B3GA2_HUMAN
ID B3GA2_HUMAN Reviewed; 323 AA.
AC Q9NPZ5; Q5JS09; Q8TF38; Q96NK4;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2;
DE EC=2.4.1.135 {ECO:0000250|UniProtKB:O35789};
DE AltName: Full=Beta-1,3-glucuronyltransferase 2;
DE AltName: Full=GlcAT-D;
DE AltName: Full=UDP-glucuronosyltransferase S;
DE Short=GlcAT-S;
DE Short=Glucuronosyltransferase S;
GN Name=B3GAT2; Synonyms=GLCATS, KIAA1963;
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].
RX PubMed=12522689; DOI=10.1007/s100380200103;
RA Marcos I., Galan J.J., Borrego S., Antinolo G.;
RT "Cloning, characterization, and chromosome mapping of the human GlcAT-S
RT gene.";
RL J. Hum. Genet. 47:677-680(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXII. The
RT complete sequences of 50 new cDNA clones which code for large proteins.";
RL DNA Res. 8:319-327(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-323.
RC TISSUE=Fetal brain;
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 [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 78-323.
RX PubMed=16897771; DOI=10.1002/prot.21118;
RA Shiba T., Kakuda S., Ishiguro M., Morita I., Oka S., Kawasaki T.,
RA Wakatsuki S., Kato R.;
RT "Crystal structure of GlcAT-S, a human glucuronyltransferase, involved in
RT the biosynthesis of the HNK-1 carbohydrate epitope.";
RL Proteins 65:499-508(2006).
CC -!- FUNCTION: Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope
CC on both glycolipids and glycoproteins. {ECO:0000250|UniProtKB:O35789}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-
CC xylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-
CC GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-
CC [protein] + H(+) + UDP; Xref=Rhea:RHEA:24168, Rhea:RHEA-COMP:12571,
CC Rhea:RHEA-COMP:12573, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:132090, ChEBI:CHEBI:132093;
CC EC=2.4.1.135; Evidence={ECO:0000250|UniProtKB:O35789};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II
CC membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in the trachea, retina, spinal cord,
CC hippocampus and other brain regions, and, at lower levels, in testis
CC and ovary.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 43 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB70889.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB85549.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY070019; AAL57718.1; -; mRNA.
DR EMBL; AY070110; AAL58977.1; -; Genomic_DNA.
DR EMBL; AY070108; AAL58977.1; JOINED; Genomic_DNA.
DR EMBL; AY070109; AAL58977.1; JOINED; Genomic_DNA.
DR EMBL; AB075843; BAB85549.1; ALT_INIT; mRNA.
DR EMBL; AL121961; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL450320; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK055248; BAB70889.1; ALT_INIT; mRNA.
DR CCDS; CCDS4974.1; -.
DR RefSeq; NP_542780.1; NM_080742.2.
DR PDB; 2D0J; X-ray; 2.00 A; A/B/C/D=78-323.
DR PDBsum; 2D0J; -.
DR AlphaFoldDB; Q9NPZ5; -.
DR SMR; Q9NPZ5; -.
DR BioGRID; 126422; 25.
DR IntAct; Q9NPZ5; 1.
DR STRING; 9606.ENSP00000230053; -.
DR CAZy; GT43; Glycosyltransferase Family 43.
DR GlyGen; Q9NPZ5; 2 sites.
DR iPTMnet; Q9NPZ5; -.
DR PhosphoSitePlus; Q9NPZ5; -.
DR BioMuta; B3GAT2; -.
DR DMDM; 14285363; -.
DR jPOST; Q9NPZ5; -.
DR MassIVE; Q9NPZ5; -.
DR MaxQB; Q9NPZ5; -.
DR PaxDb; Q9NPZ5; -.
DR PeptideAtlas; Q9NPZ5; -.
DR PRIDE; Q9NPZ5; -.
DR ProteomicsDB; 82050; -.
DR Antibodypedia; 2343; 78 antibodies from 19 providers.
DR DNASU; 135152; -.
DR Ensembl; ENST00000230053.11; ENSP00000230053.6; ENSG00000112309.11.
DR GeneID; 135152; -.
DR KEGG; hsa:135152; -.
DR MANE-Select; ENST00000230053.11; ENSP00000230053.6; NM_080742.3; NP_542780.1.
DR UCSC; uc003pfv.4; human.
DR CTD; 135152; -.
DR DisGeNET; 135152; -.
DR GeneCards; B3GAT2; -.
DR HGNC; HGNC:922; B3GAT2.
DR HPA; ENSG00000112309; Tissue enhanced (brain, retina).
DR MIM; 607497; gene.
DR neXtProt; NX_Q9NPZ5; -.
DR OpenTargets; ENSG00000112309; -.
DR PharmGKB; PA25216; -.
DR VEuPathDB; HostDB:ENSG00000112309; -.
DR eggNOG; KOG1476; Eukaryota.
DR GeneTree; ENSGT00940000159583; -.
DR HOGENOM; CLU_045177_2_0_1; -.
DR InParanoid; Q9NPZ5; -.
DR OMA; TRGVSIW; -.
DR OrthoDB; 901158at2759; -.
DR PhylomeDB; Q9NPZ5; -.
DR TreeFam; TF313522; -.
DR BioCyc; MetaCyc:HS03557-MON; -.
DR PathwayCommons; Q9NPZ5; -.
DR Reactome; R-HSA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR SignaLink; Q9NPZ5; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 135152; 7 hits in 1062 CRISPR screens.
DR ChiTaRS; B3GAT2; human.
DR EvolutionaryTrace; Q9NPZ5; -.
DR GeneWiki; B3GAT2; -.
DR GenomeRNAi; 135152; -.
DR Pharos; Q9NPZ5; Tbio.
DR PRO; PR:Q9NPZ5; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9NPZ5; protein.
DR Bgee; ENSG00000112309; Expressed in ventricular zone and 139 other tissues.
DR ExpressionAtlas; Q9NPZ5; baseline and differential.
DR Genevisible; Q9NPZ5; HS.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015018; F:galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:Ensembl.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0050650; P:chondroitin sulfate proteoglycan biosynthetic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR CDD; cd00218; GlcAT-I; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005027; Glyco_trans_43.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR10896; PTHR10896; 1.
DR Pfam; PF03360; Glyco_transf_43; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Golgi apparatus; Manganese; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..323
FT /note="Galactosylgalactosylxylosylprotein 3-beta-
FT glucuronosyltransferase 2"
FT /id="PRO_0000195172"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 3..23
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..323
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 51..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..243
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT /evidence="ECO:0000250"
FT ACT_SITE 273
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 87..89
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 185..187
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 300..302
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT SITE 218
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT /evidence="ECO:0000250"
FT SITE 310
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT /evidence="ECO:0000250"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:2D0J"
FT HELIX 94..105
FT /evidence="ECO:0007829|PDB:2D0J"
FT STRAND 111..121
FT /evidence="ECO:0007829|PDB:2D0J"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:2D0J"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:2D0J"
FT HELIX 157..170
FT /evidence="ECO:0007829|PDB:2D0J"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:2D0J"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:2D0J"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:2D0J"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:2D0J"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:2D0J"
FT STRAND 215..223
FT /evidence="ECO:0007829|PDB:2D0J"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:2D0J"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:2D0J"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:2D0J"
FT HELIX 251..256
FT /evidence="ECO:0007829|PDB:2D0J"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:2D0J"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:2D0J"
FT HELIX 272..278
FT /evidence="ECO:0007829|PDB:2D0J"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:2D0J"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:2D0J"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:2D0J"
SQ SEQUENCE 323 AA; 36919 MW; 85058D52D2D28463 CRC64;
MKSALFTRFF ILLPWILIVI IMLDVDTRRP VPPLTPRPYF SPYAVGRGGA RLPLRRGGPA
HGTQKRNQSR PQPQPEPQLP TIYAITPTYS RPVQKAELTR LANTFRQVAQ LHWILVEDAA
ARSELVSRFL ARAGLPSTHL HVPTPRRYKR PGLPRATEQR NAGLAWLRQR HQHQRAQPGV
LFFADDDNTY SLELFQEMRT TRKVSVWPVG LVGGRRYERP LVENGKVVGW YTGWRADRPF
AIDMAGFAVS LQVILSNPKA VFKRRGSQPG MQESDFLKQI TTVEELEPKA NNCTKVLVWH
TRTEKVNLAN EPKYHLDTVK IEV
