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Q05683 (DCE2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Gad2
Synonyms:Gad65
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length585 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the production of GABA.

Catalytic activity

L-glutamate = 4-aminobutanoate + CO2.

Cofactor

Pyridoxal phosphate.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasmcytosol By similarity. Cytoplasmic vesicle By similarity. Cell junctionsynapsepresynaptic cell membrane; Lipid-anchor By similarity. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Associated to cytoplasmic vesicles. In neurons, cytosolic leaflet of Golgi membranes and presynaptic clusters By similarity. Ref.3

Post-translational modification

The N-terminus is blocked.

Phosphorylated; which does not affect kinetic parameters or subcellular location. Ref.5

Palmitoylated; which is required for presynaptic clustering By similarity. Ref.3 Ref.4

Sequence similarities

Belongs to the group II decarboxylase family.

Biophysicochemical properties

Kinetic parameters:

KM=1.02 mM for glutamate Ref.5

Ontologies

Keywords
   Biological processNeurotransmitter biosynthesis
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoplasmic vesicle
Golgi apparatus
Membrane
Synapse
   LigandPyridoxal phosphate
   Molecular functionDecarboxylase
Lyase
   PTMLipoprotein
Palmitate
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processglutamate decarboxylation to succinate

Inferred from direct assay Ref.5. Source: RGD

neurotransmitter biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

response to drug

Inferred from expression pattern PubMed 19359144. Source: RGD

synaptic transmission

Traceable author statement Ref.5. Source: RGD

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

anchored component of membrane

Inferred from direct assay Ref.4. Source: RGD

axon

Inferred from electronic annotation. Source: Ensembl

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasmic vesicle

Inferred from direct assay Ref.4. Source: RGD

cytosol

Inferred from direct assay PubMed 17600303. Source: RGD

perinuclear region of cytoplasm

Inferred from direct assay Ref.4. Source: RGD

presynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

synaptic vesicle membrane

Inferred from direct assay Ref.5. Source: RGD

   Molecular_functionglutamate binding

Inferred from direct assay PubMed 10812196. Source: RGD

glutamate decarboxylase activity

Inferred from direct assay PubMed 10812196Ref.5. Source: RGD

protein heterodimerization activity

Inferred from direct assay PubMed 7836456. Source: RGD

pyridoxal phosphate binding

Inferred from direct assay PubMed 1880546. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 585585Glutamate decarboxylase 2
PRO_0000146971

Regions

Region181 – 1833Substrate binding By similarity

Sites

Binding site5581Substrate By similarity

Amino acid modifications

Modified residue31Phosphoserine Ref.5
Modified residue61Phosphoserine Ref.5
Modified residue101Phosphoserine Ref.5
Modified residue131Phosphoserine Ref.5
Modified residue3961N6-(pyridoxal phosphate)lysine By similarity
Lipidation301S-palmitoyl cysteine Ref.3 Ref.4
Lipidation451S-palmitoyl cysteine Ref.3 Ref.4

Experimental info

Mutagenesis301C → A: Abolishes palmitoylation but not membrane-association; when associates with A-45. Ref.4
Mutagenesis451C → A: Abolishes palmitoylation but not membrane-association; when associates with A-30. Ref.4
Mutagenesis731C → S: No effect on palmitoylation. Ref.4
Mutagenesis751C → S: No effect on palmitoylation. Ref.4
Mutagenesis801C → S: No effect on palmitoylation. Ref.4
Mutagenesis821C → S: No effect on palmitoylation. Ref.4
Mutagenesis1011C → S: No effect on palmitoylation. Ref.4
Sequence conflict1901G → V AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q05683 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: C04040B7BA7B37D1

FASTA58565,402
        10         20         30         40         50         60 
MASPGSGFWS FGSEDGSGDP ENPGTARAWC QVAQKFTGGI GNKLCALLYG DSEKPAESGG 

        70         80         90        100        110        120 
SVTSRAATRK VACTCDQKPC SCPKGDVNYA LLHATDLLPA CEGERPTLAF LQDVMNILLQ 

       130        140        150        160        170        180 
YVVKSFDRST KVIDFHYPNE LLQEYNWELA DQPQNLEEIL THCQTTLKYA IKTGHPRYFN 

       190        200        210        220        230        240 
QLSTGLDMVG LAADWLTSTA NTNMFTYEIA PVFVLLEYVT LKKMREIIGW PGGSGDGIFS 

       250        260        270        280        290        300 
PGGAISNMYA MLIARYKMFP EVKEKGMAAV PRLIAFTSEH SHFSLKKGAA ALGIGTDSVI 

       310        320        330        340        350        360 
LIKCDERGKM IPSDLERRIL EVKQKGFVPF LVSATAGTTV YGAFDPLLAV ADICKKYKIW 

       370        380        390        400        410        420 
MHVDAAWGGG LLMSRKHKWK LNGVERANSV TWNPHKMMGV PLQCSALLVR EEGLMQSCNQ 

       430        440        450        460        470        480 
MHASYLFQQD KHYDLSYDTG DKALQCGRHV DVFKLWLMWR AKGTTGFEAH IDKCLELAEY 

       490        500        510        520        530        540 
LYNIIKNREG YEMVFDGKPQ HTNVCFWFVP PSLRVLEDNE ERMSRLSKVA PVIKARMMEY 

       550        560        570        580 
GTTMVSYQPL GDKVNFFRMV ISNPAATHQD IDFLIEEIER LGQDL 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M72422 mRNA. Translation: AAA63488.1.
PIRJH0423.
RefSeqNP_036695.1. NM_012563.1.
UniGeneRn.29951.

3D structure databases

ProteinModelPortalQ05683.
SMRQ05683. Positions 88-584.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246551. 1 interaction.
STRING10116.ENSRNOP00000024901.

Chemistry

BindingDBQ05683.

PTM databases

PhosphoSiteQ05683.

Proteomic databases

PRIDEQ05683.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000024901; ENSRNOP00000024901; ENSRNOG00000018200.
GeneID24380.
KEGGrno:24380.
UCSCRGD:2653. rat.

Organism-specific databases

CTD2572.
RGD2653. Gad2.

Phylogenomic databases

eggNOGCOG0076.
GeneTreeENSGT00730000110441.
HOGENOMHOG000005382.
HOVERGENHBG004980.
InParanoidQ05683.
KOK01580.
OMAWRAKGTT.
OrthoDBEOG7H1JM3.
PhylomeDBQ05683.
TreeFamTF314688.

Enzyme and pathway databases

SABIO-RKQ05683.

Gene expression databases

GenevestigatorQ05683.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR002129. 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]
PfamPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio603141.
PROQ05683.

Entry information

Entry nameDCE2_RAT
AccessionPrimary (citable) accession number: Q05683
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families