B3GA2_MOUSE
ID B3GA2_MOUSE Reviewed; 324 AA.
AC P59270;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2003, sequence version 1.
DT 03-AUG-2022, entry version 148.
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;
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] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=12383500; DOI=10.1016/s0378-1119(02)00840-5;
RA Imiya K., Ishizaki T., Seiki T., Saito F., Inazawa J., Oka S., Kawasaki T.;
RT "cDNA cloning, genomic structure and chromosomal mapping of the mouse
RT glucuronyltransferase-S involved in the biosynthesis of the HNK-1
RT carbohydrate epitope.";
RL Gene 296:29-36(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic head, and Kidney;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; 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).
CC -!- FUNCTION: Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope
CC on both glycolipids and glycoproteins.
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 {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P59270-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P59270-2; Sequence=VSP_001796, VSP_001797;
CC -!- TISSUE SPECIFICITY: Expressed in brain, but not in liver and kidney.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 43 family.
CC {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; AB055902; BAC20343.1; -; mRNA.
DR EMBL; AK048146; BAC33257.1; -; mRNA.
DR EMBL; AK052640; BAC35075.1; -; mRNA.
DR EMBL; BC056368; AAH56368.1; -; mRNA.
DR EMBL; BC058082; AAH58082.1; -; mRNA.
DR CCDS; CCDS14850.1; -. [P59270-1]
DR RefSeq; NP_742122.2; NM_172124.2. [P59270-1]
DR AlphaFoldDB; P59270; -.
DR SMR; P59270; -.
DR BioGRID; 235032; 1.
DR STRING; 10090.ENSMUSP00000066582; -.
DR CAZy; GT43; Glycosyltransferase Family 43.
DR GlyGen; P59270; 2 sites.
DR PhosphoSitePlus; P59270; -.
DR MaxQB; P59270; -.
DR PaxDb; P59270; -.
DR PRIDE; P59270; -.
DR ProteomicsDB; 277142; -. [P59270-1]
DR ProteomicsDB; 277143; -. [P59270-2]
DR Antibodypedia; 2343; 78 antibodies from 19 providers.
DR DNASU; 280645; -.
DR Ensembl; ENSMUST00000063663; ENSMUSP00000066582; ENSMUSG00000026156. [P59270-1]
DR Ensembl; ENSMUST00000140583; ENSMUSP00000117089; ENSMUSG00000026156. [P59270-2]
DR GeneID; 280645; -.
DR KEGG; mmu:280645; -.
DR UCSC; uc007amd.1; mouse. [P59270-2]
DR UCSC; uc007ame.1; mouse. [P59270-1]
DR CTD; 135152; -.
DR MGI; MGI:2389490; B3gat2.
DR VEuPathDB; HostDB:ENSMUSG00000026156; -.
DR eggNOG; KOG1476; Eukaryota.
DR GeneTree; ENSGT00940000159583; -.
DR HOGENOM; CLU_045177_2_0_1; -.
DR InParanoid; P59270; -.
DR OMA; TRGVSIW; -.
DR OrthoDB; 901158at2759; -.
DR PhylomeDB; P59270; -.
DR TreeFam; TF313522; -.
DR Reactome; R-MMU-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 280645; 2 hits in 70 CRISPR screens.
DR ChiTaRS; B3gat2; mouse.
DR PRO; PR:P59270; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P59270; protein.
DR Bgee; ENSMUSG00000026156; Expressed in cortical plate and 69 other tissues.
DR ExpressionAtlas; P59270; baseline and differential.
DR Genevisible; P59270; MM.
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; ISO:MGI.
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 2: Evidence at transcript level;
KW Alternative splicing; Glycoprotein; Golgi apparatus; Manganese; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..324
FT /note="Galactosylgalactosylxylosylprotein 3-beta-
FT glucuronosyltransferase 2"
FT /id="PRO_0000195173"
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..324
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 50..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..244
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT /evidence="ECO:0000250"
FT COMPBIAS 58..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 274
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 88..90
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 186..188
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 301..303
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT SITE 219
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT /evidence="ECO:0000250"
FT SITE 311
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT /evidence="ECO:0000250"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 248..302
FT /note="FAVSLQVILSNPKAVFKRRGSQPGMQESDFLKQITTVEELEPKASNCTKVLV
FT WHT -> EQNAWDICPCRMGPRRNWERPIFIKPLSVLHSSEEILIFKIGSLMVQVEVDF
FT RSG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_001796"
FT VAR_SEQ 303..324
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_001797"
FT CONFLICT 291
FT /note="A -> V (in Ref. 1; BAC20343)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 324 AA; 37132 MW; 675C549D3787B957 CRC64;
MKSALCSRFF ILLPWILIVI IMLDVDPRRP APQLTSRPYF SPHAVGCGGS RVPLRRSSPG
RDAAEKRNES RPQLQPEPRL PTIYAITPTY SRPVQKAELT RLANTFRQVA QLHWILVEDR
ATRSELVSSF LARAGLPNTH LHVPTPRRYK RPWLPRATEQ RNAGLAWLRQ RHQHQSAQPG
VLFFADDDNT YSLELFQEMR TTRKVSVWPV GLVGGRRYER PLVKNGKVVG WYTGWREDRP
FAIDMAGFAV SLQVILSNPK AVFKRRGSQP GMQESDFLKQ ITTVEELEPK ASNCTKVLVW
HTRTEKVNLA NEPKYHLDTV NIEV
