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Protein

Lactosylceramide 4-alpha-galactosyltransferase

Gene

A4galt

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Necessary for the biosynthesis of the Pk antigen of blood histogroup P. Catalyzes the transfer of galactose to lactosylceramide and galactosylceramide. Necessary for the synthesis of the receptor for bacterial verotoxins.By similarity1 Publication

Catalytic activityi

UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-D-glucosyl-(1<->1)-ceramide = UDP + alpha-D-galactosyl-(1->4)-beta-D-galactosyl-(1->4)-D-glucosyl-(1<->1)-ceramide.1 Publication

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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT32. Glycosyltransferase Family 32.

Chemistry

SwissLipidsiSLP:000000761.
SLP:000000762.

Names & Taxonomyi

Protein namesi
Recommended name:
Lactosylceramide 4-alpha-galactosyltransferase (EC:2.4.1.228)
Alternative name(s):
Alpha-1,4-N-acetylglucosaminyltransferase
Alpha-1,4-galactosyltransferase
Alpha4Gal-T1
Globotriaosylceramide synthase
Short name:
Gb3 synthase
UDP-galactose:beta-D-galactosyl-beta1-R 4-alpha-D-galactosyltransferase
Gene namesi
Name:A4galtImported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi621583. A4galt.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3030CytoplasmicSequence analysisAdd
BLAST
Transmembranei31 – 5121Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini52 – 360309LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi199 – 2013DTD → ATA: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 360360Lactosylceramide 4-alpha-galactosyltransferasePRO_0000080582Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi210 – 2101N-linked (GlcNAc...)Sequence analysis
Glycosylationi316 – 3161N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9JI93.
PRIDEiQ9JI93.

PTM databases

PhosphoSiteiQ9JI93.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in kidney, mesenteric lymph node, spleen and brain.1 Publication

Gene expression databases

GenevisibleiQ9JI93. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000064362.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi199 – 2013DXD motif

Domaini

The conserved DXD motif is involved in enzyme activity.1 Publication

Sequence similaritiesi

Belongs to the glycosyltransferase 32 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1928. Eukaryota.
ENOG4111PD8. LUCA.
GeneTreeiENSGT00510000047981.
HOVERGENiHBG050427.
InParanoidiQ9JI93.
KOiK01988.
OMAiFVAHYNG.
OrthoDBiEOG75MVW8.
PhylomeDBiQ9JI93.

Family and domain databases

InterProiIPR007652. A1-4-GlycosylTfrase_dom.
IPR007577. GlycoTrfase_DXD_sugar-bd_CS.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF04572. Gb3_synth. 1 hit.
PF04488. Gly_transf_sug. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9JI93-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGISRSDLEE TMSKPPDCLP RMLRGTPRQR VFTLFIISFK FTFLVSILIY
60 70 80 90 100
WHTVGAPKDQ RRQYSLPVDF PCPQLAFPRV SAPGNIFFLE TSDRTNPSFL
110 120 130 140 150
FMCSVESAAR AHPESQVVVL MKGLPRDTTA WPRNLGISLL SCFPNVQIRP
160 170 180 190 200
LDLQELFEDT PLAAWYLEAQ HRWEPYLLPV LSDASRIALL WKFGGIYLDT
210 220 230 240 250
DFIVLKNLRN LTNMLGIQSR YVLNGAFLAF ERKHEFLALC IRDFVAHYNG
260 270 280 290 300
WIWGHQGPQL LTRVFKKWCS IHSLKESRAC RGVTALPPEA FYPIPWQNWK
310 320 330 340 350
KYFEDVSPEE LAQLLNATYA VHVWNKKSQG THLEATSRAL LAQLHARYCP
360
TTHRAMTMYL
Length:360
Mass (Da):41,551
Last modified:October 1, 2000 - v1
Checksum:i0A4181886DB49D6A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF248544 mRNA. Translation: AAF82758.1.
BC097323 mRNA. Translation: AAH97323.1.
RefSeqiNP_071576.1. NM_022240.2.
XP_006242179.1. XM_006242117.2.
XP_006242180.1. XM_006242118.2.
XP_006242182.1. XM_006242120.1.
UniGeneiRn.48584.

Genome annotation databases

EnsembliENSRNOT00000012914; ENSRNOP00000064362; ENSRNOG00000009736.
GeneIDi63888.
KEGGirno:63888.
UCSCiRGD:621583. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF248544 mRNA. Translation: AAF82758.1.
BC097323 mRNA. Translation: AAH97323.1.
RefSeqiNP_071576.1. NM_022240.2.
XP_006242179.1. XM_006242117.2.
XP_006242180.1. XM_006242118.2.
XP_006242182.1. XM_006242120.1.
UniGeneiRn.48584.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000064362.

Chemistry

SwissLipidsiSLP:000000761.
SLP:000000762.

Protein family/group databases

CAZyiGT32. Glycosyltransferase Family 32.

PTM databases

PhosphoSiteiQ9JI93.

Proteomic databases

PaxDbiQ9JI93.
PRIDEiQ9JI93.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000012914; ENSRNOP00000064362; ENSRNOG00000009736.
GeneIDi63888.
KEGGirno:63888.
UCSCiRGD:621583. rat.

Organism-specific databases

CTDi53947.
RGDi621583. A4galt.

Phylogenomic databases

eggNOGiKOG1928. Eukaryota.
ENOG4111PD8. LUCA.
GeneTreeiENSGT00510000047981.
HOVERGENiHBG050427.
InParanoidiQ9JI93.
KOiK01988.
OMAiFVAHYNG.
OrthoDBiEOG75MVW8.
PhylomeDBiQ9JI93.

Enzyme and pathway databases

UniPathwayiUPA00378.

Miscellaneous databases

PROiQ9JI93.

Gene expression databases

GenevisibleiQ9JI93. RN.

Family and domain databases

InterProiIPR007652. A1-4-GlycosylTfrase_dom.
IPR007577. GlycoTrfase_DXD_sugar-bd_CS.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF04572. Gb3_synth. 1 hit.
PF04488. Gly_transf_sug. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of Gb3 synthase, the key enzyme in globo-series glycosphingolipid synthesis, predicts a family of alpha1,4-glycosyltransferases conserved in plants, insects and mammals."
    Keusch J.J., Manzella S.M., Nyame K.A., Cummings R.D., Baenziger J.U.
    J. Biol. Chem. 275:25315-25321(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, MUTAGENESIS OF 199-ASP--ASP-201.
    Strain: Sprague-DawleyImported.
    Tissue: PlacentaImported.
  2. "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: Placenta.

Entry informationi

Entry nameiA4GAT_RAT
AccessioniPrimary (citable) accession number: Q9JI93
Secondary accession number(s): Q4QR98
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 81 of the entry and version 1 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.