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P48321 (DCE2_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length585 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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

Cytoplasm › cytosol By similarity. Cytoplasmic vesicle By similarity. Cell junction › synapse › presynaptic 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.

Post-translational modification

Phosphorylated; which does not affect kinetic parameters or subcellular location By similarity.

Palmitoylated; which is required for presynaptic clustering By similarity.

Sequence similarities

Belongs to the group II decarboxylase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 585585Glutamate decarboxylase 2
PRO_0000146970

Regions

Region181 – 1833Substrate binding By similarity

Sites

Binding site5581Substrate By similarity

Amino acid modifications

Modified residue31Phosphoserine By similarity
Modified residue61Phosphoserine By similarity
Modified residue101Phosphoserine By similarity
Modified residue131Phosphoserine By similarity
Modified residue3961N6-(pyridoxal phosphate)lysine By similarity
Lipidation301S-palmitoyl cysteine By similarity
Lipidation451S-palmitoyl cysteine By similarity

Sequences

Sequence LengthMass (Da)Tools
P48321 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 4FF2810637671B6B

FASTA58565,388
        10         20         30         40         50         60 
MASPGSGFWS FGSEDGSGDP ENSGTARAWC QVAQKFTGGI GNKLCALLYG DAEKPAESGG 

        70         80         90        100        110        120 
SQPPRTTSRK ATCACNQKPC NCPKAEVNYA FLHATDLLPA CDGERPTLAF LQDVMDILLQ 

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

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

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

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

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

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

       490        500        510        520        530        540 
LYNIIKNREG YEMVFDGKPQ HTNVCFWYVP PSLRVLDNNE ERMSRLSKVA PVIKARMMES 

       550        560        570        580 
GTTMVSYQPL GDKVNFFRMV ISNPAATHQD IDFLIEEIER LGQDL

« Hide

References

[1]"Sequences of two porcine glutamic acid decarboxylases (65- and 67-kDa GAD)."
Suzuki R., Asami N., Amann E., Wagatsuma M.
Gene 152:257-260(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]Yu H., Li J.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D31848 mRNA. Translation: BAA06635.1.
AY973276 mRNA. Translation: AAY28733.1.
PIRJC4064.
RefSeqNP_999060.2. NM_213895.2.
UniGeneSsc.5021.

3D structure databases

ProteinModelPortalP48321.
SMRP48321. Positions 88-584.
ModBaseSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000011796.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSSSCT00000012104; ENSSSCP00000011796; ENSSSCG00000011060.
GeneID396929.
KEGGssc:396929.

Organism-specific databases

CTD2572.

Phylogenomic databases

eggNOGCOG0076.
GeneTreeENSGT00550000074275.
HOGENOMHOG000005382.
HOVERGENHBG004980.
KOK01580.
OMAHQDIDFL.
OrthoDBEOG408N7N.

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. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITEPS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChEMBLCHEMBL4186.

Entry information

Entry nameDCE2_PIG
AccessionPrimary (citable) accession number: P48321
Secondary accession number(s): Q506P9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 3, 2013
This is version 85 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

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