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Protein

Glutamate decarboxylase 1

Gene

Gad1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei566SubstrateBy similarity1

GO - Molecular functioni

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

GO - Biological processi

  • gamma-aminobutyric acid biosynthetic process Source: RGD
  • neurotransmitter biosynthetic process Source: UniProtKB-KW
  • 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

ReactomeiR-RNO-888568. GABA synthesis.
R-RNO-888590. GABA synthesis, release, reuptake and degradation.
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
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi2652. Gad1.

Subcellular locationi

GO - Cellular componenti

  • intracellular Source: Ensembl
  • presynaptic active zone Source: MGI
Complete GO annotation...

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3758.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001469671 – 593Glutamate decarboxylase 1Add BLAST593

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei77PhosphoserineBy similarity1
Modified residuei404N6-(pyridoxal phosphate)lysineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP18088.
PRIDEiP18088.

PTM databases

iPTMnetiP18088.
PhosphoSitePlusiP18088.

Expressioni

Gene expression databases

BgeeiENSRNOG00000000007.
ExpressionAtlasiP18088. baseline and differential.
GenevisibleiP18088. RN.

Interactioni

Subunit structurei

Homodimer.

GO - Molecular functioni

  • protein heterodimerization activity Source: RGD
  • protein N-terminus binding Source: RGD

Protein-protein interaction databases

BioGridi246550. 1 interactor.
IntActiP18088. 2 interactors.
MINTiMINT-347612.
STRINGi10116.ENSRNOP00000000008.

Structurei

3D structure databases

ProteinModelPortaliP18088.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni189 – 191Substrate bindingBy similarity3

Sequence similaritiesi

Belongs to the group II decarboxylase family.Curated

Phylogenomic databases

eggNOGiKOG0629. Eukaryota.
COG0076. LUCA.
GeneTreeiENSGT00760000119205.
HOGENOMiHOG000005382.
HOVERGENiHBG004980.
InParanoidiP18088.
KOiK01580.
OMAiEYLYTKI.
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

        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)DescriptionActionsGraphical viewLength
Sequence conflicti103L → V in CAA40800 (PubMed:2299361).Curated1
Sequence conflicti284F → S in CAA40800 (PubMed:2299361).Curated1
Sequence conflicti287 – 288EH → AD in CAA40800 (PubMed:2299361).Curated2
Sequence conflicti344 – 345AG → EA in CAA40800 (PubMed:2299361).Curated2
Sequence conflicti347T → I in CAA40800 (PubMed:2299361).Curated1
Sequence conflicti352 – 353FD → LE in CAA40800 (PubMed:2299361).Curated2
Sequence conflicti380L → R in CAA40800 (PubMed:2299361).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
XP_017446943.1. XM_017591454.1.
XP_017446944.1. XM_017591455.1.
UniGeneiRn.91245.

Genome annotation databases

EnsembliENSRNOT00000000008; ENSRNOP00000000008; ENSRNOG00000000007.
ENSRNOT00000087712; ENSRNOP00000072778; ENSRNOG00000000007.
GeneIDi24379.
KEGGirno:24379.
UCSCiRGD:2652. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
XP_017446943.1. XM_017591454.1.
XP_017446944.1. XM_017591455.1.
UniGeneiRn.91245.

3D structure databases

ProteinModelPortaliP18088.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246550. 1 interactor.
IntActiP18088. 2 interactors.
MINTiMINT-347612.
STRINGi10116.ENSRNOP00000000008.

Chemistry databases

ChEMBLiCHEMBL3758.

PTM databases

iPTMnetiP18088.
PhosphoSitePlusiP18088.

Proteomic databases

PaxDbiP18088.
PRIDEiP18088.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000000008; ENSRNOP00000000008; ENSRNOG00000000007.
ENSRNOT00000087712; ENSRNOP00000072778; ENSRNOG00000000007.
GeneIDi24379.
KEGGirno:24379.
UCSCiRGD:2652. rat.

Organism-specific databases

CTDi2571.
RGDi2652. Gad1.

Phylogenomic databases

eggNOGiKOG0629. Eukaryota.
COG0076. LUCA.
GeneTreeiENSGT00760000119205.
HOGENOMiHOG000005382.
HOVERGENiHBG004980.
InParanoidiP18088.
KOiK01580.
OMAiEYLYTKI.
PhylomeDBiP18088.
TreeFamiTF314688.

Enzyme and pathway databases

ReactomeiR-RNO-888568. GABA synthesis.
R-RNO-888590. GABA synthesis, release, reuptake and degradation.
SABIO-RKP18088.

Miscellaneous databases

PROiP18088.

Gene expression databases

BgeeiENSRNOG00000000007.
ExpressionAtlasiP18088. baseline and differential.
GenevisibleiP18088. 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...

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: November 30, 2016
This is version 128 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

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 one 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.