B3GA1_MOUSE
ID B3GA1_MOUSE Reviewed; 334 AA.
AC Q9CW73; Q6PIG8; Q8BXN8; Q8R531;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2016, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1 {ECO:0000250|UniProtKB:Q9P2W7};
DE EC=2.4.1.135 {ECO:0000250|UniProtKB:O35789};
DE AltName: Full=Beta-1,3-glucuronyltransferase 1;
DE AltName: Full=Glucuronosyltransferase P;
DE Short=GlcAT-P {ECO:0000250|UniProtKB:O35789};
DE AltName: Full=UDP-GlcUA:glycoprotein beta-1,3-glucuronyltransferase;
DE Short=GlcUAT-P;
GN Name=B3gat1 {ECO:0000312|MGI:MGI:1924148};
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 2).
RX PubMed=11872162; DOI=10.1093/oxfordjournals.jbchem.a003108;
RA Yamamoto S., Oka S., Saito-Ohara F., Inazawa J., Kawasaki T.;
RT "Molecular cloning and genomic analysis of mouse glucuronyltransferase
RT involved in biosynthesis of the HNK-1 epitope.";
RL J. Biochem. 131:337-347(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Retina;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 glycoproteins. Can also play a role in glycosaminoglycan
CC biosynthesis. Substrates include asialo-orosomucoid (ASOR), asialo-
CC fetuin, and asialo-neural cell adhesion molecule. Requires
CC sphingomyelin for activity: stearoyl-sphingomyelin was the most
CC effective, followed by palmitoyl-sphingomyelin and lignoceroyl-
CC sphingomyelin. Activity was demonstrated only for sphingomyelin with a
CC saturated fatty acid and not for that with an unsaturated fatty acid,
CC regardless of the length of the acyl group.
CC {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 Evidence={ECO:0000250|UniProtKB:O35789};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Homodimer. Interacts with SAR1A.
CC {ECO:0000250|UniProtKB:O35789}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O35789}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:O35789}. Secreted
CC {ECO:0000250|UniProtKB:O35789}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O35789}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:O35789}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O35789}. Secreted
CC {ECO:0000250|UniProtKB:O35789}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=sGlcAT-P {ECO:0000250|UniProtKB:O35789};
CC IsoId=Q9CW73-1; Sequence=Displayed;
CC Name=2; Synonyms=lGlcAT-P {ECO:0000250|UniProtKB:O35789};
CC IsoId=Q9CW73-2; Sequence=VSP_058539;
CC -!- PTM: The soluble form derives from the membrane form by proteolytic
CC processing. {ECO:0000250|UniProtKB:O35789}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 43 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC31996.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB055781; BAB85676.1; -; mRNA.
DR EMBL; AK003020; BAB22514.1; -; mRNA.
DR EMBL; AK044599; BAC31996.1; ALT_INIT; mRNA.
DR EMBL; AK082739; BAC38594.1; -; mRNA.
DR EMBL; AC109831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034655; AAH34655.1; -; mRNA.
DR CCDS; CCDS22936.1; -. [Q9CW73-1]
DR CCDS; CCDS80970.1; -. [Q9CW73-2]
DR PIR; JC7828; JC7828.
DR RefSeq; NP_001297695.1; NM_001310766.1. [Q9CW73-2]
DR RefSeq; NP_084068.1; NM_029792.1. [Q9CW73-1]
DR RefSeq; XP_006510737.1; XM_006510674.1. [Q9CW73-1]
DR AlphaFoldDB; Q9CW73; -.
DR SMR; Q9CW73; -.
DR STRING; 10090.ENSMUSP00000125700; -.
DR CAZy; GT43; Glycosyltransferase Family 43.
DR GlyConnect; 2318; 3 N-Linked glycans (1 site).
DR GlyGen; Q9CW73; 3 sites, 3 N-linked glycans (1 site).
DR PhosphoSitePlus; Q9CW73; -.
DR PaxDb; Q9CW73; -.
DR PRIDE; Q9CW73; -.
DR ProteomicsDB; 273456; -. [Q9CW73-1]
DR ProteomicsDB; 273457; -. [Q9CW73-2]
DR Antibodypedia; 3739; 1556 antibodies from 46 providers.
DR DNASU; 76898; -.
DR Ensembl; ENSMUST00000115269; ENSMUSP00000110924; ENSMUSG00000045994. [Q9CW73-2]
DR Ensembl; ENSMUST00000159799; ENSMUSP00000124438; ENSMUSG00000045994. [Q9CW73-2]
DR Ensembl; ENSMUST00000160899; ENSMUSP00000124067; ENSMUSG00000045994. [Q9CW73-2]
DR Ensembl; ENSMUST00000161115; ENSMUSP00000125700; ENSMUSG00000045994. [Q9CW73-1]
DR Ensembl; ENSMUST00000161431; ENSMUSP00000124752; ENSMUSG00000045994. [Q9CW73-1]
DR GeneID; 76898; -.
DR KEGG; mmu:76898; -.
DR UCSC; uc009opo.1; mouse.
DR UCSC; uc009opp.1; mouse.
DR CTD; 27087; -.
DR MGI; MGI:1924148; B3gat1.
DR VEuPathDB; HostDB:ENSMUSG00000045994; -.
DR eggNOG; KOG1476; Eukaryota.
DR GeneTree; ENSGT00940000157165; -.
DR InParanoid; Q9CW73; -.
DR OMA; DSREYCM; -.
DR OrthoDB; 901158at2759; -.
DR PhylomeDB; Q9CW73; -.
DR TreeFam; TF313522; -.
DR Reactome; R-MMU-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 76898; 1 hit in 74 CRISPR screens.
DR ChiTaRS; B3gat1; mouse.
DR PRO; PR:Q9CW73; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9CW73; protein.
DR Bgee; ENSMUSG00000045994; Expressed in cortical plate and 106 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
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:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; IDA:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
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; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Manganese; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Secreted; Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..334
FT /note="Galactosylgalactosylxylosylprotein 3-beta-
FT glucuronosyltransferase 1"
FT /id="PRO_0000195168"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..334
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 3..5
FT /note="Essential for transport from endoplasmic reticulum
FT to Golgi apparatus and interaction with SAR1A"
FT /evidence="ECO:0000250|UniProtKB:O35789"
FT REGION 245..254
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT /evidence="ECO:0000250"
FT ACT_SITE 284
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 91..93
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 195..197
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 311..313
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT SITE 228
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT /evidence="ECO:0000250"
FT SITE 321
FT /note="Interaction with galactose moiety of substrate
FT glycoprotein"
FT /evidence="ECO:0000250"
FT MOD_RES 103
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O35789"
FT MOD_RES 108
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O35789"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1
FT /note="M -> MGNEELWVQPALEM (in isoform 2)"
FT /id="VSP_058539"
FT CONFLICT 121
FT /note="E -> G (in Ref. 2; BAC31996)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 38237 MW; 2C9AD8A19AA11379 CRC64;
MPKRRDILAI VLIVLPWTLL ITVWHQSSLA PLLAVHKDEG SDPRHEAPPG ADPREYCMSD
RDIVEVVRTE YVYTRPPPWS DTLPTIHVVT PTYSRPVQKA ELTRMANTLL HVPNLHWLVV
EDAPRRTPLT ARLLRDTGLN YTHLHVETPR NYKLRGDARD PRIPRGTMQR NLALRWLRET
FPRNSTQPGV VYFADDDNTY SLELFEEMRS TRRVSVWPVA FVGGLRYEAP RVNGAGKVVG
WKTVFDPHRP FAIDMAGFAV NLRLILQRSQ AYFKLRGVKG GYQESSLLRE LVTLNDLEPK
AANCTKILVW HTRTEKPVLV NEGKKGFTDP SVEI
