GCNT1_HUMAN
ID GCNT1_HUMAN Reviewed; 428 AA.
AC Q02742; Q6DJZ4;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase;
DE EC=2.4.1.102 {ECO:0000269|PubMed:1329093};
DE AltName: Full=Core 2 beta-1,6-N-acetylglucosaminyltransferase {ECO:0000250|UniProtKB:Q09324};
DE Short=C2GlcNAcT {ECO:0000250|UniProtKB:Q09324};
DE AltName: Full=Core 2-branching enzyme;
DE AltName: Full=Core2-GlcNAc-transferase;
DE Short=C2GNT {ECO:0000303|PubMed:1329093};
DE Short=Core 2 GNT;
DE AltName: Full=Leukocyte type core 2 beta-1,6-N-acetylglucosaminyltransferase {ECO:0000250|UniProtKB:Q09324};
DE Short=C2GnT-L {ECO:0000250|UniProtKB:Q09324};
GN Name=GCNT1; Synonyms=NACGT2;
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], VARIANT VAL-152, FUNCTION, CATALYTIC ACTIVITY,
RP AND PATHWAY.
RX PubMed=1329093; DOI=10.1073/pnas.89.19.9326;
RA Bierhuizen M.F.A., Fukuda M.;
RT "Expression cloning of a cDNA encoding UDP-GlcNAc:Gal beta 1-3-GalNAc-R
RT (GlcNAc to GalNAc) beta 1-6GlcNAc transferase by gene transfer into CHO
RT cells expressing polyoma large tumor antigen.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:9326-9330(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-152.
RC TISSUE=Placenta;
RX PubMed=7579796; DOI=10.1093/glycob/5.4.417;
RA Bierhuizen M.F.A., Maemura K., Kudo S., Fukuda M.;
RT "Genomic organization of core 2 and I branching beta-1,6-N-
RT acetylglucosaminyltransferases. Implication for evolution of the beta-1,6-
RT N-acetylglucosaminyltransferase gene family.";
RL Glycobiology 5:417-425(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 FUNCTION, INTERACTION WITH GOLPH3, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 5-LEU-LEU-6 AND 7-ARG--ARG-9.
RX PubMed=23027862; DOI=10.1074/jbc.m112.346528;
RA Ali M.F., Chachadi V.B., Petrosyan A., Cheng P.W.;
RT "Golgi phosphoprotein 3 determines cell binding properties under dynamic
RT flow by controlling Golgi localization of core 2 N-
RT acetylglucosaminyltransferase 1.";
RL J. Biol. Chem. 287:39564-39577(2012).
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 (PubMed:1329093, PubMed:23027862). The catalysis is metal ion-
CC independent and occurs with inversion of the anomeric configuration of
CC sugar donor (By similarity). 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 (By similarity).
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 (By similarity). Can
CC use Galbeta1-3GalNAcalpha1- and Galbeta1-3GalNAcbeta1- oligosaccharide
CC derivatives as acceptor substrates (By similarity).
CC {ECO:0000250|UniProtKB:Q09324, ECO:0000269|PubMed:1329093,
CC ECO:0000269|PubMed:23027862}.
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:1329093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56213;
CC Evidence={ECO:0000269|PubMed:1329093};
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:1329093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56217;
CC Evidence={ECO:0000269|PubMed:1329093};
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:0000250|UniProtKB:Q09324};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56901;
CC Evidence={ECO:0000250|UniProtKB:Q09324};
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:0000250|UniProtKB:Q09324};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69692;
CC Evidence={ECO:0000250|UniProtKB:Q09324};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:1329093}.
CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000250|UniProtKB:Q09324}.
CC -!- SUBUNIT: Interacts with GOLPH3; may control GCNT1 retention in the
CC Golgi. {ECO:0000269|PubMed:23027862}.
CC -!- INTERACTION:
CC Q02742; Q9H4A6: GOLPH3; NbExp=6; IntAct=EBI-8766035, EBI-2465479;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:23027862}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:23027862}. Note=Also detected in the trans-Golgi
CC network.
CC -!- TISSUE SPECIFICITY: Highly expressed in activated T-lymphocytes and
CC myeloid cells.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 14 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Beta-1,3-
CC galactosyl-O-glycosyl-glycoprotein beta-1,6-N-
CC acetylglucosaminyltransferase;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_541";
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DR EMBL; M97347; AAA35919.1; -; mRNA.
DR EMBL; L41415; AAA96661.1; -; Genomic_DNA.
DR EMBL; AL161626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471089; EAW62580.1; -; Genomic_DNA.
DR EMBL; BC074885; AAH74885.1; -; mRNA.
DR EMBL; BC074886; AAH74886.1; -; mRNA.
DR EMBL; BC109101; AAI09102.1; -; mRNA.
DR EMBL; BC109102; AAI09103.1; -; mRNA.
DR CCDS; CCDS6653.1; -.
DR PIR; A46293; A46293.
DR RefSeq; NP_001091102.1; NM_001097633.1.
DR RefSeq; NP_001091103.1; NM_001097634.1.
DR RefSeq; NP_001091104.1; NM_001097635.1.
DR RefSeq; NP_001091105.1; NM_001097636.1.
DR RefSeq; NP_001481.2; NM_001490.4.
DR RefSeq; XP_016870109.1; XM_017014620.1.
DR RefSeq; XP_016870110.1; XM_017014621.1.
DR AlphaFoldDB; Q02742; -.
DR SMR; Q02742; -.
DR BioGRID; 108920; 35.
DR IntAct; Q02742; 19.
DR STRING; 9606.ENSP00000415454; -.
DR ChEMBL; CHEMBL2321632; -.
DR CAZy; GT14; Glycosyltransferase Family 14.
DR GlyGen; Q02742; 2 sites.
DR iPTMnet; Q02742; -.
DR PhosphoSitePlus; Q02742; -.
DR BioMuta; GCNT1; -.
DR DMDM; 218512053; -.
DR EPD; Q02742; -.
DR jPOST; Q02742; -.
DR MassIVE; Q02742; -.
DR MaxQB; Q02742; -.
DR PaxDb; Q02742; -.
DR PeptideAtlas; Q02742; -.
DR PRIDE; Q02742; -.
DR ProteomicsDB; 58117; -.
DR Antibodypedia; 27275; 220 antibodies from 25 providers.
DR DNASU; 2650; -.
DR Ensembl; ENST00000376730.5; ENSP00000365920.4; ENSG00000187210.14.
DR Ensembl; ENST00000442371.5; ENSP00000415454.1; ENSG00000187210.14.
DR Ensembl; ENST00000444201.6; ENSP00000390703.2; ENSG00000187210.14.
DR GeneID; 2650; -.
DR KEGG; hsa:2650; -.
DR MANE-Select; ENST00000376730.5; ENSP00000365920.4; NM_001490.5; NP_001481.2.
DR UCSC; uc004akf.5; human.
DR CTD; 2650; -.
DR DisGeNET; 2650; -.
DR GeneCards; GCNT1; -.
DR HGNC; HGNC:4203; GCNT1.
DR HPA; ENSG00000187210; Group enriched (intestine, parathyroid gland, stomach, thyroid gland).
DR MIM; 600391; gene.
DR neXtProt; NX_Q02742; -.
DR OpenTargets; ENSG00000187210; -.
DR PharmGKB; PA168; -.
DR VEuPathDB; HostDB:ENSG00000187210; -.
DR eggNOG; KOG0799; Eukaryota.
DR GeneTree; ENSGT00940000161348; -.
DR HOGENOM; CLU_032341_1_2_1; -.
DR InParanoid; Q02742; -.
DR OMA; APYPPCN; -.
DR OrthoDB; 868849at2759; -.
DR PhylomeDB; Q02742; -.
DR TreeFam; TF315534; -.
DR BioCyc; MetaCyc:HS05939-MON; -.
DR BRENDA; 2.4.1.102; 2681.
DR PathwayCommons; Q02742; -.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR SignaLink; Q02742; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 2650; 15 hits in 1072 CRISPR screens.
DR ChiTaRS; GCNT1; human.
DR GeneWiki; GCNT1; -.
DR GenomeRNAi; 2650; -.
DR Pharos; Q02742; Tbio.
DR PRO; PR:Q02742; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q02742; protein.
DR Bgee; ENSG00000187210; Expressed in duodenum and 132 other tissues.
DR Genevisible; Q02742; HS.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0031985; C:Golgi cisterna; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0060352; P:cell adhesion molecule production; IMP:UniProtKB.
DR GO; GO:0009101; P:glycoprotein biosynthetic process; IMP:UniProtKB.
DR GO; GO:0060993; P:kidney morphogenesis; IEA:Ensembl.
DR GO; GO:0050901; P:leukocyte tethering or rolling; IMP:UniProtKB.
DR GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
DR GO; GO:0016268; P:O-glycan processing, core 2; IDA:UniProtKB.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; IEA:Ensembl.
DR GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR GO; GO:0048729; P:tissue morphogenesis; IEA:Ensembl.
DR InterPro; IPR003406; Glyco_trans_14.
DR Pfam; PF02485; Branch; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; 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_0000191395"
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:0000269|PubMed:23027862"
FT REGION 33..121
FT /note="Stem region"
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT REGION 122..428
FT /note="Catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT ACT_SITE 320
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT BINDING 128..130
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT BINDING 155..157
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT BINDING 187
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q09324"
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:0000250|UniProtKB:Q09324"
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:0000250|UniProtKB:Q09324"
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:0000250|UniProtKB:Q09324"
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:0000250|UniProtKB:Q09324"
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:0000250|UniProtKB:Q09324"
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:0000250|UniProtKB:Q09324"
FT BINDING 378
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT BINDING 401
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 59..413
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT DISULFID 100..172
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT DISULFID 151..199
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT DISULFID 372..381
FT /evidence="ECO:0000250|UniProtKB:Q09324"
FT VARIANT 152
FT /note="I -> V (in dbSNP:rs2282683)"
FT /evidence="ECO:0000269|PubMed:1329093,
FT ECO:0000269|PubMed:7579796"
FT /id="VAR_048000"
FT VARIANT 158
FT /note="S -> C (in dbSNP:rs11546569)"
FT /id="VAR_048001"
FT MUTAGEN 5..6
FT /note="LL->AA: Loss of interaction with GOLPH3 and loss of
FT localization to the Golgi."
FT /evidence="ECO:0000269|PubMed:23027862"
FT MUTAGEN 7..9
FT /note="RRR->AAA: Loss of interaction with GOLPH3 and loss
FT of localization to the Golgi."
FT /evidence="ECO:0000269|PubMed:23027862"
SQ SEQUENCE 428 AA; 49799 MW; 71D71A251874E1F0 CRC64;
MLRTLLRRRL FSYPTKYYFM VLVLSLITFS VLRIHQKPEF VSVRHLELAG ENPSSDINCT
KVLQGDVNEI QKVKLEILTV KFKKRPRWTP DDYINMTSDC SSFIKRRKYI VEPLSKEEAE
FPIAYSIVVH HKIEMLDRLL RAIYMPQNFY CIHVDTKSED SYLAAVMGIA SCFSNVFVAS
RLESVVYASW SRVQADLNCM KDLYAMSANW KYLINLCGMD FPIKTNLEIV RKLKLLMGEN
NLETERMPSH KEERWKKRYE VVNGKLTNTG TVKMLPPLET PLFSGSAYFV VSREYVGYVL
QNEKIQKLME WAQDTYSPDE YLWATIQRIP EVPGSLPASH KYDLSDMQAV ARFVKWQYFE
GDVSKGAPYP PCDGVHVRSV CIFGAGDLNW MLRKHHLFAN KFDVDVDLFA IQCLDEHLRH
KALETLKH
