GCNT1_MOUSE
ID GCNT1_MOUSE Reviewed; 428 AA.
AC Q09324; O35981; Q8BRB2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase;
DE EC=2.4.1.102 {ECO:0000269|PubMed:22056345};
DE AltName: Full=Core 2 beta-1,6-N-acetylglucosaminyltransferase {ECO:0000303|PubMed:9881978};
DE Short=C2GlcNAcT {ECO:0000303|PubMed:9881978};
DE AltName: Full=Core 2-branching enzyme;
DE AltName: Full=Core2-GlcNAc-transferase;
DE Short=C2GNT;
DE AltName: Full=Leukocyte type core 2 beta-1,6-N-acetylglucosaminyltransferase {ECO:0000303|PubMed:16829524};
DE Short=C2GnT-L {ECO:0000303|PubMed:16829524};
GN Name=Gcnt1;
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 [MRNA].
RC STRAIN=DBA/2J;
RA Warren C.E., Smookler D.S., Dennis J.W.;
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Kidney, and Submandibular gland;
RX PubMed=9341170; DOI=10.1074/jbc.272.43.27246;
RA Sekine M., Nara K., Suzuki A.;
RT "Tissue-specific regulation of mouse core 2 beta-1,6-N-
RT acetylglucosaminyltransferase.";
RL J. Biol. Chem. 272:27246-27252(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [4]
RP PROTEIN SEQUENCE OF 62-72; 109-116; 225-232 AND 258-265, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=7983056; DOI=10.1016/s0021-9258(18)47401-7;
RA Sekine M., Hashimoto Y., Suzuki M., Inagaki F., Takio K., Suzuki A.;
RT "Purification and characterization of UDP-GlcNAc:IV3 beta Gal-Gb4Cer beta-
RT 1,6-GlcNAc transferase from mouse kidney.";
RL J. Biol. Chem. 269:31143-31148(1994).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=9881978; DOI=10.1016/s1074-7613(00)80653-6;
RA Ellies L.G., Tsuboi S., Petryniak B., Lowe J.B., Fukuda M., Marth J.D.;
RT "Core 2 oligosaccharide biosynthesis distinguishes between selectin ligands
RT essential for leukocyte homing and inflammation.";
RL Immunity 9:881-890(1998).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, MUTAGENESIS OF CYS-217, DISULFIDE BOND, AND GLYCOSYLATION AT
RP ASN-58 AND ASN-95.
RX PubMed=12954635; DOI=10.1074/jbc.m303851200;
RA Yen T.Y., Macher B.A., Bryson S., Chang X., Tvaroska I., Tse R.,
RA Takeshita S., Lew A.M., Datti A.;
RT "Highly conserved cysteines of mouse core 2 beta1,6-N-
RT acetylglucosaminyltransferase I form a network of disulfide bonds and
RT include a thiol that affects enzyme activity.";
RL J. Biol. Chem. 278:45864-45881(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 38-428 ALONE AND IN COMPLEX WITH
RP GALBETA1-3GALNAC, DISULFIDE BOND, ACTIVE SITE, REGION, AND GLYCOSYLATION AT
RP ASN-58 AND ASN-95.
RX PubMed=16829524; DOI=10.1074/jbc.m603534200;
RA Pak J.E., Arnoux P., Zhou S., Sivarajah P., Satkunarajah M., Xing X.,
RA Rini J.M.;
RT "X-ray crystal structure of leukocyte type core 2 beta1,6-N-
RT acetylglucosaminyltransferase. Evidence for a convergence of metal ion-
RT independent glycosyltransferase mechanism.";
RL J. Biol. Chem. 281:26693-26701(2006).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 38-428 IN COMPLEX WITH
RP UDP-GLCNAC, DISULFIDE BOND, GLYCOSYLATION AT ASN-58 AND ASN-95, FUNCTION,
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-217; ARG-378 AND LYS-401.
RX PubMed=22056345; DOI=10.1016/j.jmb.2011.10.039;
RA Pak J.E., Satkunarajah M., Seetharaman J., Rini J.M.;
RT "Structural and mechanistic characterization of leukocyte-type core 2
RT beta1,6-N-acetylglucosaminyltransferase: a metal-ion-independent GT-A
RT glycosyltransferase.";
RL J. Mol. Biol. 414:798-811(2011).
CC -!- FUNCTION: Glycosyltransferase that catalyzes the transfer of an N-
CC acetylglucosamine (GlcNAc) moiety in beta1-6 linkage from UDP-GlcNAc
CC onto mucin-type core 1 O-glycan to form the branched mucin-type core 2
CC O-glycan. The catalysis is metal ion-independent and occurs with
CC inversion of the anomeric configuration of sugar donor (PubMed:9881978,
CC PubMed:12954635, PubMed:22056345). Selectively involved in synthesis of
CC mucin-type core 2 O-glycans that serve as scaffolds for the display of
CC selectin ligand sialyl Lewis X epitope by myeloid cells, with an impact
CC on homeostasis and recruitment to inflammatory sites (PubMed:9881978).
CC Can also act on glycolipid substrates. Transfers GlcNAc moiety to
CC GalGb4Cer globosides in a reaction step to the synthesis of stage-
CC specific embryonic antigen 1 (SSEA-1) determinant (PubMed:7983056). Can
CC use Galbeta1-3GalNAcalpha1-R and Galbeta1-3GalNAcbeta1-R
CC oligosaccharide derivatives as acceptor substrates (PubMed:7983056).
CC {ECO:0000269|PubMed:12954635, ECO:0000269|PubMed:22056345,
CC ECO:0000269|PubMed:7983056, ECO:0000269|PubMed:9881978}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl]-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine
CC = 3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-
CC (1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-seryl-[protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:56212, Rhea:RHEA-COMP:13922, Rhea:RHEA-
CC COMP:14419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:137949, ChEBI:CHEBI:139605; EC=2.4.1.102;
CC Evidence={ECO:0000269|PubMed:22056345};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56213;
CC Evidence={ECO:0000305|PubMed:12954635, ECO:0000305|PubMed:22056345,
CC ECO:0000305|PubMed:9881978};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl]-L-threonyl-[protein] + UDP-N-acetyl-alpha-D-
CC glucosamine = 3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-
CC glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-threonyl-
CC [protein] + H(+) + UDP; Xref=Rhea:RHEA:56216, Rhea:RHEA-COMP:13923,
CC Rhea:RHEA-COMP:14420, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:137950, ChEBI:CHEBI:139607;
CC EC=2.4.1.102; Evidence={ECO:0000269|PubMed:22056345};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56217;
CC Evidence={ECO:0000305|PubMed:12954635, ECO:0000305|PubMed:22056345,
CC ECO:0000305|PubMed:9881978};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=globoside GalGb4Cer + UDP-N-acetyl-alpha-D-glucosamine =
CC globoside GlcNAc-(beta1->6)-GalGb4Cer + H(+) + UDP;
CC Xref=Rhea:RHEA:56900, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:140691, ChEBI:CHEBI:140702;
CC Evidence={ECO:0000269|PubMed:7983056};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56901;
CC Evidence={ECO:0000305|PubMed:7983056};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GA1 + UDP-N-acetyl-alpha-D-glucosamine =
CC ganglioside beta-DGlcNAc-(1->6)-GA1 + H(+) + UDP;
CC Xref=Rhea:RHEA:69691, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:88069, ChEBI:CHEBI:187897;
CC Evidence={ECO:0000269|PubMed:7983056};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69692;
CC Evidence={ECO:0000305|PubMed:7983056};
CC -!- ACTIVITY REGULATION: Inactivated by thiol-reactive agents. Inhibited by
CC free UDP. {ECO:0000269|PubMed:12954635}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.1 mM for UDP-N-acetyl-alpha-D-glucosamine
CC {ECO:0000269|PubMed:12954635};
CC KM=0.11 mM for Beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl-R {ECO:0000269|PubMed:12954635};
CC KM=0.11 mM for Globoside GalGb4Cer {ECO:0000269|PubMed:7983056};
CC KM=0.31 mM for Ganglioside GA1 {ECO:0000269|PubMed:7983056};
CC KM=1.25 mM for and Galbeta1-3GalNAcalpha1-R
CC {ECO:0000269|PubMed:7983056};
CC KM=0.53 mM for Galbeta1-3GalNAcbeta1-R {ECO:0000269|PubMed:7983056};
CC Vmax=9.2 umol/min/mg enzyme toward beta-D-galactosyl-(1->3)-N-acetyl-
CC alpha-D-galactosaminyl-R {ECO:0000269|PubMed:12954635};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:9881978}.
CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000269|PubMed:7983056}.
CC -!- SUBUNIT: Interacts with GOLPH3; may control GCNT1 retention in the
CC Golgi. {ECO:0000250|UniProtKB:Q02742}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q02742}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q02742}. Note=Also detected in the trans-Golgi
CC network. {ECO:0000250|UniProtKB:Q02742}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney, liver, stomach, spleen, lung
CC and brain. {ECO:0000269|PubMed:7983056, ECO:0000269|PubMed:9341170}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12954635}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice show normal organogenesis and
CC fertility. The loss of core 2 O-glycans on leukocytes is associated
CC with leukocytosis and impaired neutrophil recruitment at the
CC inflammatory site, while lymphocyte homing to peripheral lymphoid
CC organs is not affected. {ECO:0000269|PubMed:9881978}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 14 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=core 2
CC beta 6 GlcNAc T1;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_574";
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DR EMBL; U19265; AAA60948.1; -; mRNA.
DR EMBL; D87332; BAA22998.1; -; mRNA.
DR EMBL; D87333; BAA22999.1; -; mRNA.
DR EMBL; AK045216; BAC32265.1; -; mRNA.
DR CCDS; CCDS29687.1; -.
DR RefSeq; NP_001129956.3; NM_001136484.3.
DR RefSeq; NP_034395.4; NM_010265.5.
DR RefSeq; NP_775618.3; NM_173442.5.
DR PDB; 2GAK; X-ray; 2.00 A; A/B=38-428.
DR PDB; 2GAM; X-ray; 2.70 A; A/B/C/D=38-428.
DR PDB; 3OTK; X-ray; 2.30 A; A/B/C/D=38-428.
DR PDBsum; 2GAK; -.
DR PDBsum; 2GAM; -.
DR PDBsum; 3OTK; -.
DR AlphaFoldDB; Q09324; -.
DR SMR; Q09324; -.
DR STRING; 10090.ENSMUSP00000133935; -.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR GlyGen; Q09324; 2 sites.
DR iPTMnet; Q09324; -.
DR PhosphoSitePlus; Q09324; -.
DR EPD; Q09324; -.
DR jPOST; Q09324; -.
DR MaxQB; Q09324; -.
DR PaxDb; Q09324; -.
DR PRIDE; Q09324; -.
DR ProteomicsDB; 265732; -.
DR Antibodypedia; 27275; 220 antibodies from 25 providers.
DR DNASU; 14537; -.
DR Ensembl; ENSMUST00000169897; ENSMUSP00000127835; ENSMUSG00000038843.
DR Ensembl; ENSMUST00000174236; ENSMUSP00000133935; ENSMUSG00000038843.
DR Ensembl; ENSMUST00000235184; ENSMUSP00000157544; ENSMUSG00000038843.
DR Ensembl; ENSMUST00000236139; ENSMUSP00000157681; ENSMUSG00000038843.
DR GeneID; 14537; -.
DR KEGG; mmu:14537; -.
DR UCSC; uc008gxm.2; mouse.
DR CTD; 2650; -.
DR MGI; MGI:95676; Gcnt1.
DR VEuPathDB; HostDB:ENSMUSG00000038843; -.
DR eggNOG; KOG0799; Eukaryota.
DR GeneTree; ENSGT00940000161348; -.
DR HOGENOM; CLU_032341_1_2_1; -.
DR InParanoid; Q09324; -.
DR OMA; APYPPCN; -.
DR OrthoDB; 868849at2759; -.
DR PhylomeDB; Q09324; -.
DR BRENDA; 2.4.1.102; 3474.
DR Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 14537; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Gcnt1; mouse.
DR EvolutionaryTrace; Q09324; -.
DR PRO; PR:Q09324; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q09324; protein.
DR Bgee; ENSMUSG00000038843; Expressed in right kidney and 198 other tissues.
DR Genevisible; Q09324; MM.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0031985; C:Golgi cisterna; ISS:UniProtKB.
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:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0003829; F:beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0060352; P:cell adhesion molecule production; ISS:UniProtKB.
DR GO; GO:0009101; P:glycoprotein biosynthetic process; ISS:UniProtKB.
DR GO; GO:0060993; P:kidney morphogenesis; IGI:MGI.
DR GO; GO:0050901; P:leukocyte tethering or rolling; ISS:UniProtKB.
DR GO; GO:0016268; P:O-glycan processing, core 2; IMP:UniProtKB.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; IMP:UniProtKB.
DR GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR GO; GO:0048729; P:tissue morphogenesis; IGI:MGI.
DR InterPro; IPR003406; Glyco_trans_14.
DR Pfam; PF02485; Branch; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Membrane; Nucleotide-binding;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..428
FT /note="Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-
FT 1,6-N-acetylglucosaminyltransferase"
FT /id="PRO_0000191396"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..428
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 5..9
FT /note="Mediates interaction with GOLPH3 and is necessary
FT and sufficient for localization to the Golgi"
FT /evidence="ECO:0000250|UniProtKB:Q02742"
FT REGION 33..121
FT /note="Stem region"
FT /evidence="ECO:0000305|PubMed:16829524"
FT REGION 122..428
FT /note="Catalytic"
FT /evidence="ECO:0000305|PubMed:16829524,
FT ECO:0000305|PubMed:22056345"
FT ACT_SITE 320
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:16829524"
FT BINDING 128..130
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:22056345,
FT ECO:0007744|PDB:3OTK"
FT BINDING 155..157
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:22056345,
FT ECO:0007744|PDB:3OTK"
FT BINDING 187
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:22056345,
FT ECO:0007744|PDB:3OTK"
FT BINDING 243
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
FT galactosaminyl group"
FT /ligand_part_id="ChEBI:CHEBI:16117"
FT /evidence="ECO:0000269|PubMed:16829524,
FT ECO:0007744|PDB:2GAM"
FT BINDING 250
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
FT galactosaminyl group"
FT /ligand_part_id="ChEBI:CHEBI:16117"
FT /evidence="ECO:0000269|PubMed:16829524,
FT ECO:0007744|PDB:2GAM"
FT BINDING 251
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
FT galactosaminyl group"
FT /ligand_part_id="ChEBI:CHEBI:16117"
FT /evidence="ECO:0000269|PubMed:16829524,
FT ECO:0007744|PDB:2GAM"
FT BINDING 254
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
FT galactosaminyl group"
FT /ligand_part_id="ChEBI:CHEBI:16117"
FT /evidence="ECO:0000269|PubMed:16829524,
FT ECO:0007744|PDB:2GAM"
FT BINDING 320
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
FT galactosaminyl group"
FT /ligand_part_id="ChEBI:CHEBI:16117"
FT /evidence="ECO:0000269|PubMed:16829524,
FT ECO:0007744|PDB:2GAM"
FT BINDING 341
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
FT galactosaminyl group"
FT /ligand_part_id="ChEBI:CHEBI:16117"
FT /evidence="ECO:0000269|PubMed:16829524,
FT ECO:0007744|PDB:2GAM"
FT BINDING 358
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_part="beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
FT galactosaminyl group"
FT /ligand_part_id="ChEBI:CHEBI:16117"
FT /evidence="ECO:0000269|PubMed:16829524,
FT ECO:0007744|PDB:2GAM"
FT BINDING 378
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:22056345,
FT ECO:0007744|PDB:3OTK"
FT BINDING 401
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:22056345,
FT ECO:0007744|PDB:3OTK"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12954635,
FT ECO:0000269|PubMed:16829524, ECO:0000269|PubMed:22056345,
FT ECO:0007744|PDB:2GAK, ECO:0007744|PDB:3OTK"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12954635,
FT ECO:0000269|PubMed:16829524, ECO:0000269|PubMed:22056345,
FT ECO:0007744|PDB:2GAK, ECO:0007744|PDB:3OTK"
FT DISULFID 59..413
FT /evidence="ECO:0000269|PubMed:12954635,
FT ECO:0000269|PubMed:16829524, ECO:0000269|PubMed:22056345,
FT ECO:0007744|PDB:2GAK, ECO:0007744|PDB:3OTK"
FT DISULFID 100..172
FT /evidence="ECO:0000269|PubMed:12954635,
FT ECO:0000269|PubMed:16829524, ECO:0000269|PubMed:22056345,
FT ECO:0007744|PDB:2GAK, ECO:0007744|PDB:3OTK"
FT DISULFID 151..199
FT /evidence="ECO:0000269|PubMed:12954635,
FT ECO:0000269|PubMed:16829524, ECO:0000269|PubMed:22056345,
FT ECO:0007744|PDB:2GAK, ECO:0007744|PDB:3OTK"
FT DISULFID 372..381
FT /evidence="ECO:0000269|PubMed:12954635,
FT ECO:0000269|PubMed:16829524, ECO:0000269|PubMed:22056345,
FT ECO:0007744|PDB:2GAK, ECO:0007744|PDB:3OTK"
FT MUTAGEN 217
FT /note="C->S: Protects from inactivation caused by air
FT oxidation or thiol-reactive agents. Reduces the affinity
FT for UDP-GlcNAc; when associated with A-378. Abolishes
FT binding to UDP-GlcNAc; when associated with A-401. Loss of
FT catalytic activity; when associated with A-378 and A-401."
FT /evidence="ECO:0000269|PubMed:12954635,
FT ECO:0000269|PubMed:22056345"
FT MUTAGEN 378
FT /note="R->A: Loss of catalytic activity; when associated
FT with S-217 and A-401. Reduces the affinity for UDP-GlcNAc;
FT when associated with S-217."
FT /evidence="ECO:0000269|PubMed:22056345"
FT MUTAGEN 401
FT /note="K->A: Loss of catalytic activity; when associated
FT with S-217 and A-378. Abolishes binding to UDP-GlcNAc; when
FT associated with S-217."
FT /evidence="ECO:0000269|PubMed:22056345"
FT CONFLICT 88
FT /note="R -> W (in Ref. 1; AAA60948 and 2; BAA22998/
FT BAA22999)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="S -> T (in Ref. 1; AAA60948)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="G -> A (in Ref. 2; BAA22998/BAA22999)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="T -> A (in Ref. 1; AAA60948 and 2; BAA22998/
FT BAA22999)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="H -> D (in Ref. 1; AAA60948 and 2; BAA22998/
FT BAA22999)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="M -> I (in Ref. 2; BAA22998/BAA22999)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="H -> R (in Ref. 1; AAA60948 and 2; BAA22998/
FT BAA22999)"
FT /evidence="ECO:0000305"
FT HELIX 59..63
FT /evidence="ECO:0007829|PDB:2GAK"
FT HELIX 67..78
FT /evidence="ECO:0007829|PDB:2GAK"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:2GAK"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:2GAK"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:2GAK"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:2GAK"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:2GAK"
FT HELIX 133..143
FT /evidence="ECO:0007829|PDB:2GAK"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:2GAK"
FT HELIX 160..171
FT /evidence="ECO:0007829|PDB:2GAK"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:2GAK"
FT HELIX 190..206
FT /evidence="ECO:0007829|PDB:2GAK"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:2GAK"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:2GAK"
FT HELIX 226..235
FT /evidence="ECO:0007829|PDB:2GAK"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:2GAK"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:2GAK"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:2GAK"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:2GAK"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:2GAK"
FT STRAND 265..272
FT /evidence="ECO:0007829|PDB:2GAK"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:2GAK"
FT HELIX 293..301
FT /evidence="ECO:0007829|PDB:2GAK"
FT HELIX 303..312
FT /evidence="ECO:0007829|PDB:2GAK"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:2GAK"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:2GAK"
FT HELIX 322..326
FT /evidence="ECO:0007829|PDB:2GAK"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:2GAK"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:2GAK"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:2GAK"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:2GAK"
FT HELIX 363..365
FT /evidence="ECO:0007829|PDB:2GAK"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:2GAK"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:2GAK"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:2GAK"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:2GAK"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:2GAK"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:2GAK"
FT HELIX 408..423
FT /evidence="ECO:0007829|PDB:2GAK"
SQ SEQUENCE 428 AA; 49839 MW; 57E54F07AFFE640B CRC64;
MLRNLFRRRL FSCPTKYYFM LLVLSLITFS VLRIHQKPEF FSVRHLELAG DDPYSNVNCT
KILQGDPEEI QKVKLEILTV QFKKRPRRTP HDYINMTRDC ASFIRTRKYI VEPLTKEEVG
FPIAYSIVVH HKIEMLDRLL RAIYMPQNFY CIHVDRKAEE SFLAAVQGIA SCFDNVFVAS
QLESVVYASW SRVKADLNCM KDLYRMNANW KYLINLCGMD FPIKTNLEIV RKLKCSTGEN
NLETEKMPPN KEERWKKRYT VVDGKLTNTG IVKAPPPLKT PLFSGSAYFV VTREYVGYVL
ENENIQKLME WAQDTYSPDE FLWATIQRIP EVPGSFPSSN KYDLSDMNAI ARFVKWQYFE
GHVSNGAPYP PCSGVHVRSV CVFGAGDLSW MLRQHHLFAN KFDMDVDPFA IQCLDEHLRH
KALENLEH
