Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00546
Entry Name
UniProt Accession
Theoretical PI
6.45
Molecular Weight
65411.28
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Glutamate decarboxylase 2
Protein Synonyms/Alias
4.1.1.15; 65 kDa glutamic acid decarboxylase; GAD-65; Glutamate decarboxylase 65 kDa isoform;
Gene Name
GAD2
Gene Synonyms/Alias
GAD65;
Created Date
01-FEB-1996
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
30
Canonical
PGTARAWCQVAQKFT
[1]
S-Palmitoylation
45
Canonical
GGIGNKLCALLYGDA
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Kanaani J, el-Husseini Ael-D, Aguilera-Moreno A, Diacovo JM, Bredt DS,Baekkeskov S. A combination of three distinct trafficking signals mediates axonaltargeting and presynaptic clustering of GAD65. J Cell Biol. 2002 Sep30;158(7):1229-38.[PMID:12356867]
Functional Description
Catalyzes the production of GABA.
Sequence Annotation
Region: 181 183 Substrate binding.
Binding site: 558 558 Substrate.
Modified residue: 3 3 Phosphoserine.
Modified residue: 6 6 Phosphoserine.
Modified residue: 10 10 Phosphoserine.
Modified residue: 13 13 Phosphoserine.
Modified residue: 396 396 N6-(pyridoxal phosphate)lysine.
Protein Length
585 AA.
Protein Sequence
(Canonical)
MASPGSGFWS FGSEDGSGDS ENPGTARAWC QVAQKFTGGI GNKLCALLYG DAEKPAESGG  60
SQPPRAAARK AACACDQKPC SCSKVDVNYA FLHATDLLPA CDGERPTLAF LQDVMNILLQ  120
YVVKSFDRST KVIDFHYPNE LLQEYNWELA DQPQNLEEIL MHCQTTLKYA IKTGHPRYFN  180
QLSTGLDMVG LAADWLTSTA NTNMFTYEIA PVFVLLEYVT LKKMREIIGW PGGSGDGIFS  240
PGGAISNMYA MMIARFKMFP EVKEKGMAAL PRLIAFTSEH SHFSLKKGAA ALGIGTDSVI  300
LIKCDERGKM IPSDLERRIL EAKQKGFVPF LVSATAGTTV YGAFDPLLAV ADICKKYKIW  360
MHVDAAWGGG LLMSRKHKWK LSGVERANSV TWNPHKMMGV PLQCSALLVR EEGLMQNCNQ  420
MHASYLFQQD KHYDLSYDTG DKALQCGRHV DVFKLWLMWR AKGTTGFEAH VDKCLELAEY  480
LYNIIKNREG YEMVFDGKPQ HTNVCFWYIP PSLRTLEDNE ERMSRLSKVA PVIKARMMEY  540
GTTMVSYQPL GDKVNFFRMV ISNPAATHQD IDFLIEEIER LGQDL                  585
FASTA
(Canonical)
>LipidDB-9606-00546|Q05329
MASPGSGFWSFGSEDGSGDSENPGTARAWCQVAQKFTGGIGNKLCALLYGDAEKPAESGG
SQPPRAAARKAACACDQKPCSCSKVDVNYAFLHATDLLPACDGERPTLAFLQDVMNILLQ
YVVKSFDRSTKVIDFHYPNELLQEYNWELADQPQNLEEILMHCQTTLKYAIKTGHPRYFN
QLSTGLDMVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLKKMREIIGWPGGSGDGIFS
PGGAISNMYAMMIARFKMFPEVKEKGMAALPRLIAFTSEHSHFSLKKGAAALGIGTDSVI
LIKCDERGKMIPSDLERRILEAKQKGFVPFLVSATAGTTVYGAFDPLLAVADICKKYKIW
MHVDAAWGGGLLMSRKHKWKLSGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQNCNQ
MHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAHVDKCLELAEY
LYNIIKNREGYEMVFDGKPQHTNVCFWYIPPSLRTLEDNEERMSRLSKVAPVIKARMMEY
GTTMVSYQPLGDKVNFFRMVISNPAATHQDIDFLIEEIERLGQDL
Gene Ontology
GO:0031225; C:anchored component of membrane; IEA:Ensembl
GO:0030424; C:axon; IEA:Ensembl
GO:0030054; C:cell junction; IEA:UniProtKB-KW
GO:0061202; C:clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane; TAS:Reactome
GO:0005829; C:cytosol; IEA:Ensembl
GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW
GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0030672; C:synaptic vesicle membrane; IEA:Ensembl
GO:0016595; F:glutamate binding; IEA:Ensembl
GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC
GO:0030170; F:pyridoxal phosphate binding; IEA:Ensembl
GO:0006540; P:glutamate decarboxylation to succinate; TAS:ProtInc
GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW
GO:0007269; P:neurotransmitter secretion; TAS:Reactome
GO:0042493; P:response to drug; IEA:Ensembl
GO:0007268; P:synaptic transmission; TAS:Reactome
Interpro
InterPro; IPR002129; PyrdxlP-dep_de-COase
InterPro; IPR015424; PyrdxlP-dep_Trfase
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1
InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2
InterPro; IPR021115; Pyridoxal-P_BS
Pfam
Pfam; PF00282; Pyridoxal_deC;
SMART
PROSITE
PROSITE; PS00392; DDC_GAD_HDC_YDC;
PRINTS