ID Q548L6_MOUSE Unreviewed; 593 AA. AC Q548L6; DT 24-MAY-2005, integrated into UniProtKB/TrEMBL. DT 24-MAY-2005, sequence version 1. DT 24-JAN-2024, entry version 156. DE RecName: Full=Glutamate decarboxylase 1 {ECO:0000256|ARBA:ARBA00040578}; DE EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421}; GN Name=Gad1 {ECO:0000313|MGI:MGI:95632}; GN Synonyms=gad67 {ECO:0000313|EMBL:AFX68720.1}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAL37394.1}; RN [1] {ECO:0000313|EMBL:BAE23133.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE23133.1}; RC TISSUE=Brain {ECO:0000313|EMBL:BAE36059.1}, Diencephalon RC {ECO:0000313|EMBL:BAE23133.1}, and Pancreas RC {ECO:0000313|EMBL:BAE28589.1}; RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9; RA Carninci P., Hayashizaki Y.; RT "High-efficiency full-length cDNA cloning."; RL Methods Enzymol. 303:19-44(1999). RN [2] {ECO:0000313|EMBL:BAE23133.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE23133.1}; RC TISSUE=Brain {ECO:0000313|EMBL:BAE36059.1}, Diencephalon RC {ECO:0000313|EMBL:BAE23133.1}, and Pancreas RC {ECO:0000313|EMBL:BAE28589.1}; RX PubMed=11042159; DOI=10.1101/gr.145100; RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.; RT "Normalization and subtraction of cap-trapper-selected cDNAs to prepare RT full-length cDNA libraries for rapid discovery of new genes."; RL Genome Res. 10:1617-1630(2000). RN [3] {ECO:0000313|EMBL:BAE23133.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE23133.1}; RC TISSUE=Brain {ECO:0000313|EMBL:BAE36059.1}, Diencephalon RC {ECO:0000313|EMBL:BAE23133.1}, and Pancreas RC {ECO:0000313|EMBL:BAE28589.1}; RX PubMed=11076861; DOI=10.1101/gr.152600; RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P., RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N., RA Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R., RA Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S., RA Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y., RA Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y., RA Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.; RT "RIKEN integrated sequence analysis (RISA) system--384-format sequencing RT pipeline with 384 multicapillary sequencer."; RL Genome Res. 10:1757-1771(2000). RN [4] {ECO:0000313|EMBL:AAL37394.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:AAL37393.1}, and DBA/2J RC {ECO:0000313|EMBL:AAL37394.1}; RC TISSUE=Whole brain {ECO:0000313|EMBL:AAL37394.1}; RA Fehr C., Buck K.J.; RT "Glutamic acid decarboxylase gene (Gad1 and Gad2) sequence and expression RT in C57BL/6J and DBA/2J mice."; RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:BAE23133.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE23133.1}; RC TISSUE=Brain {ECO:0000313|EMBL:BAE36059.1}, Diencephalon RC {ECO:0000313|EMBL:BAE23133.1}, and Pancreas RC {ECO:0000313|EMBL:BAE28589.1}; RX PubMed=11217851; DOI=10.1038/35055500; RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). RN [6] {ECO:0000313|EMBL:BAE23133.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE23133.1}; RC TISSUE=Brain {ECO:0000313|EMBL:BAE36059.1}, Diencephalon RC {ECO:0000313|EMBL:BAE23133.1}, and Pancreas RC {ECO:0000313|EMBL:BAE28589.1}; RX PubMed=12466851; DOI=10.1038/nature01266; RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [7] {ECO:0000313|EMBL:BAE36059.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE23133.1}; RC TISSUE=Brain {ECO:0000313|EMBL:BAE36059.1}, Diencephalon RC {ECO:0000313|EMBL:BAE23133.1}, and Pancreas RC {ECO:0000313|EMBL:BAE28589.1}; RA Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F., RA Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M., RA Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K., RA Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T., RA Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.; RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases. RN [8] {ECO:0000313|EMBL:BAE23133.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE23133.1}; RC TISSUE=Brain {ECO:0000313|EMBL:BAE36059.1}, Diencephalon RC {ECO:0000313|EMBL:BAE23133.1}, and Pancreas RC {ECO:0000313|EMBL:BAE28589.1}; RG The FANTOM Consortium; RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group); RT "The Transcriptional Landscape of the Mammalian Genome."; RL Science 309:1559-1563(2005). RN [9] {ECO:0000313|EMBL:BAE23133.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE23133.1}; RC TISSUE=Brain {ECO:0000313|EMBL:BAE36059.1}, Diencephalon RC {ECO:0000313|EMBL:BAE23133.1}, and Pancreas RC {ECO:0000313|EMBL:BAE28589.1}; RX PubMed=16141073; DOI=10.1126/science.1112009; RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium; RT "Antisense Transcription in the Mammalian Transcriptome."; RL Science 309:1564-1566(2005). RN [10] {ECO:0007829|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [11] {ECO:0000313|EMBL:AFX68720.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=23220582; DOI=10.1016/j.ibmb.2012.11.001; RA Ilg T., Berger M., Noack S., Rohwer A., Gassel M.; RT "Glutamate decarboxylase of the parasitic arthropods Ctenocephalides felis RT and Rhipicephalus microplus: gene identification, cloning, expression, RT assay development, identification of inhibitors by high throughput RT screening and comparison with the orthologs from Drosophila melanogaster RT and mouse."; RL Insect Biochem. Mol. Biol. 43:162-177(2013). CC -!- FUNCTION: Catalyzes the synthesis of the inhibitory neurotransmitter CC gamma-aminobutyric acid (GABA) with pyridoxal 5'-phosphate as cofactor. CC {ECO:0000256|ARBA:ARBA00037700}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2; CC Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15; CC Evidence={ECO:0000256|ARBA:ARBA00036502}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17786; CC Evidence={ECO:0000256|ARBA:ARBA00036502}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933, CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}. CC -!- SIMILARITY: Belongs to the group II decarboxylase family. CC {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF326547; AAL37393.1; -; mRNA. DR EMBL; AF326548; AAL37394.1; -; mRNA. DR EMBL; KC134210; AFX68720.1; -; mRNA. DR EMBL; AK136801; BAE23133.1; -; mRNA. DR EMBL; AK148497; BAE28589.1; -; mRNA. DR EMBL; AK160868; BAE36059.1; -; mRNA. DR RefSeq; NP_032103.2; NM_008077.5. DR RefSeq; XP_006498828.1; XM_006498765.3. DR RefSeq; XP_006498829.1; XM_006498766.3. DR AlphaFoldDB; Q548L6; -. DR SMR; Q548L6; -. DR MaxQB; Q548L6; -. DR Antibodypedia; 3831; 852 antibodies from 46 providers. DR DNASU; 14415; -. DR GeneID; 14415; -. DR KEGG; mmu:14415; -. DR AGR; MGI:95632; -. DR CTD; 2571; -. DR MGI; MGI:95632; Gad1. DR VEuPathDB; HostDB:ENSMUSG00000070880; -. DR HOGENOM; CLU_011856_0_0_1; -. DR OMA; RHATYHA; -. DR OrthoDB; 888358at2759; -. DR BioGRID-ORCS; 14415; 2 hits in 80 CRISPR screens. DR ExpressionAtlas; Q548L6; baseline and differential. DR GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; IEA:Ensembl. DR GO; GO:0006538; P:glutamate catabolic process; IEA:Ensembl. DR CDD; cd06450; DOPA_deC_like; 1. DR Gene3D; 3.90.1150.170; -; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1. DR InterPro; IPR002129; PyrdxlP-dep_de-COase. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR021115; Pyridoxal-P_BS. DR PANTHER; PTHR45677:SF5; GLUTAMATE DECARBOXYLASE 1; 1. DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1. DR Pfam; PF00282; Pyridoxal_deC; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1. PE 1: Evidence at protein level; KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382}; KW Neurotransmitter biosynthesis {ECO:0000256|ARBA:ARBA00022979}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50, KW ECO:0000256|RuleBase:RU000382}. FT REGION 1..22 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 404 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50" SQ SEQUENCE 593 AA; 66648 MW; 82D1AAF216F25100 CRC64; MASSTPSPAT SSNAGADPNT TNLRPTTYDT WCGVAHGCTR KLGLKICGFL QRTNSLEEKS RLVSAFRERQ SSKNLLSCEN SDQGARFRRT ETDFSNLFAQ DLLPAKNGEE QTAQFLLEVV DILLNYVRKT FDRSTKVLDF HHPHQLLEGM EGFNLELSDH PESLEQILVD CRDTLKYGVR TGHPRFFNQL STGLDIIGLA GEWLTSTANT NMFTYEIAPV FVLMEQITLK KMREIVGWSN KDGDGIFSPG GAISNMYSIM AARYKYFPEV KTKGMAAVPK LVLFTSEHSH YSIKKAGAAL GFGTDNVILI KCNERGKIIP ADLEAKILDA KQKGYVPLYV NATAGTTVYG AFDPIQEIAD ICEKYNLWLH VDAAWGGGLL MSRKHRHKLS GIERANSVTW NPHKMMGVLL QCSAILVKEK GILQGCNQMC AGYLFQPDKQ YDVSYDTGDK AIQCGRHVDI FKFWLMWKAK GTVGFENQIN KCLELADYLY AKIKNREEFE MVFDGEPEHT NVCFWYIPQS LRGVPDSPER REKLHRVAPK IKALMMESGT TMVGYQPQGD KANFFRMVIS NPAATQSDID FLIEEIERLG QDL //