MGT4A_HUMAN
ID MGT4A_HUMAN Reviewed; 535 AA.
AC Q9UM21; B4E2R6; D3DVH6; E9PEN2; Q53S97; Q86Z15;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A {ECO:0000305};
DE EC=2.4.1.145 {ECO:0000269|PubMed:17006639};
DE AltName: Full=N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IVa;
DE Short=GlcNAc-T IVa;
DE Short=GnT-IVa;
DE Short=N-acetylglucosaminyltransferase IVa;
DE AltName: Full=UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IVa;
DE Contains:
DE RecName: Full=Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A soluble form;
GN Name=MGAT4A {ECO:0000312|HGNC:HGNC:7047};
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=10024668; DOI=10.1093/glycob/9.3.303;
RA Yoshida A., Minowa M.T., Takamatsu S., Hara T., Oguri S., Ikenaga H.,
RA Takeuchi M.;
RT "Tissue specific expression and chromosomal mapping of a human UDP-N-
RT acetylglucosamine: alpha1,3-d-mannoside beta1, 4-N-
RT acetylglucosaminyltransferase.";
RL Glycobiology 9:303-310(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Trachea;
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
RA Minowa M.T., Takeuchi M.;
RT "Alternative splicing in human N-acetylglucosaminyltransferase IVa gene.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP OVEREXPRESSION IN CHORIOCARCINOMA.
RX PubMed=10463590;
RA Takamatsu S., Oguri S., Minowa M.T., Yoshida A., Nakamura K., Takeuchi M.,
RA Kobata A.;
RT "Unusually high expression of N-acetylglucosaminyltransferase-IVa in human
RT choriocarcinoma cell lines: a possible enzymatic basis of the formation of
RT abnormal biantennary sugar chain.";
RL Cancer Res. 59:3949-3953(1999).
RN [8]
RP DOWN-REGULATION IN PANCREATIC CANCER.
RX PubMed=16434023; DOI=10.1016/j.bbrc.2005.12.208;
RA Ide Y., Miyoshi E., Nakagawa T., Gu J., Tanemura M., Nishida T., Ito T.,
RA Yamamoto H., Kozutsumi Y., Taniguchi N.;
RT "Aberrant expression of N-acetylglucosaminyltransferase-IVa and IVb (GnT-
RT IVa and b) in pancreatic cancer.";
RL Biochem. Biophys. Res. Commun. 341:478-482(2006).
RN [9]
RP BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP GLYCOSYLATION.
RX PubMed=17006639; DOI=10.1007/s10719-006-6216-3;
RA Oguri S., Yoshida A., Minowa M.T., Takeuchi M.;
RT "Kinetic properties and substrate specificities of two recombinant human N-
RT acetylglucosaminyltransferase-IV isozymes.";
RL Glycoconj. J. 23:473-480(2006).
RN [10]
RP PHOSPHORYLATION AT SER-474.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
CC -!- FUNCTION: Glycosyltransferase that catalyze the transfer of GlcNAc from
CC UDP-GlcNAc to the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of
CC N-linked glycans through a beta1-4 linkage and participates in the
CC production of tri- and tetra-antennary N-linked sugar chains
CC (PubMed:17006639). Involved in glucose transport by mediating
CC SLC2A2/GLUT2 glycosylation, thereby controlling cell-surface expression
CC of SLC2A2 in pancreatic beta cells (By similarity).
CC {ECO:0000250|UniProtKB:Q812G0, ECO:0000269|PubMed:17006639}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[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 = H(+) +
CC N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-
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:69615,
CC Rhea:RHEA-COMP:14369, Rhea:RHEA-COMP:17732, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60615,
CC ChEBI:CHEBI:187873; Evidence={ECO:0000269|PubMed:17006639};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69616;
CC Evidence={ECO:0000305|PubMed:17006639};
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; Evidence={ECO:0000269|PubMed:17006639};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16058;
CC Evidence={ECO:0000305|PubMed:17006639};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-
CC (1->2)-{beta-D-GlcNAc-(1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP-N-
CC acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-
CC D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-{beta-D-
CC GlcNAc-(1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-
CC (1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP;
CC Xref=Rhea:RHEA:69619, Rhea:RHEA-COMP:17733, Rhea:RHEA-COMP:17734,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:187874, ChEBI:CHEBI:187875;
CC Evidence={ECO:0000269|PubMed:17006639};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69620;
CC Evidence={ECO:0000305|PubMed:17006639};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-D-Fuc-(1->6)]-
CC beta-D-GlcNAc}-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)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-[alpha-D-Fuc-(1->6)]-beta-D-GlcNAc}-asparaginyl-
CC [protein] + UDP; Xref=Rhea:RHEA:69623, Rhea:RHEA-COMP:17735,
CC Rhea:RHEA-COMP:17736, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:187876, ChEBI:CHEBI:187877;
CC Evidence={ECO:0000269|PubMed:17006639};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69624;
CC Evidence={ECO:0000305|PubMed:17006639};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)-alpha-D-Man-
CC (1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP-N-
CC acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-Gal-(1->4)-beta-D-
CC GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-
CC GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-
CC (1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP;
CC Xref=Rhea:RHEA:69627, Rhea:RHEA-COMP:17737, Rhea:RHEA-COMP:17738,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:187878, ChEBI:CHEBI:187879;
CC Evidence={ECO:0000269|PubMed:17006639};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69628;
CC Evidence={ECO:0000305|PubMed:17006639};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->3)-{alpha-D-Man-(1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP-N-
CC acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-
CC D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-{alpha-D-Man-
CC (1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC beta-D-GlcNAc}-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:69631,
CC Rhea:RHEA-COMP:17739, Rhea:RHEA-COMP:17740, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:187880,
CC ChEBI:CHEBI:187881; Evidence={ECO:0000269|PubMed:17006639};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69632;
CC Evidence={ECO:0000305|PubMed:17006639};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-beta-D-Man-
CC (1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] +
CC UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-
CC [beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-
CC GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP;
CC Xref=Rhea:RHEA:69635, Rhea:RHEA-COMP:17741, Rhea:RHEA-COMP:17742,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:187882, ChEBI:CHEBI:187883;
CC Evidence={ECO:0000269|PubMed:17006639};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69636;
CC Evidence={ECO:0000305|PubMed:17006639};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:O77836};
CC -!- ACTIVITY REGULATION: Inhibited by UDP. {ECO:0000250|UniProtKB:O77836}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.118 mM for UDP-GlcNAc {ECO:0000269|PubMed:17006639};
CC KM=3.19 mM for 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-Asn residue
CC {ECO:0000269|PubMed:17006639};
CC KM=0.971 mM for N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-
CC D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-
CC (1->4)-beta-D-GlcNAc}-L-Asn residue {ECO:0000269|PubMed:17006639};
CC KM=0.532 mM for N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-
CC D-GlcNAc-(1->2)-{beta-D-GlcNAc-(1->6)}-alpha-D-Man-(1->6)]-beta-D-
CC Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-Asn residue
CC {ECO:0000269|PubMed:17006639};
CC KM=0.358 mM for UDP-GlcNAc (soluble form)
CC {ECO:0000269|PubMed:17006639};
CC KM=1.04 mM for 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-GlcNAc-
CC (1->4)-beta-D-GlcNAc} (soluble form) {ECO:0000269|PubMed:17006639};
CC Vmax=1.17 pmol/min/mg enzyme (for N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-
CC Man-(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-Asn
CC residue) {ECO:0000269|PubMed:17006639};
CC Vmax=0.934 pmol/min/mg enzyme (for N(4)-{beta-D-GlcNAc-(1->2)-alpha-
CC D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-
CC (1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-Asn residue)
CC {ECO:0000269|PubMed:17006639};
CC Vmax=1.52 pmol/min/mg enzyme (for N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-
CC Man-(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}-Asn
CC residue) {ECO:0000269|PubMed:17006639};
CC Vmax=70.3 nmol/min/mg enzyme (for N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-
CC Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-
CC (1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-L-Asn residue} with soluble
CC form) {ECO:0000269|PubMed:17006639};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:17006639}.
CC -!- SUBCELLULAR LOCATION: [Alpha-1,3-mannosyl-glycoprotein 4-beta-N-
CC acetylglucosaminyltransferase A]: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9D4R2}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q9D4R2}.
CC -!- SUBCELLULAR LOCATION: [Alpha-1,3-mannosyl-glycoprotein 4-beta-N-
CC acetylglucosaminyltransferase A soluble form]: Secreted
CC {ECO:0000250|UniProtKB:O77836}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UM21-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UM21-2; Sequence=VSP_046075, VSP_046076, VSP_046077;
CC -!- TISSUE SPECIFICITY: Expressed in pancreas, spleen, thymus, prostate,
CC small intestine, peripheral blood leukocytes and lymph node. Strongly
CC overexpressed in choriocarcinoma cancer cell lines. Down-regulated in
CC pancreatic cancer. {ECO:0000269|PubMed:10024668}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17006639}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 54 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB000616; BAA86388.1; -; mRNA.
DR EMBL; AK304393; BAG65228.1; -; mRNA.
DR EMBL; AC064860; AAY14976.1; -; Genomic_DNA.
DR EMBL; AC109826; AAY24092.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01896.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01897.1; -; Genomic_DNA.
DR EMBL; BC127107; AAI27108.1; -; mRNA.
DR EMBL; BC127108; AAI27109.1; -; mRNA.
DR EMBL; AB053222; BAC55023.1; -; Genomic_DNA.
DR CCDS; CCDS2036.1; -. [Q9UM21-1]
DR CCDS; CCDS54380.1; -. [Q9UM21-2]
DR RefSeq; NP_001153626.1; NM_001160154.1. [Q9UM21-2]
DR RefSeq; NP_036346.1; NM_012214.2. [Q9UM21-1]
DR AlphaFoldDB; Q9UM21; -.
DR SMR; Q9UM21; -.
DR BioGRID; 116451; 1.
DR IntAct; Q9UM21; 1.
DR STRING; 9606.ENSP00000264968; -.
DR CAZy; GT54; Glycosyltransferase Family 54.
DR GlyGen; Q9UM21; 2 sites.
DR iPTMnet; Q9UM21; -.
DR PhosphoSitePlus; Q9UM21; -.
DR BioMuta; MGAT4A; -.
DR EPD; Q9UM21; -.
DR jPOST; Q9UM21; -.
DR MassIVE; Q9UM21; -.
DR MaxQB; Q9UM21; -.
DR PaxDb; Q9UM21; -.
DR PeptideAtlas; Q9UM21; -.
DR PRIDE; Q9UM21; -.
DR ProteomicsDB; 19928; -.
DR ProteomicsDB; 85172; -. [Q9UM21-1]
DR Antibodypedia; 32749; 91 antibodies from 23 providers.
DR DNASU; 11320; -.
DR Ensembl; ENST00000264968.7; ENSP00000264968.2; ENSG00000071073.13. [Q9UM21-1]
DR Ensembl; ENST00000393487.6; ENSP00000377127.1; ENSG00000071073.13. [Q9UM21-1]
DR Ensembl; ENST00000409391.1; ENSP00000386841.1; ENSG00000071073.13. [Q9UM21-1]
DR Ensembl; ENST00000414521.6; ENSP00000404889.2; ENSG00000071073.13. [Q9UM21-2]
DR GeneID; 11320; -.
DR KEGG; hsa:11320; -.
DR MANE-Select; ENST00000393487.6; ENSP00000377127.1; NM_012214.3; NP_036346.1.
DR UCSC; uc002sze.3; human. [Q9UM21-1]
DR CTD; 11320; -.
DR DisGeNET; 11320; -.
DR GeneCards; MGAT4A; -.
DR HGNC; HGNC:7047; MGAT4A.
DR HPA; ENSG00000071073; Tissue enhanced (bone).
DR MIM; 604623; gene.
DR neXtProt; NX_Q9UM21; -.
DR OpenTargets; ENSG00000071073; -.
DR PharmGKB; PA30782; -.
DR VEuPathDB; HostDB:ENSG00000071073; -.
DR eggNOG; ENOG502QPQJ; Eukaryota.
DR GeneTree; ENSGT00940000159177; -.
DR HOGENOM; CLU_027046_3_0_1; -.
DR InParanoid; Q9UM21; -.
DR OMA; ERIRWRT; -.
DR OrthoDB; 593094at2759; -.
DR PhylomeDB; Q9UM21; -.
DR TreeFam; TF324570; -.
DR BioCyc; MetaCyc:HS01024-MON; -.
DR BRENDA; 2.4.1.145; 2681.
DR PathwayCommons; Q9UM21; -.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR Reactome; R-HSA-9694548; Maturation of spike protein.
DR Reactome; R-HSA-975577; N-Glycan antennae elongation.
DR SignaLink; Q9UM21; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 11320; 31 hits in 1072 CRISPR screens.
DR ChiTaRS; MGAT4A; human.
DR GenomeRNAi; 11320; -.
DR Pharos; Q9UM21; Tbio.
DR PRO; PR:Q9UM21; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9UM21; protein.
DR Bgee; ENSG00000071073; Expressed in jejunal mucosa and 180 other tissues.
DR ExpressionAtlas; Q9UM21; baseline and differential.
DR Genevisible; Q9UM21; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005795; C:Golgi stack; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; ISS:UniProtKB.
DR GO; GO:0008454; F:alpha-1,3-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0046487; P:glyoxylate metabolic process; ISS:UniProtKB.
DR GO; GO:0006491; P:N-glycan processing; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Secreted; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..535
FT /note="Alpha-1,3-mannosyl-glycoprotein 4-beta-N-
FT acetylglucosaminyltransferase A"
FT /id="PRO_0000288581"
FT CHAIN 93..535
FT /note="Alpha-1,3-mannosyl-glycoprotein 4-beta-N-
FT acetylglucosaminyltransferase A soluble form"
FT /evidence="ECO:0000250|UniProtKB:O77836"
FT /id="PRO_0000288582"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..535
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT COILED 28..63
FT /evidence="ECO:0000255"
FT MOD_RES 474
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..6
FT /note="MRLRNG -> MNYSIT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046075"
FT VAR_SEQ 7..134
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046076"
FT VAR_SEQ 528..535
FT /note="IHIKKATN -> QRVFSGWWQKSRDKAEGPQAPLLF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046077"
FT CONFLICT 280
FT /note="L -> F (in Ref. 2; BAG65228)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 61544 MW; C139E5F323A083A1 CRC64;
MRLRNGTVAT ALAFITSFLT LSWYTTWQNG KEKLIAYQRE FLALKERLRI AEHRISQRSS
ELNTIVQQFK RVGAETNGSK DALNKFSDNT LKLLKELTSK KSLQVPSIYY HLPHLLKNEG
SLQPAVQIGN GRTGVSIVMG IPTVKREVKS YLIETLHSLI DNLYPEEKLD CVIVVFIGET
DIDYVHGVVA NLEKEFSKEI SSGLVEVISP PESYYPDLTN LKETFGDSKE RVRWRTKQNL
DYCFLMMYAQ EKGIYYIQLE DDIIVKQNYF NTIKNFALQL SSEEWMILEF SQLGFIGKMF
QAPDLTLIVE FIFMFYKEKP IDWLLDHILW VKVCNPEKDA KHCDRQKANL RIRFRPSLFQ
HVGLHSSLSG KIQKLTDKDY MKPLLLKIHV NPPAEVSTSL KVYQGHTLEK TYMGEDFFWA
ITPIAGDYIL FKFDKPVNVE SYLFHSGNQE HPGDILLNTT VEVLPFKSEG LEISKETKDK
RLEDGYFRIG KFENGVAEGM VDPSLNPISA FRLSVIQNSA VWAILNEIHI KKATN
