ID   MGAT2_HUMAN             Reviewed;         447 AA.
AC   Q10469; B3KPC5; B3KQM0;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, entry version 201.
DE   RecName: Full=Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase;
DE            EC=2.4.1.143 {ECO:0000269|PubMed:29666272, ECO:0000269|PubMed:7635144, ECO:0000269|PubMed:8808595};
DE   AltName: Full=Beta-1,2-N-acetylglucosaminyltransferase II;
DE   AltName: Full=GlcNAc-T II;
DE            Short=GNT-II;
DE   AltName: Full=Mannoside acetylglucosaminyltransferase 2;
DE   AltName: Full=N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II;
GN   Name=MGAT2;
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], PROTEIN SEQUENCE OF 1-16, CATALYTIC
RP   ACTIVITY, AND PATHWAY.
RC   TISSUE=Leukocyte;
RX   PubMed=7635144; DOI=10.1111/j.1432-1033.1995.tb20703.x;
RA   Tan J., D'Agostaro A.F., Bendiak B., Reck F., Sarkar M., Squire J.A.,
RA   Leong P., Schachter H.;
RT   "The human UDP-N-acetylglucosamine: alpha-6-D-mannoside-beta-1,2-N-
RT   acetylglucosaminyltransferase II gene (MGAT2). Cloning of genomic DNA,
RT   localization to chromosome 14q21, expression in insect cells and
RT   purification of the recombinant protein.";
RL   Eur. J. Biochem. 231:317-328(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
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].
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=20378551; DOI=10.1074/jbc.m110.103184;
RA   Hassinen A., Rivinoja A., Kauppila A., Kellokumpu S.;
RT   "Golgi N-glycosyltransferases form both homo- and heterodimeric enzyme
RT   complexes in live cells.";
RL   J. Biol. Chem. 285:17771-17777(2010).
RN   [6] {ECO:0007744|PDB:5VCM, ECO:0007744|PDB:5VCR, ECO:0007744|PDB:5VCS}
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 29-447 IN COMPLEXES WITH
RP   MANGANESE AND UDP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY,
RP   GLYCOSYLATION AT ASN-86, DISULFIDE BONDS, AND MUTAGENESIS OF ARG-198;
RP   ASP-217; GLU-259; TYR-294; ASN-318; TYR-344; TRP-346 AND ASP-347.
RX   PubMed=29666272; DOI=10.1073/pnas.1716988115;
RA   Kadirvelraj R., Yang J.Y., Sanders J.H., Liu L., Ramiah A., Prabhakar P.K.,
RA   Boons G.J., Wood Z.A., Moremen K.W.;
RT   "Human N-acetylglucosaminyltransferase II substrate recognition uses a
RT   modular architecture that includes a convergent exosite.";
RL   Proc. Natl. Acad. Sci. U.S.A. 115:4637-4642(2018).
RN   [7]
RP   VARIANTS CDG2A ARG-262 AND PHE-290, FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP   AND CHARACTERIZATION OF VARIANTS CDG2A ARG-262 AND PHE-290.
RX   PubMed=8808595;
RA   Tan J., Dunn J., Jaeken J., Schachter H.;
RT   "Mutations in the MGAT2 gene controlling complex N-glycan synthesis cause
RT   carbohydrate-deficient glycoprotein syndrome type II, an autosomal
RT   recessive disease with defective brain development.";
RL   Am. J. Hum. Genet. 59:810-817(1996).
RN   [8]
RP   VARIANT CDG2A ASP-318, FUNCTION, AND PATHWAY.
RX   PubMed=11228641; DOI=10.1136/jmg.37.11.875;
RA   Cormier-Daire V., Amiel J., Vuillaumier-Barrot S., Tan J., Durand G.,
RA   Munnich A., Le Merrer M., Seta N.;
RT   "Congenital disorders of glycosylation IIa cause growth retardation, mental
RT   retardation, and facial dysmorphism.";
RL   J. Med. Genet. 37:875-877(2000).
CC   -!- FUNCTION: Plays an essential role in protein N-glycosylation. Catalyzes
CC       the transfer of N-acetylglucosamine (GlcNAc) onto the free terminal
CC       mannose moiety in the core structure of the nascent N-linked glycan
CC       chain, giving rise to the second branch in complex glycans.
CC       {ECO:0000269|PubMed:11228641, ECO:0000269|PubMed:29666272,
CC       ECO:0000269|PubMed:8808595}.
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)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-
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:12941,
CC         Rhea:RHEA-COMP:13526, Rhea:RHEA-COMP:14369, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60615,
CC         ChEBI:CHEBI:60651; EC=2.4.1.143;
CC         Evidence={ECO:0000269|PubMed:29666272, ECO:0000269|PubMed:7635144,
CC         ECO:0000269|PubMed:8808595};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:29666272};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000269|PubMed:11228641, ECO:0000269|PubMed:29666272,
CC       ECO:0000269|PubMed:7635144, ECO:0000269|PubMed:8808595}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20378551}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:20378551}; Single-pass type II membrane protein
CC       {ECO:0000305}.
CC   -!- DISEASE: Congenital disorder of glycosylation 2A (CDG2A) [MIM:212066]:
CC       A multisystem disorder caused by a defect in glycoprotein biosynthesis
CC       and characterized by under-glycosylated serum glycoproteins. Congenital
CC       disorders of glycosylation result in a wide variety of clinical
CC       features, such as defects in the nervous system development,
CC       psychomotor retardation, dysmorphic features, hypotonia, coagulation
CC       disorders, and immunodeficiency. The broad spectrum of features
CC       reflects the critical role of N-glycoproteins during embryonic
CC       development, differentiation, and maintenance of cell functions.
CC       {ECO:0000269|PubMed:11228641, ECO:0000269|PubMed:8808595}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 16 (GT16) protein
CC       family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC       Note=Alpha-1,6-mannosyl-glycoprotein
CC       2-beta-N-acetylglucosaminyltransferase;
CC       URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_534";
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DR   EMBL; U15128; AAA86956.1; -; Genomic_DNA.
DR   EMBL; AK056167; BAG51637.1; -; mRNA.
DR   EMBL; AK075199; BAG52082.1; -; mRNA.
DR   EMBL; CH471078; EAW65758.1; -; Genomic_DNA.
DR   EMBL; BC006390; AAH06390.1; -; mRNA.
DR   CCDS; CCDS9690.1; -.
DR   PIR; S66256; S66256.
DR   RefSeq; NP_002399.1; NM_002408.3.
DR   PDB; 5VCM; X-ray; 1.60 A; A/B=29-447.
DR   PDB; 5VCR; X-ray; 1.99 A; A/B=29-447.
DR   PDB; 5VCS; X-ray; 2.80 A; A/B=29-447.
DR   PDBsum; 5VCM; -.
DR   PDBsum; 5VCR; -.
DR   PDBsum; 5VCS; -.
DR   AlphaFoldDB; Q10469; -.
DR   SMR; Q10469; -.
DR   BioGRID; 110403; 35.
DR   CORUM; Q10469; -.
DR   IntAct; Q10469; 7.
DR   STRING; 9606.ENSP00000307423; -.
DR   BindingDB; Q10469; -.
DR   ChEMBL; CHEMBL2321630; -.
DR   CAZy; GT16; Glycosyltransferase Family 16.
DR   GlyCosmos; Q10469; 4 sites, 1 glycan.
DR   GlyGen; Q10469; 6 sites, 3 O-linked glycans (4 sites).
DR   iPTMnet; Q10469; -.
DR   PhosphoSitePlus; Q10469; -.
DR   SwissPalm; Q10469; -.
DR   BioMuta; MGAT2; -.
DR   DMDM; 1708004; -.
DR   EPD; Q10469; -.
DR   jPOST; Q10469; -.
DR   MassIVE; Q10469; -.
DR   MaxQB; Q10469; -.
DR   PaxDb; 9606-ENSP00000307423; -.
DR   PeptideAtlas; Q10469; -.
DR   ProteomicsDB; 58853; -.
DR   Pumba; Q10469; -.
DR   Antibodypedia; 10266; 172 antibodies from 23 providers.
DR   DNASU; 4247; -.
DR   Ensembl; ENST00000305386.4; ENSP00000307423.2; ENSG00000168282.6.
DR   GeneID; 4247; -.
DR   KEGG; hsa:4247; -.
DR   MANE-Select; ENST00000305386.4; ENSP00000307423.2; NM_002408.4; NP_002399.1.
DR   UCSC; uc001wwr.4; human.
DR   AGR; HGNC:7045; -.
DR   CTD; 4247; -.
DR   DisGeNET; 4247; -.
DR   GeneCards; MGAT2; -.
DR   GeneReviews; MGAT2; -.
DR   HGNC; HGNC:7045; MGAT2.
DR   HPA; ENSG00000168282; Low tissue specificity.
DR   MalaCards; MGAT2; -.
DR   MIM; 212066; phenotype.
DR   MIM; 602616; gene.
DR   neXtProt; NX_Q10469; -.
DR   OpenTargets; ENSG00000168282; -.
DR   Orphanet; 79329; MGAT2-CDG.
DR   PharmGKB; PA30780; -.
DR   VEuPathDB; HostDB:ENSG00000168282; -.
DR   eggNOG; KOG2791; Eukaryota.
DR   GeneTree; ENSGT00390000007341; -.
DR   HOGENOM; CLU_032753_2_1_1; -.
DR   InParanoid; Q10469; -.
DR   OMA; MHHKKTC; -.
DR   OrthoDB; 3676111at2759; -.
DR   PhylomeDB; Q10469; -.
DR   TreeFam; TF314772; -.
DR   BioCyc; MetaCyc:HS09725-MONOMER; -.
DR   BRENDA; 2.4.1.143; 2681.
DR   PathwayCommons; Q10469; -.
DR   Reactome; R-HSA-4793952; Defective MGAT2 causes CDG-2a.
DR   Reactome; R-HSA-9694548; Maturation of spike protein.
DR   Reactome; R-HSA-975578; Reactions specific to the complex N-glycan synthesis pathway.
DR   SignaLink; Q10469; -.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 4247; 57 hits in 1156 CRISPR screens.
DR   ChiTaRS; MGAT2; human.
DR   GeneWiki; MGAT2; -.
DR   GenomeRNAi; 4247; -.
DR   Pharos; Q10469; Tchem.
DR   PRO; PR:Q10469; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q10469; Protein.
DR   Bgee; ENSG00000168282; Expressed in jejunal mucosa and 201 other cell types or tissues.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR   GO; GO:0005795; C:Golgi stack; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0008455; F:alpha-1,6-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0009312; P:oligosaccharide biosynthetic process; IEA:InterPro.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR   GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IDA:UniProtKB.
DR   GO; GO:0019082; P:viral protein processing; TAS:Reactome.
DR   InterPro; IPR007754; GlcNAc_II.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR12871:SF0; ALPHA-1,6-MANNOSYL-GLYCOPROTEIN 2-BETA-N-ACETYLGLUCOSAMINYLTRANSFERASE; 1.
DR   PANTHER; PTHR12871; BETA-1,2-N-ACETYLGLUCOSAMINYLTRANSFERASE II; 1.
DR   Pfam; PF05060; MGAT2; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   Genevisible; Q10469; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Congenital disorder of glycosylation;
KW   Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein;
KW   Glycosyltransferase; Golgi apparatus; Manganese; Membrane; Metal-binding;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..447
FT                   /note="Alpha-1,6-mannosyl-glycoprotein 2-beta-N-
FT                   acetylglucosaminyltransferase"
FT                   /id="PRO_0000080517"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        10..29
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..447
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   BINDING         123..127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:29666272,
FT                   ECO:0007744|PDB:5VCM"
FT   BINDING         154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:29666272,
FT                   ECO:0007744|PDB:5VCM"
FT   BINDING         229..233
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:29666272,
FT                   ECO:0007744|PDB:5VCM"
FT   BINDING         261
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000269|PubMed:29666272,
FT                   ECO:0007744|PDB:5VCM"
FT   BINDING         298
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:29666272,
FT                   ECO:0007744|PDB:5VCM"
FT   BINDING         374
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000269|PubMed:29666272,
FT                   ECO:0007744|PDB:5VCM"
FT   CARBOHYD        69
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        86
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:29666272,
FT                   ECO:0007744|PDB:5VCM, ECO:0007744|PDB:5VCR,
FT                   ECO:0007744|PDB:5VCS"
FT   DISULFID        196..210
FT                   /evidence="ECO:0000269|PubMed:29666272,
FT                   ECO:0007744|PDB:5VCM, ECO:0007744|PDB:5VCR,
FT                   ECO:0007744|PDB:5VCS"
FT   DISULFID        283..286
FT                   /evidence="ECO:0000269|PubMed:29666272,
FT                   ECO:0007744|PDB:5VCM, ECO:0007744|PDB:5VCR,
FT                   ECO:0007744|PDB:5VCS"
FT   DISULFID        334..357
FT                   /evidence="ECO:0000269|PubMed:29666272,
FT                   ECO:0007744|PDB:5VCM, ECO:0007744|PDB:5VCR,
FT                   ECO:0007744|PDB:5VCS"
FT   DISULFID        339..440
FT                   /evidence="ECO:0000269|PubMed:29666272,
FT                   ECO:0007744|PDB:5VCM, ECO:0007744|PDB:5VCR,
FT                   ECO:0007744|PDB:5VCS"
FT   DISULFID        378..386
FT                   /evidence="ECO:0000269|PubMed:29666272,
FT                   ECO:0007744|PDB:5VCM"
FT   VARIANT         262
FT                   /note="H -> R (in CDG2A; strongly reduced protein levels;
FT                   loss of enzyme activity; dbSNP:rs104894447)"
FT                   /evidence="ECO:0000269|PubMed:8808595"
FT                   /id="VAR_003415"
FT   VARIANT         290
FT                   /note="S -> F (in CDG2A; strongly reduced protein levels;
FT                   loss of enzyme activity; dbSNP:rs104894446)"
FT                   /evidence="ECO:0000269|PubMed:8808595"
FT                   /id="VAR_003416"
FT   VARIANT         318
FT                   /note="N -> D (in CDG2A; dbSNP:rs104894448)"
FT                   /evidence="ECO:0000269|PubMed:11228641"
FT                   /id="VAR_012343"
FT   MUTAGEN         198
FT                   /note="R->A: Strongly decreased catalytic activity and
FT                   affinity for UDP-GlcNAc."
FT                   /evidence="ECO:0000269|PubMed:29666272"
FT   MUTAGEN         217
FT                   /note="D->A: Nearly abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:29666272"
FT   MUTAGEN         259
FT                   /note="E->A: Loss of catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:29666272"
FT   MUTAGEN         294
FT                   /note="Y->A: Strongly decreased catalytic activity and
FT                   affinity for UDP-GlcNAc."
FT                   /evidence="ECO:0000269|PubMed:29666272"
FT   MUTAGEN         318
FT                   /note="N->A: Strongly decreased catalytic activity and
FT                   affinity for UDP-GlcNAc."
FT                   /evidence="ECO:0000269|PubMed:29666272"
FT   MUTAGEN         344
FT                   /note="Y->A: Nearly abolishes catalytic activity and
FT                   strongly decreases affinity for UDP-GlcNAc."
FT                   /evidence="ECO:0000269|PubMed:29666272"
FT   MUTAGEN         346
FT                   /note="W->A: Loss of catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:29666272"
FT   MUTAGEN         347
FT                   /note="D->A: Loss of catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:29666272"
FT   CONFLICT        299
FT                   /note="S -> R (in Ref. 2; BAG52082)"
FT                   /evidence="ECO:0000305"
FT   HELIX           87..101
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   HELIX           110..112
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   STRAND          117..124
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   HELIX           128..140
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   STRAND          148..155
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   HELIX           158..165
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   STRAND          172..176
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   TURN            181..183
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   STRAND          185..187
FT                   /evidence="ECO:0007829|PDB:5VCS"
FT   HELIX           202..208
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   TURN            211..214
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   HELIX           225..243
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   HELIX           246..248
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   STRAND          253..259
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   STRAND          262..264
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   HELIX           268..282
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   STRAND          288..291
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   TURN            301..305
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   STRAND          306..311
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   HELIX           314..317
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   STRAND          319..323
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   HELIX           325..332
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   HELIX           335..340
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   STRAND          341..344
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   HELIX           346..356
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   STRAND          358..360
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   STRAND          363..369
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   STRAND          371..374
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   TURN            380..382
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   HELIX           388..401
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   HELIX           403..405
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   STRAND          412..420
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   HELIX           434..442
FT                   /evidence="ECO:0007829|PDB:5VCM"
FT   TURN            443..445
FT                   /evidence="ECO:0007829|PDB:5VCM"
SQ   SEQUENCE   447 AA;  51550 MW;  533B76D08BD8A572 CRC64;
     MRFRIYKRKV LILTLVVAAC GFVLWSSNGR QRKNEALAPP LLDAEPARGA GGRGGDHPSV
     AVGIRRVSNV SAASLVPAVP QPEADNLTLR YRSLVYQLNF DQTLRNVDKA GTWAPRELVL
     VVQVHNRPEY LRLLLDSLRK AQGIDNVLVI FSHDFWSTEI NQLIAGVNFC PVLQVFFPFS
     IQLYPNEFPG SDPRDCPRDL PKNAALKLGC INAEYPDSFG HYREAKFSQT KHHWWWKLHF
     VWERVKILRD YAGLILFLEE DHYLAPDFYH VFKKMWKLKQ QECPECDVLS LGTYSASRSF
     YGMADKVDVK TWKSTEHNMG LALTRNAYQK LIECTDTFCT YDDYNWDWTL QYLTVSCLPK
     FWKVLVPQIP RIFHAGDCGM HHKKTCRPST QSAQIESLLN NNKQYMFPET LTISEKFTVV
     AISPPRKNGG WGDIRDHELC KSYRRLQ
//