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Protein

Glutamate decarboxylase 2

Gene

Gad2

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

Functioni

Catalyzes the production of GABA.

Catalytic activityi

L-glutamate = 4-aminobutanoate + CO2.

Cofactori

Kineticsi

  1. KM=1.02 mM for glutamate1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei558 – 5581SubstrateBy similarity

    GO - Molecular functioni

    • glutamate binding Source: RGD
    • glutamate decarboxylase activity Source: RGD
    • protein heterodimerization activity Source: RGD
    • pyridoxal phosphate binding Source: RGD

    GO - Biological processi

    • glutamate decarboxylation to succinate Source: RGD
    • neurotransmitter biosynthetic process Source: UniProtKB-KW
    • response to drug Source: RGD
    • synaptic transmission Source: RGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Biological processi

    Neurotransmitter biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    ReactomeiREACT_289838. GABA synthesis, release, reuptake and degradation.
    REACT_303944. GABA synthesis.
    SABIO-RKQ05683.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate decarboxylase 2 (EC:4.1.1.15)
    Alternative name(s):
    65 kDa glutamic acid decarboxylase
    Short name:
    GAD-65
    Glutamate decarboxylase 65 kDa isoform
    Gene namesi
    Name:Gad2
    Synonyms:Gad65
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494 Componenti: Chromosome 17

    Organism-specific databases

    RGDi2653. Gad2.

    Subcellular locationi

    GO - Cellular componenti

    • anchored component of membrane Source: RGD
    • axon Source: Ensembl
    • cell junction Source: UniProtKB-KW
    • cytoplasmic vesicle Source: RGD
    • cytosol Source: RGD
    • Golgi membrane Source: UniProtKB-SubCell
    • inhibitory synapse Source: MGI
    • perinuclear region of cytoplasm Source: RGD
    • presynaptic membrane Source: UniProtKB-SubCell
    • synaptic vesicle membrane Source: RGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane, Synapse

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi30 – 301C → A: Abolishes palmitoylation but not membrane-association; when associates with A-45. 1 Publication
    Mutagenesisi45 – 451C → A: Abolishes palmitoylation but not membrane-association; when associates with A-30. 1 Publication
    Mutagenesisi73 – 731C → S: No effect on palmitoylation. 1 Publication
    Mutagenesisi75 – 751C → S: No effect on palmitoylation. 1 Publication
    Mutagenesisi80 – 801C → S: No effect on palmitoylation. 1 Publication
    Mutagenesisi82 – 821C → S: No effect on palmitoylation. 1 Publication
    Mutagenesisi101 – 1011C → S: No effect on palmitoylation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 585585Glutamate decarboxylase 2PRO_0000146971Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31Phosphoserine1 Publication
    Modified residuei6 – 61Phosphoserine1 Publication
    Modified residuei10 – 101Phosphoserine1 Publication
    Modified residuei13 – 131Phosphoserine1 Publication
    Lipidationi30 – 301S-palmitoyl cysteine1 Publication
    Lipidationi45 – 451S-palmitoyl cysteine1 Publication
    Modified residuei396 – 3961N6-(pyridoxal phosphate)lysineBy similarity

    Post-translational modificationi

    The N-terminus is blocked.
    Phosphorylated; which does not affect kinetic parameters or subcellular location.1 Publication
    Palmitoylated; which is required for presynaptic clustering.By similarity

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    PRIDEiQ05683.

    PTM databases

    PhosphoSiteiQ05683.

    Expressioni

    Gene expression databases

    ExpressionAtlasiQ05683. baseline.
    GenevisibleiQ05683. RN.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi246551. 1 interaction.
    IntActiQ05683. 1 interaction.
    STRINGi10116.ENSRNOP00000024901.

    Structurei

    3D structure databases

    ProteinModelPortaliQ05683.
    SMRiQ05683. Positions 88-584.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni181 – 1833Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the group II decarboxylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0076.
    GeneTreeiENSGT00760000119205.
    HOGENOMiHOG000005382.
    HOVERGENiHBG004980.
    InParanoidiQ05683.
    KOiK01580.
    OMAiWRAKGTT.
    OrthoDBiEOG7H1JM3.
    PhylomeDBiQ05683.
    TreeFamiTF314688.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR002129. PyrdxlP-dep_de-COase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    IPR021115. Pyridoxal-P_BS.
    [Graphical view]
    PfamiPF00282. Pyridoxal_deC. 1 hit.
    [Graphical view]
    SUPFAMiSSF53383. SSF53383. 1 hit.
    PROSITEiPS00392. DDC_GAD_HDC_YDC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q05683-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MASPGSGFWS FGSEDGSGDP ENPGTARAWC QVAQKFTGGI GNKLCALLYG
    60 70 80 90 100
    DSEKPAESGG SVTSRAATRK VACTCDQKPC SCPKGDVNYA LLHATDLLPA
    110 120 130 140 150
    CEGERPTLAF LQDVMNILLQ YVVKSFDRST KVIDFHYPNE LLQEYNWELA
    160 170 180 190 200
    DQPQNLEEIL THCQTTLKYA IKTGHPRYFN QLSTGLDMVG LAADWLTSTA
    210 220 230 240 250
    NTNMFTYEIA PVFVLLEYVT LKKMREIIGW PGGSGDGIFS PGGAISNMYA
    260 270 280 290 300
    MLIARYKMFP EVKEKGMAAV PRLIAFTSEH SHFSLKKGAA ALGIGTDSVI
    310 320 330 340 350
    LIKCDERGKM IPSDLERRIL EVKQKGFVPF LVSATAGTTV YGAFDPLLAV
    360 370 380 390 400
    ADICKKYKIW MHVDAAWGGG LLMSRKHKWK LNGVERANSV TWNPHKMMGV
    410 420 430 440 450
    PLQCSALLVR EEGLMQSCNQ MHASYLFQQD KHYDLSYDTG DKALQCGRHV
    460 470 480 490 500
    DVFKLWLMWR AKGTTGFEAH IDKCLELAEY LYNIIKNREG YEMVFDGKPQ
    510 520 530 540 550
    HTNVCFWFVP PSLRVLEDNE ERMSRLSKVA PVIKARMMEY GTTMVSYQPL
    560 570 580
    GDKVNFFRMV ISNPAATHQD IDFLIEEIER LGQDL
    Length:585
    Mass (Da):65,402
    Last modified:February 1, 1996 - v1
    Checksum:iC04040B7BA7B37D1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti190 – 1901G → V AA sequence (PubMed:3385490).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M72422 mRNA. Translation: AAA63488.1.
    PIRiJH0423.
    RefSeqiNP_036695.1. NM_012563.1.
    UniGeneiRn.29951.

    Genome annotation databases

    EnsembliENSRNOT00000024901; ENSRNOP00000024901; ENSRNOG00000018200.
    GeneIDi24380.
    KEGGirno:24380.
    UCSCiRGD:2653. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M72422 mRNA. Translation: AAA63488.1.
    PIRiJH0423.
    RefSeqiNP_036695.1. NM_012563.1.
    UniGeneiRn.29951.

    3D structure databases

    ProteinModelPortaliQ05683.
    SMRiQ05683. Positions 88-584.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi246551. 1 interaction.
    IntActiQ05683. 1 interaction.
    STRINGi10116.ENSRNOP00000024901.

    Chemistry

    BindingDBiQ05683.

    PTM databases

    PhosphoSiteiQ05683.

    Proteomic databases

    PRIDEiQ05683.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSRNOT00000024901; ENSRNOP00000024901; ENSRNOG00000018200.
    GeneIDi24380.
    KEGGirno:24380.
    UCSCiRGD:2653. rat.

    Organism-specific databases

    CTDi2572.
    RGDi2653. Gad2.

    Phylogenomic databases

    eggNOGiCOG0076.
    GeneTreeiENSGT00760000119205.
    HOGENOMiHOG000005382.
    HOVERGENiHBG004980.
    InParanoidiQ05683.
    KOiK01580.
    OMAiWRAKGTT.
    OrthoDBiEOG7H1JM3.
    PhylomeDBiQ05683.
    TreeFamiTF314688.

    Enzyme and pathway databases

    ReactomeiREACT_289838. GABA synthesis, release, reuptake and degradation.
    REACT_303944. GABA synthesis.
    SABIO-RKQ05683.

    Miscellaneous databases

    NextBioi603141.
    PROiQ05683.

    Gene expression databases

    ExpressionAtlasiQ05683. baseline.
    GenevisibleiQ05683. RN.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR002129. PyrdxlP-dep_de-COase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    IPR021115. Pyridoxal-P_BS.
    [Graphical view]
    PfamiPF00282. Pyridoxal_deC. 1 hit.
    [Graphical view]
    SUPFAMiSSF53383. SSF53383. 1 hit.
    PROSITEiPS00392. DDC_GAD_HDC_YDC. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Two genes encode distinct glutamate decarboxylases."
      Erlander M.G., Tillakaratne N.J., Feldblum S., Patel N., Tobin A.J.
      Neuron 7:91-100(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Hippocampus.
    2. "Characterization of the proteins purified with monoclonal antibodies to glutamic acid decarboxylase."
      Chang Y.C., Gottlieb D.I.
      J. Neurosci. 8:2123-2130(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 190-219; 225-266 AND 524-558.
      Tissue: Brain.
    3. "Membrane anchoring of the autoantigen GAD65 to microvesicles in pancreatic beta-cells by palmitoylation in the NH2-terminal domain."
      Christgau S., Aanstoot H.-J., Schierbeck H., Begley K., Tullin S., Hejnaes K., Baekkeskov S.
      J. Cell Biol. 118:309-320(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PALMITOYLATION.
    4. "Amino acid residues 24-31 but not palmitoylation of cysteines 30 and 45 are required for membrane anchoring of glutamic acid decarboxylase, GAD65."
      Shi Y., Veit B., Baekkeskov S.
      J. Cell Biol. 124:927-934(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-30 AND CYS-45, MUTAGENESIS OF CYS-30; CYS-45; CYS-73; CYS-75; CYS-80; CYS-82 AND CYS-101.
    5. "Phosphorylation of serine residues 3, 6, 10, and 13 distinguishes membrane anchored from soluble glutamic acid decarboxylase 65 and is restricted to glutamic acid decarboxylase 65alpha."
      Namchuk M., Lindsay L., Turck C.W., Kanaani J., Baekkeskov S.
      J. Biol. Chem. 272:1548-1557(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-3; SER-6; SER-10 AND SER-13, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiDCE2_RAT
    AccessioniPrimary (citable) accession number: Q05683
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: June 24, 2015
    This is version 112 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, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.