reactome.
DR InterPro; IPR006759; Glyco_transf_54.
DR PANTHER; PTHR12062; PTHR12062; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; 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_0000288596"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..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"
FT VAR_SEQ 1
FT /note="M -> MLGKDMVRFVVRKTVQRSVAKGSRRCKKRM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056096"
FT VARIANT 428
FT /note="T -> S (in dbSNP:rs17855890)"
FT /evidence="ECO:0000269|PubMed:10570912,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_032447"
SQ SEQUENCE 478 AA; 56061 MW; 7D09A1BB6B6800C6 CRC64;
MFKFHQMKHI FEILDKMRCL RKRSTVSFLG VLVIFLLFMN LYIEDSYVLE GDKQLIRETS
THQLNSERYV HTFKDLSNFS GAINVTYRYL AATPLQRKRY LTIGLSSVKR KKGNYLLETI
KSIFEQSSYE ELKEISVVVH LADFNSSWRD AMVQDITQKF AHHIIAGRLM VIHAPEEYYP
ILDGLKRNYN DPEDRVKFRS KQNVDYAFLL NFCANTSDYY VMLEDDVRCS KNFLTAIKKV
IASLEGTYWV TLEFSKLGYI GKLYHSHDLP RLAHFLLMFY QEMPCDWLLT HFRGLLAQKN
VIRFKPSLFQ HMGYYSSYKG TENKLKDDDF EEESFDIPDN PPASLYTNMN VFENYEASKA
YSSVDEYFWG KPPSTGDVFV IVFENPIIIK KIKVNTGTED RQNDILHHGA LDVGENVMPS
KQRRQCSTYL RLGEFKNGNF EMSGVNQKIP FDIHCMRIYV TKTQKEWLII RSISIWTS
