Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A0A4Z3

- A3LT2_RAT

UniProt

A0A4Z3 - A3LT2_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Alpha-1,3-galactosyltransferase 2

Gene

A3galt2

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

Functioni

Synthesizes the galactose-alpha(1,3)-galactose group on the glycosphingolipid isoglobotrihexosylceramide or isogloboside 3 (iGb3) by catalyzing the transfer of galactose from UDP-Galactose to its acceptor molecule Gal-beta-1,4-Glc-ceramide. Can also catalyze the addition of galactose to iGb3 itself to form polygalactose structures. Synthesis of iGb3 is the initial step in the formation of the isoglobo-series glycolipid pathway and is the precursor to isogloboside 4 (iGb4) and isoForssman glycolipids. Can glycosylate only lipids and not proteins and is solely responsible for initiating the synthesis of isoglobo-series glycosphingolipids.3 Publications

Catalytic activityi

UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R = UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R.

Cofactori

Mn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi198 – 1981ManganeseBy similarity
Metal bindingi200 – 2001ManganeseBy similarity

GO - Molecular functioni

  1. alpha-1,3-galactosyltransferase activity Source: Ensembl
  2. metal ion binding Source: UniProtKB-KW
  3. N-acetyllactosaminide 3-alpha-galactosyltransferase activity Source: UniProtKB-EC
  4. transferase activity, transferring glycosyl groups Source: RGD

GO - Biological processi

  1. glycosphingolipid biosynthetic process Source: UniProtKB
  2. lipid glycosylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Protein family/group databases

CAZyiGT6. Glycosyltransferase Family 6.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-1,3-galactosyltransferase 2 (EC:2.4.1.87)
Short name:
A3galt2
Alternative name(s):
Isoglobotriaosylceramide synthase
Short name:
iGb3 synthase
Short name:
iGb3S
Gene namesi
Name:A3galt2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 5

Organism-specific databases

RGDi727913. A3galt2.

Subcellular locationi

Golgi apparatusGolgi stack membrane 2 Publications; Single-pass type II membrane protein 2 Publications
Note: Also found in numerous large vesicles throughout the cytoplasm of the soma.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei12 – 3120Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini32 – 339308LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB
  2. integral component of membrane Source: UniProtKB-KW
  3. vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi187 – 1871L → P: Significant loss of activity. 1 Publication
Mutagenesisi198 – 2003DVD → AVA: Catalytically inactive. 1 Publication
Mutagenesisi252 – 2521Y → N: Complete loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 339339Alpha-1,3-galactosyltransferase 2PRO_0000314872Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi57 – 571N-linked (GlcNAc...)Sequence Analysis
Glycosylationi99 – 991N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiA0A4Z3.
PRIDEiA0A4Z3.

Expressioni

Tissue specificityi

Dorsal root ganglia neurons (at protein level). High levels in spleen, thymus and skeletal muscle, intermediate levels in lung, uterus, pituitary and heart, low levels in brain, and undetected in adrenal gland and liver.3 Publications

Gene expression databases

GenevestigatoriA0A4Z3.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000007851.

Structurei

3D structure databases

ProteinModelPortaliA0A4Z3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The conserved DXD motif is involved in cofactor binding. The manganese ion interacts with the beta-phosphate group of UDP and may also have a role in catalysis.

Sequence similaritiesi

Belongs to the glycosyltransferase 6 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG277430.
GeneTreeiENSGT00400000022032.
HOGENOMiHOG000234339.
HOVERGENiHBG003563.
InParanoidiA0A4Z3.
OMAiVFTERPA.
OrthoDBiEOG7QG44N.
PhylomeDBiA0A4Z3.
TreeFamiTF330991.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR005076. Glyco_trans_6.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR10462. PTHR10462. 1 hit.
PfamiPF03414. Glyco_transf_6. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

A0A4Z3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALEGLRAKK RLLWRLFLSA FGLLGLYHYW FKIFRLFEVF IPMGICPMAI
60 70 80 90 100
MPLLKDNFTG VLRHWARPEV LTCTSWGAPI IWDETFDPHV AEREARRQNL
110 120 130 140 150
TIGLTVFAVG RYLEKYLEHF LVSAEQYFMV GQNVVYYVFT DRPEAVPHVA
160 170 180 190 200
LGQGRLLRVK PVRREKRWQD VSMARMLTLH EALGGQLGRE ADYVFCLDVD
210 220 230 240 250
QYFSGNFGPE VLADLVAQLH AWHFRWPRWM LPYERDKRSA AALSLSEGDF
260 270 280 290 300
YYHAAVFGGS VAALLKLTAH CATGQQLDRE HGIEARWHDE SHLNKFFWLS
310 320 330
KPTKLLSPEF CWAEEIGWRP EIHHPRLIWA PKEYALVRT
Length:339
Mass (Da):39,548
Last modified:November 28, 2006 - v1
Checksum:i171A191001F0C6CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF248543 mRNA. Translation: AAF82757.1.
BC061714 mRNA. Translation: AAH61714.1.
RefSeqiNP_612533.1. NM_138524.2.
UniGeneiRn.37737.

Genome annotation databases

EnsembliENSRNOT00000007851; ENSRNOP00000007851; ENSRNOG00000005935.
GeneIDi171553.
KEGGirno:171553.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF248543 mRNA. Translation: AAF82757.1 .
BC061714 mRNA. Translation: AAH61714.1 .
RefSeqi NP_612533.1. NM_138524.2.
UniGenei Rn.37737.

3D structure databases

ProteinModelPortali A0A4Z3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000007851.

Protein family/group databases

CAZyi GT6. Glycosyltransferase Family 6.

Proteomic databases

PaxDbi A0A4Z3.
PRIDEi A0A4Z3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000007851 ; ENSRNOP00000007851 ; ENSRNOG00000005935 .
GeneIDi 171553.
KEGGi rno:171553.

Organism-specific databases

CTDi 127550.
RGDi 727913. A3galt2.

Phylogenomic databases

eggNOGi NOG277430.
GeneTreei ENSGT00400000022032.
HOGENOMi HOG000234339.
HOVERGENi HBG003563.
InParanoidi A0A4Z3.
OMAi VFTERPA.
OrthoDBi EOG7QG44N.
PhylomeDBi A0A4Z3.
TreeFami TF330991.

Miscellaneous databases

NextBioi 622541.

Gene expression databases

Genevestigatori A0A4Z3.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR005076. Glyco_trans_6.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view ]
PANTHERi PTHR10462. PTHR10462. 1 hit.
Pfami PF03414. Glyco_transf_6. 1 hit.
[Graphical view ]
SUPFAMi SSF53448. SSF53448. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Expression cloning of a new member of the ABO blood group glycosyltransferases, iGb3 synthase, that directs the synthesis of isoglobo-glycosphingolipids."
    Keusch J.J., Manzella S.M., Nyame K.A., Cummings R.D., Baenziger J.U.
    J. Biol. Chem. 275:25308-25314(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF 198-ASP--ASP-200.
    Strain: Sprague-Dawley.
    Tissue: Placenta.
  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: Prostate.
  3. "Characterization of the rat alpha(1,3)galactosyltransferase: evidence for two independent genes encoding glycosyltransferases that synthesize Galalpha(1,3)Gal by two separate glycosylation pathways."
    Taylor S.G., McKenzie I.F., Sandrin M.S.
    Glycobiology 13:327-337(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  4. "Enzymes that synthesize the IB4 epitope are not sufficient to impart IB4 binding in dorsal root ganglia of rat."
    Fullmer J.M., Riedl M., Williams F.G., Sandrin M., Elde R.
    J. Comp. Neurol. 501:70-82(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  5. "Humans lack iGb3 due to the absence of functional iGb3-synthase: implications for NKT cell development and transplantation."
    Christiansen D., Milland J., Mouhtouris E., Vaughan H., Pellicci D.G., McConville M.J., Godfrey D.I., Sandrin M.S.
    PLoS Biol. 6:E172-E172(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-187 AND TYR-252.

Entry informationi

Entry nameiA3LT2_RAT
AccessioniPrimary (citable) accession number: A0A4Z3
Secondary accession number(s): A2JQW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 28, 2006
Last modified: November 26, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

This gene is not expressed in humans, and even if it were to be expressed, this enzyme appears to be inactive because of multiple mutations including an amino-acid substitution Leu-187 to Pro and Tyr-252 to Asn.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3