Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10116-01326
Entry Name
UniProt Accession
Theoretical PI
6.45
Molecular Weight
65402.28
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][2]
S-Palmitoylation
Organism
Rattus norvegicus (Rat)
NCBI Taxa ID
10116
Reference
[1] Christgau S, Aanstoot HJ, Schierbeck H, Begley K, Tullin S, Hejnaes K,Baekkeskov S. Membrane anchoring of the autoantigen GAD65 to microvesicles inpancreatic beta-cells by palmitoylation in the NH2-terminal domain. J Cell Biol. 1992 Jul;118(2):309-20.[PMID:1321158]
[2] Shi Y, Veit B, Baekkeskov S. Amino acid residues 24-31 but not palmitoylation of cysteines 30 and 45 are required for membrane anchoring of glutamic aciddecarboxylase, GAD65. J Cell Biol. 1994 Mar;124(6):927-34.[PMID:8132714]
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 FGSEDGSGDP ENPGTARAWC QVAQKFTGGI GNKLCALLYG DSEKPAESGG  60
SVTSRAATRK VACTCDQKPC SCPKGDVNYA LLHATDLLPA CEGERPTLAF LQDVMNILLQ  120
YVVKSFDRST KVIDFHYPNE LLQEYNWELA DQPQNLEEIL THCQTTLKYA IKTGHPRYFN  180
QLSTGLDMVG LAADWLTSTA NTNMFTYEIA PVFVLLEYVT LKKMREIIGW PGGSGDGIFS  240
PGGAISNMYA MLIARYKMFP EVKEKGMAAV PRLIAFTSEH SHFSLKKGAA ALGIGTDSVI  300
LIKCDERGKM IPSDLERRIL EVKQKGFVPF LVSATAGTTV YGAFDPLLAV ADICKKYKIW  360
MHVDAAWGGG LLMSRKHKWK LNGVERANSV TWNPHKMMGV PLQCSALLVR EEGLMQSCNQ  420
MHASYLFQQD KHYDLSYDTG DKALQCGRHV DVFKLWLMWR AKGTTGFEAH IDKCLELAEY  480
LYNIIKNREG YEMVFDGKPQ HTNVCFWFVP PSLRVLEDNE ERMSRLSKVA PVIKARMMEY  540
GTTMVSYQPL GDKVNFFRMV ISNPAATHQD IDFLIEEIER LGQDL                  585
FASTA
(Canonical)
>LipidDB-10116-01326|Q05683
MASPGSGFWSFGSEDGSGDPENPGTARAWCQVAQKFTGGIGNKLCALLYGDSEKPAESGG
SVTSRAATRKVACTCDQKPCSCPKGDVNYALLHATDLLPACEGERPTLAFLQDVMNILLQ
YVVKSFDRSTKVIDFHYPNELLQEYNWELADQPQNLEEILTHCQTTLKYAIKTGHPRYFN
QLSTGLDMVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLKKMREIIGWPGGSGDGIFS
PGGAISNMYAMLIARYKMFPEVKEKGMAAVPRLIAFTSEHSHFSLKKGAAALGIGTDSVI
LIKCDERGKMIPSDLERRILEVKQKGFVPFLVSATAGTTVYGAFDPLLAVADICKKYKIW
MHVDAAWGGGLLMSRKHKWKLNGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQSCNQ
MHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAHIDKCLELAEY
LYNIIKNREGYEMVFDGKPQHTNVCFWFVPPSLRVLEDNEERMSRLSKVAPVIKARMMEY
GTTMVSYQPLGDKVNFFRMVISNPAATHQDIDFLIEEIERLGQDL
Gene Ontology
GO:0031225; C:anchored component of membrane; IDA:RGD
GO:0030424; C:axon; IEA:Ensembl
GO:0030054; C:cell junction; IEA:UniProtKB-KW
GO:0031410; C:cytoplasmic vesicle; IDA:RGD
GO:0005829; C:cytosol; IDA:RGD
GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW
GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD
GO:0005886; C:plasma membrane; IEA:UniProtKB-KW
GO:0030672; C:synaptic vesicle membrane; IDA:RGD
GO:0016595; F:glutamate binding; IDA:RGD
GO:0004351; F:glutamate decarboxylase activity; IDA:RGD
GO:0046982; F:protein heterodimerization activity; IDA:RGD
GO:0030170; F:pyridoxal phosphate binding; IDA:RGD
GO:0006540; P:glutamate decarboxylation to succinate; IDA:RGD
GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW
GO:0042493; P:response to drug; IEP:RGD
GO:0007268; P:synaptic transmission; TAS:RGD
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