Q9P2W7 (B3GA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	B3GAT1
Synonyms:	GLCATP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	334 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Catalytic activity	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.
Cofactor	Manganese.
Pathway	Protein modification; protein glycosylation.
Subunit structure	Homodimer Potential.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein.
Tissue specificity	Mainly expressed in the brain.
Sequence similarities	Belongs to the glycosyltransferase 43 family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Manganese Metal-binding
Molecular function	Transferase
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Traceable author statement. Source: Reactome chondroitin sulfate metabolic process Traceable author statement. Source: Reactome protein glycosylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome integral to membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity Inferred from electronic annotation. Source: Compara galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 334

334

Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1

PRO_0000195167

Regions

Topological domain

1 – 6

6

Cytoplasmic Potential

Transmembrane

7 – 27

21

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

28 – 334

307

Lumenal Potential

Nucleotide binding

91 – 93

3

UDP-glucuronate binding

Nucleotide binding

195 – 197

3

UDP-glucuronate binding

Nucleotide binding

311 – 313

3

UDP-glucuronate binding

Region

245 – 254

10

Interaction with galactose moiety of substrate glycoprotein

Sites

Active site

284

1

Proton donor/acceptor

Metal binding

197

1

Manganese By similarity

Binding site

122

1

UDP-glucuronate

Binding site

165

1

UDP-glucuronate

Binding site

170

1

UDP-glucuronate By similarity

Site

228

1

Interaction with galactose moiety of substrate glycoprotein

Site

321

1

Interaction with galactose moiety of substrate glycoprotein By similarity

Amino acid modifications

Glycosylation

140

1

N-linked (GlcNAc...) Potential

Glycosylation

184

1

N-linked (GlcNAc...) Potential

Glycosylation

303

1

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

131

1

A → T.
Corresponds to variant rs35434644 [ dbSNP | Ensembl ].

VAR_044538

Experimental info

Sequence conflict

240

1

G → R in BAA96077. Ref.1

Secondary structure

1

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334

Helix Strand Turn

Details...

Beta strand

85 – 92

8

Helix

98 – 109

12

Beta strand

112 – 125

14

Helix

128 – 137

10

Beta strand

140 – 145

6

Helix

150 – 153

4

Helix

167 – 180

14

Beta strand

183 – 185

3

Beta strand

189 – 193

5

Beta strand

198 – 200

3

Helix

202 – 209

8

Beta strand

212 – 216

5

Beta strand

219 – 221

3

Beta strand

225 – 232

8

Beta strand

238 – 242

5

Beta strand

244 – 246

3

Helix

255 – 257

3

Beta strand

258 – 261

4

Helix

262 – 267

6

Beta strand

275 – 278

4

Helix

283 – 291

9

Helix

294 – 296

3

Beta strand

297 – 299

3

Helix

301 – 304

4

Helix

320 – 322

3

Turn

323 – 325

3

Sequences

	Sequence		Length	Mass (Da)
	Q9P2W7 [UniParc]. Last modified July 22, 2008. Version 2. Checksum: 0DF42399D19701B3	FASTA	334	38,256
	10 20 30 40 50 60 MPKRRDILAI VLIVLPWTLL ITVWHQSTLA PLLAVHKDEG SDPRRETPPG ADPREYCTSD 70 80 90 100 110 120 RDIVEVVRTE YVYTRPPPWS DTLPTIHVVT PTYSRPVQKA ELTRMANTLL HVPNLHWLVV 130 140 150 160 170 180 EDAPRRTPLT ARLLRDTGLN YTHLHVETPR NYKLRGDARD PRIPRGTMQR NLALRWLRET 190 200 210 220 230 240 FPRNSSQPGV VYFADDDNTY SLELFEEMRS TRRVSVWPVA FVGGLRYEAP RVNGAGKVVG 250 260 270 280 290 300 WKTVFDPHRP FAIDMAGFAV NLRLILQRSQ AYFKLRGVKG GYQESSLLRE LVTLNDLEPK 310 320 330 AANCTKILVW HTRTEKPVLV NEGKKGFTDP SVEI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and chromosomal mapping of human glucuronyltransferase involved in biosynthesis of the HNK-1 carbohydrate epitope." Mitsumoto Y., Oka S., Sakuma H., Inazawa J., Kawasaki T. Genomics 65:166-173(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"Structural basis for acceptor substrate recognition of a human glucuronyltransferase, GlcAT-P, an enzyme critical in the biosynthesis of the carbohydrate epitope HNK-1." Kakuda S., Shiba T., Ishiguro M., Tagawa H., Oka S., Kajihara Y., Kawasaki T., Wakatsuki S., Kato R. J. Biol. Chem. 279:22693-22703(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 83-334 IN COMPLEX WITH UDP-GLUCURONIC ACID AND GALACTOSE MOIETY OF SUBSTRATE GLYCOPROTEIN.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB029396 mRNA. Translation: BAA96077.1.
CR457098 mRNA. Translation: CAG33379.1.
BC010466 mRNA. Translation: AAH10466.1.

IPI

IPI01013111.

RefSeq

NP_061114.2. NM_018644.3.
NP_473366.1. NM_054025.2.

UniGene

Hs.381050.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1V82	X-ray	1.85	A/B	83-334	[»]
1V83	X-ray	1.90	A/B	83-334	[»]
1V84	X-ray	1.82	A/B	83-334	[»]

ProteinModelPortal

Q9P2W7.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9P2W7. 2 interactions.

STRING

9606.ENSP00000307875.

Protein family/group databases

CAZy

GT43. Glycosyltransferase Family 43.

PTM databases

PhosphoSite

Q9P2W7.

Polymorphism databases

DMDM

205830910.

Proteomic databases

PaxDb

Q9P2W7.

PRIDE

Q9P2W7.

Protocols and materials databases

DNASU

27087.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000312527; ENSP00000307875; ENSG00000109956.
ENST00000392580; ENSP00000376359; ENSG00000109956.
ENST00000524765; ENSP00000433847; ENSG00000109956.

GeneID

27087.

KEGG

hsa:27087.

UCSC

uc001qhq.3. human.

Organism-specific databases

CTD

27087.

GeneCards

GC11M134281.

H-InvDB

HIX0010301.

HGNC

HGNC:921. B3GAT1.

HPA

CAB002500.
CAB010893.

MIM

151290. gene.

neXtProt

NX_Q9P2W7.

PharmGKB

PA25215.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG310844.

HOVERGEN

HBG050650.

InParanoid

Q9P2W7.

KO

K00735.

OrthoDB

EOG4XPQG4.

PhylomeDB

Q9P2W7.

Enzyme and pathway databases

BioCyc

MetaCyc:HS03272-MONOMER.

BRENDA

2.4.1.135. 2681.

Reactome

REACT_111217. Metabolism.
REACT_116125. Disease.

UniPathway

UPA00378.

Gene expression databases

ArrayExpress

Q9P2W7.

Bgee

Q9P2W7.

CleanEx

HS_B3GAT1.

Genevestigator

Q9P2W7.

GermOnline

ENSG00000109956. Homo sapiens.

Family and domain databases

InterPro

IPR005027. Glyco_trans_43.
[Graphical view]

PANTHER

PTHR10896. PTHR10896. 1 hit.

Pfam

PF03360. Glyco_transf_43. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL4067.

EvolutionaryTrace

Q9P2W7.

GenomeRNAi

27087.

NextBio

49699.

SOURCE

Search...

Entry information

Entry name

B3GA1_HUMAN

Accession

Primary (citable) accession number: Q9P2W7
Secondary accession number(s): Q96FS7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	July 22, 2008
Last modified:	May 1, 2013
This is version 127 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.