B3GA1_RAT
ID B3GA1_RAT Reviewed; 334 AA.
AC O35789; A0A0H2UHF1;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1 {ECO:0000250|UniProtKB:Q9P2W7};
DE EC=2.4.1.135 {ECO:0000269|PubMed:19181664};
DE AltName: Full=Beta-1,3-glucuronyltransferase 1;
DE AltName: Full=Glucuronosyltransferase P;
DE Short=GlcAT-P {ECO:0000303|PubMed:19181664};
DE AltName: Full=UDP-GlcUA:glycoprotein beta-1,3-glucuronyltransferase;
DE Short=GlcUAT-P;
GN Name=B3gat1 {ECO:0000312|RGD:70880};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 62-95;
RP 185-209; 214-231; 238-262; 269-274; 280-289 AND 307-333.
RC TISSUE=Brain;
RX PubMed=9177175; DOI=10.1073/pnas.94.12.6093;
RA Terayama K., Oka S., Seiki T., Miki Y., Nakamura A., Kozutsumi Y.,
RA Takio K., Kawasaki T.;
RT "Cloning and functional expression of a novel glucuronyltransferase
RT involved in the biosynthesis of the carbohydrate epitope HNK-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:6093-6098(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, CATALYTIC ACTIVITY, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2),
RP PROTEOLYTIC CLEAVAGE, MUTAGENESIS OF 3-LYS--ARG-5, REGION, AND INTERACTION
RP WITH SAR1A.
RX PubMed=19181664; DOI=10.1074/jbc.m807517200;
RA Kizuka Y., Tonoyama Y., Oka S.;
RT "Distinct transport and intracellular activities of two GlcAT-P isoforms.";
RL J. Biol. Chem. 284:9247-9256(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND CHARACTERIZATION.
RC TISSUE=Fetal brain;
RX PubMed=9804790; DOI=10.1074/jbc.273.46.30295;
RA Terayama K., Seiki T., Nakamura A., Matsumori K., Ohta S., Oka S.,
RA Sugita M., Kawasaki T.;
RT "Purification and characterization of a glucuronyltransferase involved in
RT the biosynthesis of the HNK-1 epitope on glycoproteins from rat brain.";
RL J. Biol. Chem. 273:30295-30300(1998).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-103 AND THR-108, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
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:0000269|PubMed:19181664, ECO:0000269|PubMed:9804790}.
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:0000269|PubMed:19181664,
CC ECO:0000269|PubMed:9804790};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:9804790};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Homodimer (PubMed:9804790). Interacts with SAR1A
CC (PubMed:19181664). {ECO:0000269|PubMed:19181664,
CC ECO:0000269|PubMed:9804790}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Golgi apparatus membrane
CC {ECO:0000269|PubMed:19181664}; Single-pass type II membrane protein.
CC Secreted {ECO:0000269|PubMed:19181664}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Golgi apparatus membrane
CC {ECO:0000269|PubMed:19181664}; Single-pass type II membrane protein.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:19181664}. Secreted
CC {ECO:0000269|PubMed:19181664}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=sGlcAT-P {ECO:0000303|PubMed:19181664};
CC IsoId=O35789-1; Sequence=Displayed;
CC Name=2; Synonyms=lGlcAT-P {ECO:0000303|PubMed:19181664};
CC IsoId=O35789-2; Sequence=VSP_058540;
CC -!- TISSUE SPECIFICITY: Brain. Greater expression found in the cerebral
CC cortex than the cerebellum.
CC -!- PTM: The soluble form derives from the membrane form by proteolytic
CC processing. {ECO:0000269|PubMed:19181664}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 43 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20551.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D88035; BAA20551.1; ALT_INIT; mRNA.
DR EMBL; AABR07069533; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474007; EDL83354.1; -; Genomic_DNA.
DR EMBL; CH474007; EDL83353.1; -; Genomic_DNA.
DR EMBL; CH474007; EDL83351.1; -; Genomic_DNA.
DR RefSeq; NP_446455.1; NM_054003.1. [O35789-2]
DR RefSeq; XP_006242795.1; XM_006242733.3. [O35789-2]
DR RefSeq; XP_006242796.1; XM_006242734.3. [O35789-1]
DR AlphaFoldDB; O35789; -.
DR SMR; O35789; -.
DR STRING; 10116.ENSRNOP00000009825; -.
DR CAZy; GT43; Glycosyltransferase Family 43.
DR GlyGen; O35789; 3 sites.
DR iPTMnet; O35789; -.
DR PhosphoSitePlus; O35789; -.
DR PaxDb; O35789; -.
DR Ensembl; ENSRNOT00000009825; ENSRNOP00000009825; ENSRNOG00000007142. [O35789-2]
DR GeneID; 117108; -.
DR KEGG; rno:117108; -.
DR UCSC; RGD:70880; rat. [O35789-1]
DR CTD; 27087; -.
DR RGD; 70880; B3gat1.
DR VEuPathDB; HostDB:ENSRNOG00000007142; -.
DR eggNOG; KOG1476; Eukaryota.
DR GeneTree; ENSGT00940000157165; -.
DR HOGENOM; CLU_045177_1_0_1; -.
DR InParanoid; O35789; -.
DR OMA; DSREYCM; -.
DR OrthoDB; 901158at2759; -.
DR TreeFam; TF313522; -.
DR Reactome; R-RNO-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR UniPathway; UPA00378; -.
DR PRO; PR:O35789; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Proteomes; UP000234681; Chromosome 8.
DR Bgee; ENSRNOG00000007142; Expressed in frontal cortex and 5 other tissues.
DR Genevisible; O35789; RN.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005796; C:Golgi lumen; TAS:RGD.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015018; F:galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity; IDA: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; ISO:RGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
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 Alternative splicing; Direct protein sequencing; Endoplasmic reticulum;
KW Glycoprotein; Golgi apparatus; Manganese; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Secreted; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..334
FT /note="Galactosylgalactosylxylosylprotein 3-beta-
FT glucuronosyltransferase 1"
FT /id="PRO_0000195170"
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:0000269|PubMed:19181664"
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:0007744|PubMed:16641100"
FT MOD_RES 108
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16641100"
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 -> MGNEELWAQPALEM (in isoform 2)"
FT /id="VSP_058540"
FT MUTAGEN 3..5
FT /note="KRR->AAA: Significantly disrupts Golgi apparatus
FT localization. Decreases galactosylgalactosylxylosylprotein
FT 3-beta-glucuronosyltransferase activity. Impairs secretion
FT and interaction with SAR1A."
FT /evidence="ECO:0000269|PubMed:19181664"
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
