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P18088

- DCE1_RAT

UniProt

P18088 - DCE1_RAT

Protein

Glutamate decarboxylase 1

Gene

Gad1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      Previous versions | rss
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    Functioni

    Catalyzes the production of GABA.

    Catalytic activityi

    L-glutamate = 4-aminobutanoate + CO2.

    Cofactori

    Pyridoxal phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei566 – 5661SubstrateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. gamma-aminobutyric acid biosynthetic process Source: RGD
    2. neurotransmitter biosynthetic process Source: UniProtKB-KW
    3. response to drug 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-RKP18088.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate decarboxylase 1 (EC:4.1.1.15)
    Alternative name(s):
    67 kDa glutamic acid decarboxylase
    Short name:
    GAD-67
    Glutamate decarboxylase 67 kDa isoform
    Gene namesi
    Name:Gad1
    Synonyms:Gad67
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 3

    Organism-specific databases

    RGDi2652. Gad1.

    Subcellular locationi

    GO - Cellular componenti

    1. axon terminus Source: Ensembl
    2. cell cortex Source: Ensembl
    3. mitochondrion Source: Ensembl
    4. presynaptic active zone Source: Ensembl

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 593593Glutamate decarboxylase 1PRO_0000146967Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei404 – 4041N6-(pyridoxal phosphate)lysineBy similarity

    Proteomic databases

    PaxDbiP18088.
    PRIDEiP18088.

    PTM databases

    PhosphoSiteiP18088.

    Expressioni

    Gene expression databases

    ArrayExpressiP18088.
    GenevestigatoriP18088.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi246550. 1 interaction.
    IntActiP18088. 2 interactions.
    MINTiMINT-347612.

    Structurei

    3D structure databases

    ProteinModelPortaliP18088.
    SMRiP18088. Positions 92-592.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni189 – 1913Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the group II decarboxylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0076.
    GeneTreeiENSGT00730000110441.
    HOGENOMiHOG000005382.
    HOVERGENiHBG004980.
    InParanoidiP18088.
    KOiK01580.
    OMAiEYLYTKI.
    OrthoDBiEOG7H1JM3.
    PhylomeDBiP18088.
    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.

    P18088-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASSTPSPAT SSNAGADPNT TNLRPTTYDT WCGVAHGCTR KLGLKICGFL    50
    QRTNSLEEKS RLVSAFRERQ ASKNLLSCEN SDPGARFRRT ETDFSNLFAQ 100
    DLLPAKNGEE QTVQFLLEVV DILLNYVRKT FDRSTKVLDF HHPHQLLEGM 150
    EGFNLELSDH PESLEQILVD CRDTLKYGVR TGHPRFFNQL STGLDIIGLA 200
    GEWLTSTANT NMFTYEIAPV FVLMEQITLK KMREIIGWSN KDGDGIFSPG 250
    GAISNMYSIM AARYKYFPEV KTKGMAAVPK LVLFTSEHSH YSIKKAGAAL 300
    GFGTDNVILI KCNERGKIIP ADLEAKILDA KQKGFVPLYV NATAGTTVYG 350
    AFDPIQEIAD ICEKYNLWLH VDAAWGGGLL MSRKHRHKLS GIERANSVTW 400
    NPHKMMGVLL QCSAILVKEK GILQGCNQMC AGYLFQPDKQ YDVSYDTGDK 450
    AIQCGRHVDI FKFWLMWKAK GTVGFENQIN KCLELAEYLY AKIKNREEFE 500
    MVFNGEPEHT NVCFWYIPQS LRGVPDSPER REKLHRVAPK IKALMMESGT 550
    TMVGYQPQGD KANFFRMVIS NPAATQSDID FLIEEIERLG QDL 593
    Length:593
    Mass (Da):66,640
    Last modified:November 1, 1990 - v1
    Checksum:iEF83239C30301F69
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti103 – 1031L → V in CAA40800. (PubMed:2299361)Curated
    Sequence conflicti284 – 2841F → S in CAA40800. (PubMed:2299361)Curated
    Sequence conflicti287 – 2882EH → AD in CAA40800. (PubMed:2299361)Curated
    Sequence conflicti344 – 3452AG → EA in CAA40800. (PubMed:2299361)Curated
    Sequence conflicti347 – 3471T → I in CAA40800. (PubMed:2299361)Curated
    Sequence conflicti352 – 3532FD → LE in CAA40800. (PubMed:2299361)Curated
    Sequence conflicti380 – 3801L → R in CAA40800. (PubMed:2299361)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34445 mRNA. Translation: AAC42037.1.
    X57572 mRNA. Translation: CAA40800.1.
    X57573 mRNA. Translation: CAA40801.1.
    M76177 mRNA. Translation: AAA41184.1.
    PIRiA41367.
    RefSeqiNP_058703.1. NM_017007.1.
    UniGeneiRn.91245.

    Genome annotation databases

    EnsembliENSRNOT00000000008; ENSRNOP00000000008; ENSRNOG00000000007.
    GeneIDi24379.
    KEGGirno:24379.
    UCSCiRGD:2652. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34445 mRNA. Translation: AAC42037.1 .
    X57572 mRNA. Translation: CAA40800.1 .
    X57573 mRNA. Translation: CAA40801.1 .
    M76177 mRNA. Translation: AAA41184.1 .
    PIRi A41367.
    RefSeqi NP_058703.1. NM_017007.1.
    UniGenei Rn.91245.

    3D structure databases

    ProteinModelPortali P18088.
    SMRi P18088. Positions 92-592.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 246550. 1 interaction.
    IntActi P18088. 2 interactions.
    MINTi MINT-347612.

    Chemistry

    ChEMBLi CHEMBL3758.

    PTM databases

    PhosphoSitei P18088.

    Proteomic databases

    PaxDbi P18088.
    PRIDEi P18088.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000000008 ; ENSRNOP00000000008 ; ENSRNOG00000000007 .
    GeneIDi 24379.
    KEGGi rno:24379.
    UCSCi RGD:2652. rat.

    Organism-specific databases

    CTDi 2571.
    RGDi 2652. Gad1.

    Phylogenomic databases

    eggNOGi COG0076.
    GeneTreei ENSGT00730000110441.
    HOGENOMi HOG000005382.
    HOVERGENi HBG004980.
    InParanoidi P18088.
    KOi K01580.
    OMAi EYLYTKI.
    OrthoDBi EOG7H1JM3.
    PhylomeDBi P18088.
    TreeFami TF314688.

    Enzyme and pathway databases

    Reactomei REACT_196234. GABA synthesis.
    SABIO-RK P18088.

    Miscellaneous databases

    NextBioi 603137.
    PROi P18088.

    Gene expression databases

    ArrayExpressi P18088.
    Genevestigatori P18088.

    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. "Characterization of a cDNA coding for rat glutamic acid decarboxylase."
      Wyborski R.J., Bond R.W., Gottlieb D.I.
      Brain Res. Mol. Brain Res. 8:193-198(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Rat brain glutamic acid decarboxylase sequence deduced from a cloned cDNA."
      Julien J.F., Samama P., Mallet J.
      J. Neurochem. 54:703-705(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Cloning, characterization, and autoimmune recognition of rat islet glutamic acid decarboxylase in insulin-dependent diabetes mellitus."
      Michelsen B.K., Petersen J.S., Boel E., Moldrup A., Dyrberg T., Madsen O.D.
      Proc. Natl. Acad. Sci. U.S.A. 88:8754-8758(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiDCE1_RAT
    AccessioniPrimary (citable) accession number: P18088
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 108 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3