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A0A4Z3

- A3LT2_RAT

UniProt

A0A4Z3 - A3LT2_RAT

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
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (28 Nov 2006)
      Previous versions | rss
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    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

    Manganese.By similarity

    Sites

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. glycosphingolipid biosynthetic process Source: UniProtKB
    2. lipid glycosylation Source: UniProtKB

    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.

    GO - Cellular componenti

    1. Golgi apparatus Source: UniProtKB
    2. Golgi cisterna membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW
    4. vesicle Source: UniProtKB

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi187 – 1871L → P: Significant loss of activity. 2 Publications
    Mutagenesisi198 – 2003DVD → AVA: Catalytically inactive. 1 Publication
    Mutagenesisi252 – 2521Y → N: Complete loss of activity. 2 Publications

    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...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1111CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini32 – 339308LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei12 – 3120Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    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

    MALEGLRAKK RLLWRLFLSA FGLLGLYHYW FKIFRLFEVF IPMGICPMAI    50
    MPLLKDNFTG VLRHWARPEV LTCTSWGAPI IWDETFDPHV AEREARRQNL 100
    TIGLTVFAVG RYLEKYLEHF LVSAEQYFMV GQNVVYYVFT DRPEAVPHVA 150
    LGQGRLLRVK PVRREKRWQD VSMARMLTLH EALGGQLGRE ADYVFCLDVD 200
    QYFSGNFGPE VLADLVAQLH AWHFRWPRWM LPYERDKRSA AALSLSEGDF 250
    YYHAAVFGGS VAALLKLTAH CATGQQLDRE HGIEARWHDE SHLNKFFWLS 300
    KPTKLLSPEF CWAEEIGWRP EIHHPRLIWA PKEYALVRT 339
    Length:339
    Mass (Da):39,548
    Last modified:November 28, 2006 - v1
    Checksum:i171A191001F0C6CF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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

    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: October 1, 2014
    This is version 57 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