Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

Q05683

- DCE2_RAT

UniProt

Q05683 - DCE2_RAT

Protein

Glutamate decarboxylase 2

Gene

Gad2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the production of GABA.

    Catalytic activityi

    L-glutamate = 4-aminobutanoate + CO2.

    Cofactori

    Pyridoxal phosphate.

    Kineticsi

    1. KM=1.02 mM for glutamate1 Publication

    Sites

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

    GO - Molecular functioni

    1. glutamate binding Source: RGD
    2. glutamate decarboxylase activity Source: RGD
    3. protein heterodimerization activity Source: RGD
    4. pyridoxal phosphate binding Source: RGD

    GO - Biological processi

    1. glutamate decarboxylation to succinate Source: RGD
    2. neurotransmitter biosynthetic process Source: UniProtKB-KW
    3. response to drug Source: RGD
    4. synaptic transmission Source: RGD

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Biological processi

    Neurotransmitter biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    ReactomeiREACT_196234. 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: Chromosome 17

    Organism-specific databases

    RGDi2653. Gad2.

    Subcellular locationi

    Cytoplasmcytosol By similarity. Cytoplasmic vesicle By similarity. Cell junctionsynapsepresynaptic cell membrane By similarity; Lipid-anchor By similarity. Golgi apparatus membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
    Note: Associated to cytoplasmic vesicles. In neurons, cytosolic leaflet of Golgi membranes and presynaptic clusters By similarity.By similarity

    GO - Cellular componenti

    1. anchored component of membrane Source: RGD
    2. axon Source: Ensembl
    3. cell junction Source: UniProtKB-KW
    4. cytoplasmic vesicle Source: RGD
    5. cytosol Source: RGD
    6. Golgi membrane Source: UniProtKB-SubCell
    7. perinuclear region of cytoplasm Source: RGD
    8. presynaptic membrane Source: UniProtKB-SubCell
    9. synaptic vesicle membrane Source: RGD

    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 cysteine2 Publications
    Lipidationi45 – 451S-palmitoyl cysteine2 Publications
    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

    GenevestigatoriQ05683.

    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.
    GeneTreeiENSGT00730000110441.
    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

    MASPGSGFWS FGSEDGSGDP ENPGTARAWC QVAQKFTGGI GNKLCALLYG    50
    DSEKPAESGG SVTSRAATRK VACTCDQKPC SCPKGDVNYA LLHATDLLPA 100
    CEGERPTLAF LQDVMNILLQ YVVKSFDRST KVIDFHYPNE LLQEYNWELA 150
    DQPQNLEEIL THCQTTLKYA IKTGHPRYFN QLSTGLDMVG LAADWLTSTA 200
    NTNMFTYEIA PVFVLLEYVT LKKMREIIGW PGGSGDGIFS PGGAISNMYA 250
    MLIARYKMFP EVKEKGMAAV PRLIAFTSEH SHFSLKKGAA ALGIGTDSVI 300
    LIKCDERGKM IPSDLERRIL EVKQKGFVPF LVSATAGTTV YGAFDPLLAV 350
    ADICKKYKIW MHVDAAWGGG LLMSRKHKWK LNGVERANSV TWNPHKMMGV 400
    PLQCSALLVR EEGLMQSCNQ MHASYLFQQD KHYDLSYDTG DKALQCGRHV 450
    DVFKLWLMWR AKGTTGFEAH IDKCLELAEY LYNIIKNREG YEMVFDGKPQ 500
    HTNVCFWFVP PSLRVLEDNE ERMSRLSKVA PVIKARMMEY GTTMVSYQPL 550
    GDKVNFFRMV ISNPAATHQD IDFLIEEIER LGQDL 585
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M72422 mRNA. Translation: AAA63488.1 .
    PIRi JH0423.
    RefSeqi NP_036695.1. NM_012563.1.
    UniGenei Rn.29951.

    3D structure databases

    ProteinModelPortali Q05683.
    SMRi Q05683. Positions 88-584.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 246551. 1 interaction.
    IntActi Q05683. 1 interaction.
    STRINGi 10116.ENSRNOP00000024901.

    Chemistry

    BindingDBi Q05683.

    PTM databases

    PhosphoSitei Q05683.

    Proteomic databases

    PRIDEi Q05683.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000024901 ; ENSRNOP00000024901 ; ENSRNOG00000018200 .
    GeneIDi 24380.
    KEGGi rno:24380.
    UCSCi RGD:2653. rat.

    Organism-specific databases

    CTDi 2572.
    RGDi 2653. Gad2.

    Phylogenomic databases

    eggNOGi COG0076.
    GeneTreei ENSGT00730000110441.
    HOGENOMi HOG000005382.
    HOVERGENi HBG004980.
    InParanoidi Q05683.
    KOi K01580.
    OMAi WRAKGTT.
    OrthoDBi EOG7H1JM3.
    PhylomeDBi Q05683.
    TreeFami TF314688.

    Enzyme and pathway databases

    Reactomei REACT_196234. GABA synthesis.
    SABIO-RK Q05683.

    Miscellaneous databases

    NextBioi 603141.
    PROi Q05683.

    Gene expression databases

    Genevestigatori Q05683.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProi IPR002129. 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 ]
    Pfami PF00282. Pyridoxal_deC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53383. SSF53383. 1 hit.
    PROSITEi PS00392. DDC_GAD_HDC_YDC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 106 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