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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

  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
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.
REACT_262380. GABA synthesis, release, reuptake and degradation.
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
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.
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.
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_196234. GABA synthesis.
REACT_262380. GABA synthesis, release, reuptake and degradation.
SABIO-RKQ05683.

Miscellaneous databases

NextBioi603141.
PROiQ05683.

Gene expression databases

ExpressionAtlasiQ05683. baseline.
GenevestigatoriQ05683.

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: January 7, 2015
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, 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.