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Q0VCA1

- DCE1_BOVIN

UniProt

Q0VCA1 - DCE1_BOVIN

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Protein

Glutamate decarboxylase 1

Gene

GAD1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Catalyzes the production of GABA.By similarity

Catalytic activityi

L-glutamate = 4-aminobutanoate + CO2.

Cofactori

Pyridoxal phosphate.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei567 – 5671SubstrateBy similarity

GO - Molecular functioni

  1. glutamate decarboxylase activity Source: UniProtKB-EC
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. carboxylic acid metabolic process Source: InterPro
  2. neurotransmitter biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Neurotransmitter biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiREACT_211255. GABA synthesis, release, reuptake and degradation.
REACT_221236. GABA synthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate decarboxylase 1 (EC:4.1.1.15)
Gene namesi
Name:GAD1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 2

Subcellular locationi

GO - Cellular componenti

  1. intracellular Source: Ensembl
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 594594Glutamate decarboxylase 1PRO_0000289582Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei405 – 4051N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PRIDEiQ0VCA1.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000009547.

Structurei

3D structure databases

ProteinModelPortaliQ0VCA1.
SMRiQ0VCA1. Positions 93-593.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni190 – 1923Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the group II decarboxylase family.Curated

Phylogenomic databases

eggNOGiCOG0076.
GeneTreeiENSGT00760000119205.
HOGENOMiHOG000005382.
HOVERGENiHBG004980.
InParanoidiQ0VCA1.
KOiK01580.
OMAiEYLYTKI.
OrthoDBiEOG7H1JM3.
TreeFamiTF314688.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR002129. 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]
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q0VCA1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASSTPSSSA TSSNAGADPN TTNLRPTTYD TWCGVAHGCT RKLGLKICGF
60 70 80 90 100
LQRTNSLEEK SRLVSAFKER QSSKNLLSCE NSDKDGRFRR TETDFSNLFA
110 120 130 140 150
RDLLPAKNGE EQTVQFLLEV VDILLNYVRK TFDRSTKVLD FHHPHQLLEG
160 170 180 190 200
MEGFNLELSD HPESLEQILV DCRDTLKYGV RTGHPRFFNQ LSTGLDIIGL
210 220 230 240 250
AGEWLTSTAN TNMFTYEIAP VFVLMEQITL KKMREIVGWS SKDGDGIFSP
260 270 280 290 300
GGAISNMYSI MAARFKYFPE VKTKGMAAVP KLVLFTSEHS HYSIKKAGAA
310 320 330 340 350
LGFGTDNVIL IKCNERGKII PADLETKILE AKQKGYVPLY VNATAGTTVY
360 370 380 390 400
GAFDPIQEIA DICEKYNLWL HVDAAWGGGL LMSQKHRHKL SGIERANSVT
410 420 430 440 450
WNPHKMMGVL LQCSAILVKE KGILQGCNQM CAGYLFQPDK QYDVSYDTGD
460 470 480 490 500
KAIQCGRHVD IFKFWLMWKA KGTVGFENQI NKCLELAEYL YAKIKNREEF
510 520 530 540 550
EMVFDGEPEH TNVCFWYIPQ SLRGVPDSPE RREKLHRVAP KIKALMMESG
560 570 580 590
TTMVGYQPQG DKANFFRMVI SNPAATQSDI DFLIEEIERL GQDL
Length:594
Mass (Da):66,784
Last modified:September 5, 2006 - v1
Checksum:i2936F526D5E64EDD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC120278 mRNA. Translation: AAI20279.1.
RefSeqiNP_001069224.1. NM_001075756.2.
XP_005202387.1. XM_005202330.1.
UniGeneiBt.26356.

Genome annotation databases

EnsembliENSBTAT00000009547; ENSBTAP00000009547; ENSBTAG00000007258.
GeneIDi517552.
KEGGibta:517552.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC120278 mRNA. Translation: AAI20279.1 .
RefSeqi NP_001069224.1. NM_001075756.2.
XP_005202387.1. XM_005202330.1.
UniGenei Bt.26356.

3D structure databases

ProteinModelPortali Q0VCA1.
SMRi Q0VCA1. Positions 93-593.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9913.ENSBTAP00000009547.

Proteomic databases

PRIDEi Q0VCA1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000009547 ; ENSBTAP00000009547 ; ENSBTAG00000007258 .
GeneIDi 517552.
KEGGi bta:517552.

Organism-specific databases

CTDi 2571.

Phylogenomic databases

eggNOGi COG0076.
GeneTreei ENSGT00760000119205.
HOGENOMi HOG000005382.
HOVERGENi HBG004980.
InParanoidi Q0VCA1.
KOi K01580.
OMAi EYLYTKI.
OrthoDBi EOG7H1JM3.
TreeFami TF314688.

Enzyme and pathway databases

Reactomei REACT_211255. GABA synthesis, release, reuptake and degradation.
REACT_221236. GABA synthesis.

Miscellaneous databases

NextBioi 20872469.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi IPR002129. 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 ]
Pfami PF00282. Pyridoxal_deC. 1 hit.
[Graphical view ]
SUPFAMi SSF53383. SSF53383. 1 hit.
PROSITEi PS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Fetal cerebellum.

Entry informationi

Entry nameiDCE1_BOVIN
AccessioniPrimary (citable) accession number: Q0VCA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: September 5, 2006
Last modified: October 29, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3