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P18088 (DCE1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 106. 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 1

EC=4.1.1.15
Alternative name(s):
67 kDa glutamic acid decarboxylase
Short name=GAD-67
Glutamate decarboxylase 67 kDa isoform
Gene names
Name:Gad1
Synonyms:Gad67
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length593 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.

Sequence similarities

Belongs to the group II decarboxylase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 593593Glutamate decarboxylase 1
PRO_0000146967

Regions

Region189 – 1913Substrate binding By similarity

Sites

Binding site5661Substrate By similarity

Amino acid modifications

Modified residue4041N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict1031L → V in CAA40800. Ref.2
Sequence conflict2841F → S in CAA40800. Ref.2
Sequence conflict287 – 2882EH → AD in CAA40800. Ref.2
Sequence conflict344 – 3452AG → EA in CAA40800. Ref.2
Sequence conflict3471T → I in CAA40800. Ref.2
Sequence conflict352 – 3532FD → LE in CAA40800. Ref.2
Sequence conflict3801L → R in CAA40800. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P18088 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: EF83239C30301F69

FASTA59366,640
        10         20         30         40         50         60 
MASSTPSPAT SSNAGADPNT TNLRPTTYDT WCGVAHGCTR KLGLKICGFL QRTNSLEEKS 

        70         80         90        100        110        120 
RLVSAFRERQ ASKNLLSCEN SDPGARFRRT ETDFSNLFAQ DLLPAKNGEE QTVQFLLEVV 

       130        140        150        160        170        180 
DILLNYVRKT FDRSTKVLDF HHPHQLLEGM EGFNLELSDH PESLEQILVD CRDTLKYGVR 

       190        200        210        220        230        240 
TGHPRFFNQL STGLDIIGLA GEWLTSTANT NMFTYEIAPV FVLMEQITLK KMREIIGWSN 

       250        260        270        280        290        300 
KDGDGIFSPG GAISNMYSIM AARYKYFPEV KTKGMAAVPK LVLFTSEHSH YSIKKAGAAL 

       310        320        330        340        350        360 
GFGTDNVILI KCNERGKIIP ADLEAKILDA KQKGFVPLYV NATAGTTVYG AFDPIQEIAD 

       370        380        390        400        410        420 
ICEKYNLWLH VDAAWGGGLL MSRKHRHKLS GIERANSVTW NPHKMMGVLL QCSAILVKEK 

       430        440        450        460        470        480 
GILQGCNQMC AGYLFQPDKQ YDVSYDTGDK AIQCGRHVDI FKFWLMWKAK GTVGFENQIN 

       490        500        510        520        530        540 
KCLELAEYLY AKIKNREEFE MVFNGEPEHT NVCFWYIPQS LRGVPDSPER REKLHRVAPK 

       550        560        570        580        590 
IKALMMESGT TMVGYQPQGD KANFFRMVIS NPAATQSDID FLIEEIERLG QDL 

« Hide

References

[1]"Characterization of a cDNA coding for rat glutamic acid decarboxylase."
Wyborski R.J., Bond R.W., Gottlieb D.I.
Brain Res. Mol. Brain Res. 8:193-198(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Rat brain glutamic acid decarboxylase sequence deduced from a cloned cDNA."
Julien J.F., Samama P., Mallet J.
J. Neurochem. 54:703-705(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Cloning, characterization, and autoimmune recognition of rat islet glutamic acid decarboxylase in insulin-dependent diabetes mellitus."
Michelsen B.K., Petersen J.S., Boel E., Moldrup A., Dyrberg T., Madsen O.D.
Proc. Natl. Acad. Sci. U.S.A. 88:8754-8758(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M34445 mRNA. Translation: AAC42037.1.
X57572 mRNA. Translation: CAA40800.1.
X57573 mRNA. Translation: CAA40801.1.
M76177 mRNA. Translation: AAA41184.1.
PIRA41367.
RefSeqNP_058703.1. NM_017007.1.
UniGeneRn.91245.

3D structure databases

ProteinModelPortalP18088.
SMRP18088. Positions 92-592.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246550. 1 interaction.
MINTMINT-347612.

Chemistry

ChEMBLCHEMBL3758.

PTM databases

PhosphoSiteP18088.

Proteomic databases

PaxDbP18088.
PRIDEP18088.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000000008; ENSRNOP00000000008; ENSRNOG00000000007.
GeneID24379.
KEGGrno:24379.
UCSCRGD:2652. rat.

Organism-specific databases

CTD2571.
RGD2652. Gad1.

Phylogenomic databases

eggNOGCOG0076.
GeneTreeENSGT00730000110441.
HOGENOMHOG000005382.
HOVERGENHBG004980.
InParanoidP18088.
KOK01580.
OMAEYLYTKI.
OrthoDBEOG7H1JM3.
PhylomeDBP18088.
TreeFamTF314688.

Enzyme and pathway databases

SABIO-RKP18088.

Gene expression databases

ArrayExpressP18088.
GenevestigatorP18088.

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

NextBio603137.
PROP18088.

Entry information

Entry nameDCE1_RAT
AccessionPrimary (citable) accession number: P18088
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: May 14, 2014
This is version 106 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