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   24-JAN-2024, entry version 186.
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   GlyCosmos; Q9NPZ5; 2 sites, No reported glycans.
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; 9606-ENSP00000230053; -.
DR   PeptideAtlas; Q9NPZ5; -.
DR   ProteomicsDB; 82050; -.
DR   Antibodypedia; 2343; 81 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   AGR; HGNC:922; -.
DR   CTD; 135152; -.
DR   DisGeNET; 135152; -.
DR   GeneCards; B3GAT2; -.
DR   HGNC; HGNC:922; B3GAT2.
DR   HPA; ENSG00000112309; Group enriched (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; RNVALAW; -.
DR   OrthoDB; 5321308at2759; -.
DR   PhylomeDB; Q9NPZ5; -.
DR   TreeFam; TF313522; -.
DR   BioCyc; MetaCyc:HS03557-MONOMER; -.
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 1138 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 140 other cell types or tissues.
DR   ExpressionAtlas; Q9NPZ5; baseline and differential.
DR   GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
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   InterPro; IPR005027; Glyco_trans_43.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR10896:SF8; GALACTOSYLGALACTOSYLXYLOSYLPROTEIN 3-BETA-GLUCURONOSYLTRANSFERASE 2; 1.
DR   PANTHER; PTHR10896; GALACTOSYLGALACTOSYLXYLOSYLPROTEIN 3-BETA-GLUCURONOSYLTRANSFERASE BETA-1,3-GLUCURONYLTRANSFERASE; 1.
DR   Pfam; PF03360; Glyco_transf_43; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   Genevisible; Q9NPZ5; HS.
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
//