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P18088

- DCE1_RAT

UniProt

P18088 - DCE1_RAT

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Protein

Glutamate decarboxylase 1

Gene

Gad1

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

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
Complete GO annotation...

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. intracellular Source: Ensembl
Complete GO annotation...

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

ExpressionAtlasiP18088. baseline and differential.
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.
GeneTreeiENSGT00760000119205.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASSTPSPAT SSNAGADPNT TNLRPTTYDT WCGVAHGCTR KLGLKICGFL
60 70 80 90 100
QRTNSLEEKS RLVSAFRERQ ASKNLLSCEN SDPGARFRRT ETDFSNLFAQ
110 120 130 140 150
DLLPAKNGEE QTVQFLLEVV DILLNYVRKT FDRSTKVLDF HHPHQLLEGM
160 170 180 190 200
EGFNLELSDH PESLEQILVD CRDTLKYGVR TGHPRFFNQL STGLDIIGLA
210 220 230 240 250
GEWLTSTANT NMFTYEIAPV FVLMEQITLK KMREIIGWSN KDGDGIFSPG
260 270 280 290 300
GAISNMYSIM AARYKYFPEV KTKGMAAVPK LVLFTSEHSH YSIKKAGAAL
310 320 330 340 350
GFGTDNVILI KCNERGKIIP ADLEAKILDA KQKGFVPLYV NATAGTTVYG
360 370 380 390 400
AFDPIQEIAD ICEKYNLWLH VDAAWGGGLL MSRKHRHKLS GIERANSVTW
410 420 430 440 450
NPHKMMGVLL QCSAILVKEK GILQGCNQMC AGYLFQPDKQ YDVSYDTGDK
460 470 480 490 500
AIQCGRHVDI FKFWLMWKAK GTVGFENQIN KCLELAEYLY AKIKNREEFE
510 520 530 540 550
MVFNGEPEHT NVCFWYIPQS LRGVPDSPER REKLHRVAPK IKALMMESGT
560 570 580 590
TMVGYQPQGD KANFFRMVIS NPAATQSDID FLIEEIERLG QDL
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 ENSGT00760000119205.
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

ExpressionAtlasi P18088. baseline and differential.
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 29, 2014
This is version 109 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