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Protein

Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1

Gene

B3gat1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on glycoproteins. Can also play a role in glycosaminoglycan biosynthesis. Substrates include asialo-orosomucoid (ASOR), asialo-fetuin, and asialo-neural cell adhesion molecule. Requires sphingomyelin for activity: stearoyl-sphingomyelin was the most effective, followed by palmitoyl-sphingomyelin and lignoceroyl-sphingomyelin. Activity was demonstrated only for sphingomyelin with a saturated fatty acid and not for that with an unsaturated fatty acid, regardless of the length of the acyl group (By similarity).By similarity

Catalytic activityi

UDP-glucuronate + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein = UDP + 3-beta-D-glucuronosyl-3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein.

Cofactori

Mn2+By similarity

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei122 – 1221UDP-glucuronateBy similarity
Binding sitei165 – 1651UDP-glucuronateBy similarity
Binding sitei170 – 1701UDP-glucuronateBy similarity
Metal bindingi197 – 1971ManganeseBy similarity
Active sitei284 – 2841Proton donor/acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi91 – 933UDP-glucuronate bindingBy similarity
Nucleotide bindingi195 – 1973UDP-glucuronate bindingBy similarity
Nucleotide bindingi311 – 3133UDP-glucuronate bindingBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT43. Glycosyltransferase Family 43.

Names & Taxonomyi

Protein namesi
Recommended name:
Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1 (EC:2.4.1.135)
Alternative name(s):
Beta-1,3-glucuronyltransferase 1
Glucuronosyltransferase P
Short name:
GlcAT-P
UDP-GlcUA:glycoprotein beta-1,3-glucuronyltransferase
Short name:
GlcUAT-P
Gene namesi
Name:B3gat1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1924148. B3gat1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence analysis
Transmembranei7 – 2721Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini28 – 334307LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 334334Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1PRO_0000195168Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei103 – 1031PhosphothreonineBy similarity
Modified residuei108 – 1081PhosphothreonineBy similarity
Glycosylationi140 – 1401N-linked (GlcNAc...)Sequence analysis
Glycosylationi184 – 1841N-linked (GlcNAc...)Sequence analysis
Glycosylationi303 – 3031N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ9CW73.
PRIDEiQ9CW73.

PTM databases

PhosphoSiteiQ9CW73.

Expressioni

Gene expression databases

BgeeiQ9CW73.

Interactioni

Subunit structurei

Homodimer.Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei228 – 2281Interaction with galactose moiety of substrate glycoproteinBy similarity
Sitei321 – 3211Interaction with galactose moiety of substrate glycoproteinBy similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000125700.

Structurei

3D structure databases

ProteinModelPortaliQ9CW73.
SMRiQ9CW73. Positions 83-334.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni245 – 25410Interaction with galactose moiety of substrate glycoproteinBy similarity

Sequence similaritiesi

Belongs to the glycosyltransferase 43 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1476. Eukaryota.
ENOG410XP79. LUCA.
HOGENOMiHOG000261693.
HOVERGENiHBG050650.
InParanoidiQ9CW73.
KOiK00735.
OrthoDBiEOG7QG44X.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR005027. Glyco_trans_43.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR10896. PTHR10896. 1 hit.
PfamiPF03360. Glyco_transf_43. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9CW73-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKRRDILAI VLIVLPWTLL ITVWHQSSLA PLLAVHKDEG SDPRHEAPPG
60 70 80 90 100
ADPREYCMSD RDIVEVVRTE YVYTRPPPWS DTLPTIHVVT PTYSRPVQKA
110 120 130 140 150
ELTRMANTLL HVPNLHWLVV GDAPRRTPLT ARLLRDTGLN YTHLHVETPR
160 170 180 190 200
NYKLRGDARD PRIPRGTMQR NLALRWLRET FPRNSTQPGV VYFADDDNTY
210 220 230 240 250
SLELFEEMRS TRRVSVWPVA FVGGLRYEAP RVNGAGKVVG WKTVFDPHRP
260 270 280 290 300
FAIDMAGFAV NLRLILQRSQ AYFKLRGVKG GYQESSLLRE LVTLNDLEPK
310 320 330
AANCTKILVW HTRTEKPVLV NEGKKGFTDP SVEI
Length:334
Mass (Da):38,165
Last modified:April 26, 2005 - v2
Checksum:i6BDAF9F6DA80A40C
GO

Sequence cautioni

The sequence BAC31996.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti121 – 1211G → E in BAB22514 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003020 mRNA. Translation: BAB22514.1.
AK044599 mRNA. Translation: BAC31996.1. Different initiation.
RefSeqiNP_001297695.1. NM_001310766.1.
UniGeneiMm.218788.

Genome annotation databases

GeneIDi76898.
KEGGimmu:76898.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003020 mRNA. Translation: BAB22514.1.
AK044599 mRNA. Translation: BAC31996.1. Different initiation.
RefSeqiNP_001297695.1. NM_001310766.1.
UniGeneiMm.218788.

3D structure databases

ProteinModelPortaliQ9CW73.
SMRiQ9CW73. Positions 83-334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000125700.

Protein family/group databases

CAZyiGT43. Glycosyltransferase Family 43.

PTM databases

PhosphoSiteiQ9CW73.

Proteomic databases

PaxDbiQ9CW73.
PRIDEiQ9CW73.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi76898.
KEGGimmu:76898.

Organism-specific databases

CTDi27087.
MGIiMGI:1924148. B3gat1.

Phylogenomic databases

eggNOGiKOG1476. Eukaryota.
ENOG410XP79. LUCA.
HOGENOMiHOG000261693.
HOVERGENiHBG050650.
InParanoidiQ9CW73.
KOiK00735.
OrthoDBiEOG7QG44X.

Enzyme and pathway databases

UniPathwayiUPA00378.

Miscellaneous databases

PROiQ9CW73.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CW73.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR005027. Glyco_trans_43.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR10896. PTHR10896. 1 hit.
PfamiPF03360. Glyco_transf_43. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain and Retina.

Entry informationi

Entry nameiB3GA1_MOUSE
AccessioniPrimary (citable) accession number: Q9CW73
Secondary accession number(s): Q8BXN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: April 26, 2005
Last modified: May 11, 2016
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.