MGT4B_HUMAN
ID MGT4B_HUMAN Reviewed; 548 AA.
AC Q9UQ53; A8MPR0; Q86TF1; Q96GH4; Q9NSK6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B {ECO:0000305};
DE EC=2.4.1.145 {ECO:0000269|PubMed:17006639};
DE AltName: Full=N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IVb;
DE Short=GlcNAc-T IVb;
DE Short=GnT-IVb;
DE Short=N-acetylglucosaminyltransferase IVb;
DE AltName: Full=UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IVb;
GN Name=MGAT4B {ECO:0000312|HGNC:HGNC:7048}; ORFNames=UNQ906/PRO1927;
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), TISSUE SPECIFICITY, CATALYTIC
RP ACTIVITY, FUNCTION, AND PATHWAY.
RC TISSUE=Lung;
RX PubMed=10372966; DOI=10.1023/a:1006951519522;
RA Yoshida A., Minowa M.T., Takamatsu S., Hara T., Ikenaga H., Takeuchi M.;
RT "A novel second isoenzyme of the human UDP-N-acetylglucosamine:alpha1,3-D-
RT mannoside beta1,4-N-acetylglucosaminyltransferase family: cDNA cloning,
RT expression, and chromosomal assignment.";
RL Glycoconj. J. 15:1115-1123(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PHE-491.
RC TISSUE=PNS, and Uterus;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 176-548 (ISOFORM 2).
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP OVEREXPRESSION 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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION,
RP AND PATHWAY.
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).
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, PubMed:10372966). Prefers complex-type N-glycans over
CC hybrid-types (PubMed:17006639). Has lower affinities for donors or
CC acceptors than MGAT4A, suggesting that, under physiological conditions,
CC it is not the main contributor in N-glycan biosynthesis
CC (PubMed:17006639). {ECO:0000269|PubMed:10372966,
CC 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:10372966,
CC ECO:0000269|PubMed:17006639};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16058;
CC Evidence={ECO:0000269|PubMed:10372966, 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.242 mM for UDP-GlcNAc {ECO:0000269|PubMed:17006639};
CC KM=10.5 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=5.72 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}-L-Asn residue {ECO:0000269|PubMed:17006639};
CC KM=3.35 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}-Asn residue
CC {ECO:0000269|PubMed:17006639};
CC KM=0.341 mM for UDP-GlcNAc (soluble form)
CC {ECO:0000269|PubMed:17006639};
CC KM=6.94 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=0.792 pmol/min/mg enzyme (for N(4)-{beta-D-GlcNAc-(1->2)-alpha-
CC D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-{beta-D-GlcNAc-(1->6)}-alpha-D-
CC Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-
CC Asn residue) {ECO:0000269|PubMed:17006639};
CC Vmax=0.887 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=1.64 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=46.6 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 -!- INTERACTION:
CC Q9UQ53; Q92624: APPBP2; NbExp=3; IntAct=EBI-725713, EBI-743771;
CC Q9UQ53; Q96CV9: OPTN; NbExp=3; IntAct=EBI-725713, EBI-748974;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9D4R2}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q9D4R2}. Note=A processed soluble form also
CC exists. {ECO:0000269|PubMed:17006639}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UQ53-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UQ53-2; Sequence=VSP_025716;
CC Name=3;
CC IsoId=Q9UQ53-3; Sequence=VSP_043231;
CC -!- TISSUE SPECIFICITY: Widely expressed. Strongly overexpressed in
CC pancreatic cancer. {ECO:0000269|PubMed:10372966}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17006639}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 54 family.
CC {ECO:0000305}.
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DR EMBL; AB000624; BAA83464.1; -; mRNA.
DR EMBL; AY358984; AAQ89343.1; -; mRNA.
DR EMBL; AK023137; BAG51162.1; -; mRNA.
DR EMBL; AC008393; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471165; EAW53791.1; -; Genomic_DNA.
DR EMBL; BC009464; AAH09464.2; -; mRNA.
DR EMBL; BC051835; AAH51835.1; -; mRNA.
DR EMBL; AL162067; CAB82404.2; -; mRNA.
DR CCDS; CCDS4448.1; -. [Q9UQ53-1]
DR CCDS; CCDS4449.1; -. [Q9UQ53-3]
DR PIR; T47170; T47170.
DR RefSeq; NP_055090.1; NM_014275.4. [Q9UQ53-1]
DR RefSeq; NP_463459.1; NM_054013.3. [Q9UQ53-3]
DR AlphaFoldDB; Q9UQ53; -.
DR SMR; Q9UQ53; -.
DR BioGRID; 116438; 31.
DR CORUM; Q9UQ53; -.
DR IntAct; Q9UQ53; 8.
DR STRING; 9606.ENSP00000338487; -.
DR CAZy; GT54; Glycosyltransferase Family 54.
DR GlyGen; Q9UQ53; 2 sites.
DR iPTMnet; Q9UQ53; -.
DR PhosphoSitePlus; Q9UQ53; -.
DR BioMuta; MGAT4B; -.
DR DMDM; 74735195; -.
DR EPD; Q9UQ53; -.
DR jPOST; Q9UQ53; -.
DR MassIVE; Q9UQ53; -.
DR MaxQB; Q9UQ53; -.
DR PaxDb; Q9UQ53; -.
DR PeptideAtlas; Q9UQ53; -.
DR PRIDE; Q9UQ53; -.
DR ProteomicsDB; 85509; -. [Q9UQ53-1]
DR ProteomicsDB; 85510; -. [Q9UQ53-2]
DR ProteomicsDB; 85511; -. [Q9UQ53-3]
DR Antibodypedia; 29519; 80 antibodies from 17 providers.
DR DNASU; 11282; -.
DR Ensembl; ENST00000292591.12; ENSP00000292591.7; ENSG00000161013.17. [Q9UQ53-1]
DR Ensembl; ENST00000337755.9; ENSP00000338487.5; ENSG00000161013.17. [Q9UQ53-3]
DR Ensembl; ENST00000638266.2; ENSP00000492708.1; ENSG00000284501.2. [Q9UQ53-1]
DR Ensembl; ENST00000639538.1; ENSP00000491766.1; ENSG00000284501.2. [Q9UQ53-3]
DR GeneID; 11282; -.
DR KEGG; hsa:11282; -.
DR MANE-Select; ENST00000292591.12; ENSP00000292591.7; NM_014275.5; NP_055090.1.
DR UCSC; uc003mkr.4; human. [Q9UQ53-1]
DR CTD; 11282; -.
DR DisGeNET; 11282; -.
DR GeneCards; MGAT4B; -.
DR HGNC; HGNC:7048; MGAT4B.
DR HPA; ENSG00000161013; Tissue enhanced (liver).
DR MIM; 604561; gene.
DR neXtProt; NX_Q9UQ53; -.
DR OpenTargets; ENSG00000161013; -.
DR PharmGKB; PA30783; -.
DR VEuPathDB; HostDB:ENSG00000161013; -.
DR eggNOG; ENOG502QPQJ; Eukaryota.
DR GeneTree; ENSGT00940000156526; -.
DR HOGENOM; CLU_027046_3_0_1; -.
DR InParanoid; Q9UQ53; -.
DR OMA; KKNFITT; -.
DR OrthoDB; 593094at2759; -.
DR PhylomeDB; Q9UQ53; -.
DR TreeFam; TF324570; -.
DR BioCyc; MetaCyc:HS08564-MON; -.
DR BRENDA; 2.4.1.145; 2681.
DR PathwayCommons; Q9UQ53; -.
DR Reactome; R-HSA-9694548; Maturation of spike protein.
DR Reactome; R-HSA-975577; N-Glycan antennae elongation.
DR SignaLink; Q9UQ53; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 11282; 18 hits in 1079 CRISPR screens.
DR ChiTaRS; MGAT4B; human.
DR GeneWiki; MGAT4B; -.
DR GenomeRNAi; 11282; -.
DR Pharos; Q9UQ53; Tbio.
DR PRO; PR:Q9UQ53; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9UQ53; protein.
DR Bgee; ENSG00000161013; Expressed in mucosa of transverse colon and 95 other tissues.
DR ExpressionAtlas; Q9UQ53; baseline and differential.
DR Genevisible; Q9UQ53; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
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:0008375; F:acetylglucosaminyltransferase activity; IBA:GO_Central.
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:0006491; P:N-glycan processing; TAS:ProtInc.
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; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..548
FT /note="Alpha-1,3-mannosyl-glycoprotein 4-beta-N-
FT acetylglucosaminyltransferase B"
FT /id="PRO_0000288593"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..548
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT COILED 36..83
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..32
FT /note="MRLRNGTFLTLLLFCLCAFLSLSWYAALSGQK -> MSRVAGTRTDVNELLQ
FT RWTPRCVRWHTGGARRVALDRPLVTACLPPA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043231"
FT VAR_SEQ 348
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_025716"
FT VARIANT 257
FT /note="Q -> H (in dbSNP:rs190631)"
FT /id="VAR_053913"
FT VARIANT 491
FT /note="L -> F (in dbSNP:rs17854722)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_032446"
SQ SEQUENCE 548 AA; 63198 MW; 1EFF2E681D683C4D CRC64;
MRLRNGTFLT LLLFCLCAFL SLSWYAALSG QKGDVVDVYQ REFLALRDRL HAAEQESLKR
SKELNLVLDE IKRAVSERQA LRDGDGNRTW GRLTEDPRLK PWNGSHRHVL HLPTVFHHLP
HLLAKESSLQ PAVRVGQGRT GVSVVMGIPS VRREVHSYLT DTLHSLISEL SPQEKEDSVI
VVLIAETDSQ YTSAVTENIK ALFPTEIHSG LLEVISPSPH FYPDFSRLRE SFGDPKERVR
WRTKQNLDYC FLMMYAQSKG IYYVQLEDDI VAKPNYLSTM KNFALQQPSE DWMILEFSQL
GFIGKMFKSL DLSLIVEFIL MFYRDKPIDW LLDHILWVKV CNPEKDAKHC DRQKANLRIR
FKPSLFQHVG THSSLAGKIQ KLKDKDFGKQ ALRKEHVNPP AEVSTSLKTY QHFTLEKAYL
REDFFWAFTP AAGDFIRFRF FQPLRLERFF FRSGNIEHPE DKLFNTSVEV LPFDNPQSDK
EALQEGRTAT LRYPRSPDGY LQIGSFYKGV AEGEVDPAFG PLEALRLSIQ TDSPVWVILS
EIFLKKAD
