GADL1_MOUSE
ID GADL1_MOUSE Reviewed; 550 AA.
AC Q80WP8; Q9CTD2;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 3.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Acidic amino acid decarboxylase GADL1 {ECO:0000303|PubMed:29372909};
DE AltName: Full=Aspartate 1-decarboxylase;
DE Short=ADC;
DE EC=4.1.1.11 {ECO:0000269|PubMed:26327310};
DE AltName: Full=Cysteine sulfinic acid decarboxylase;
DE Short=CSADC;
DE EC=4.1.1.29 {ECO:0000269|PubMed:26327310};
DE AltName: Full=Glutamate decarboxylase-like protein 1 {ECO:0000303|PubMed:23038267};
GN Name=Gadl1 {ECO:0000303|PubMed:23038267};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 23-550 (ISOFORM 2).
RC TISSUE=Olfactory epithelium;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 341-550 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=23038267; DOI=10.1074/jbc.m112.393728;
RA Liu P., Ge X., Ding H., Jiang H., Christensen B.M., Li J.;
RT "Role of glutamate decarboxylase-like protein 1 (GADL1) in taurine
RT biosynthesis.";
RL J. Biol. Chem. 287:40898-40906(2012).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=26327310; DOI=10.1016/j.neuint.2015.08.013;
RA Winge I., Teigen K., Fossbakk A., Mahootchi E., Kleppe R., Skoeldberg F.,
RA Kaempe O., Haavik J.;
RT "Mammalian CSAD and GADL1 have distinct biochemical properties and patterns
RT of brain expression.";
RL Neurochem. Int. 90:173-184(2015).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 49-550, COFACTOR, AND SUBUNIT.
RX PubMed=29372909; DOI=10.1107/s2053230x17017848;
RA Raasakka A., Mahootchi E., Winge I., Luan W., Kursula P., Haavik J.;
RT "Structure of the mouse acidic amino acid decarboxylase GADL1.";
RL Acta Crystallogr. F Struct. Biol. Commun. 74:65-73(2018).
CC -!- FUNCTION: Catalyzes the decarboxylation of L-aspartate, 3-sulfino-L-
CC alanine (cysteine sulfinic acid), and L-cysteate to beta-alanine,
CC hypotaurine and taurine, respectively. The preferred substrate is L-
CC aspartate. Does not exhibit any decarboxylation activity toward
CC glutamate. {ECO:0000269|PubMed:26327310}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-aspartate = beta-alanine + CO2; Xref=Rhea:RHEA:19497,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29991,
CC ChEBI:CHEBI:57966; EC=4.1.1.11;
CC Evidence={ECO:0000269|PubMed:26327310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-sulfino-L-alanine + H(+) = CO2 + hypotaurine;
CC Xref=Rhea:RHEA:16877, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57853, ChEBI:CHEBI:61085; EC=4.1.1.29;
CC Evidence={ECO:0000269|PubMed:26327310};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-cysteate = CO2 + taurine; Xref=Rhea:RHEA:25221,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58090,
CC ChEBI:CHEBI:507393; EC=4.1.1.29;
CC Evidence={ECO:0000269|PubMed:26327310};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:29372909};
CC -!- ACTIVITY REGULATION: Activated weakly by 0.2-0.4 mM Li(+). Inhibited by
CC bis-carboxymethyl-trithiocarbonate, ethylxanthogenacetic acid and 2,5-
CC disulfoaniline. {ECO:0000269|PubMed:26327310}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.12 mM for 3-sulfino-L-alanine (cysteine sulfinic acid)
CC {ECO:0000269|PubMed:26327310};
CC KM=31.7 mM for L-aspartate {ECO:0000269|PubMed:26327310};
CC Vmax=3.84 umol/min/mg enzyme with 3-sulfino-L-alanine (cysteine
CC sulfinic acid) as substrate {ECO:0000269|PubMed:26327310};
CC Vmax=1.41 umol/min/mg enzyme with L-aspartate as substrate
CC {ECO:0000269|PubMed:26327310};
CC Note=kcat is 3.6 sec(-1) with 3-sulfino-L-alanine (cysteine sulfinic
CC acid) as substrate. kcat 1.3 sec(-1) is with L-aspartate as
CC substrate. {ECO:0000269|PubMed:26327310};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:26327310,
CC ECO:0000269|PubMed:29372909}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80WP8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80WP8-2; Sequence=VSP_029752;
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscles and kidney (at
CC protein level). Expressed in skeletal muscle and weakly in brain. Not
CC expressed in liver or kidney. Expressed in brain, olfactory bulb,
CC liver, muscle and kidney with the highest expression in olfactory bulb
CC and almost not detected in liver (at protein level) (PubMed:26327310).
CC {ECO:0000269|PubMed:23038267, ECO:0000269|PubMed:26327310}.
CC -!- DEVELOPMENTAL STAGE: Expression in total brain lysate is weak but seems
CC to decrease with age as detected from 17 dpc to 12 months.
CC {ECO:0000269|PubMed:26327310}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; AC133169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC167467; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC052327; AAH52327.1; -; mRNA.
DR EMBL; AK003937; BAB23083.1; -; mRNA.
DR RefSeq; NP_082914.1; NM_028638.1.
DR PDB; 6ENZ; Other; 3.00 A; A/B=49-550.
DR PDBsum; 6ENZ; -.
DR AlphaFoldDB; Q80WP8; -.
DR SMR; Q80WP8; -.
DR BioGRID; 216228; 1.
DR IntAct; Q80WP8; 1.
DR STRING; 10090.ENSMUSP00000077694; -.
DR iPTMnet; Q80WP8; -.
DR PhosphoSitePlus; Q80WP8; -.
DR jPOST; Q80WP8; -.
DR PaxDb; Q80WP8; -.
DR PRIDE; Q80WP8; -.
DR ProteomicsDB; 273022; -. [Q80WP8-1]
DR ProteomicsDB; 273023; -. [Q80WP8-2]
DR GeneID; 73748; -.
DR KEGG; mmu:73748; -.
DR UCSC; uc009ryr.2; mouse. [Q80WP8-1]
DR CTD; 339896; -.
DR MGI; MGI:1920998; Gadl1.
DR eggNOG; KOG0629; Eukaryota.
DR InParanoid; Q80WP8; -.
DR OrthoDB; 810772at2759; -.
DR PhylomeDB; Q80WP8; -.
DR Reactome; R-MMU-1614558; Degradation of cysteine and homocysteine.
DR Reactome; R-MMU-8963693; Aspartate and asparagine metabolism.
DR BioGRID-ORCS; 73748; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Gadl1; mouse.
DR PRO; PR:Q80WP8; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q80WP8; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004068; F:aspartate 1-decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004782; F:sulfinoalanine decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR InterPro; IPR039025; GADL1.
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:SF1; PTHR45677:SF1; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Decarboxylase; Lyase;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..550
FT /note="Acidic amino acid decarboxylase GADL1"
FT /id="PRO_0000312225"
FT MOD_RES 362
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:29372909,
FT ECO:0007744|PDB:6ENZ"
FT VAR_SEQ 494..550
FT /note="VAPAIKEKMMKKGSLMLGYQPHRGKVNFFRQVVISPQVSREDMDFLLDEIDS
FT LGRDM -> RTVQFICRGFLLERNADSHFALRNWKTFPSVLA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029752"
FT CONFLICT 341
FT /note="R -> K (in Ref. 3; BAB23083)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 550 AA; 62519 MW; 7CEFEAC6428E65BF CRC64;
MSHARDDHQG ASQGSQWLSQ ARTLVQEGTL FNFIRCLLLF QGDSGQKEMT PGKKIPIFVD
GVVLNGPQTD VKAGEKFVEE ACRLIMEEVV LKATDVNEKV CEWQPPEQLR QLLDLEMRDT
GESQDKLLKL CQDVIHFSVK TNHPRFFNQL YAGLDYYSLA ARIITEALNP SIYTYEVSPV
FLLVEEAVLK KMIECVGWKE GDGIFNPGGS VSNMCAMNLA RYRHCPDIKE KGLSGLPRLI
LFTSAECHYS MKKAASFLGI GTQNVYFVET DGRGKMIPED LEKQIWQARQ EGAVPFLVCA
TSGTTVLGAF DPLDEIAEVC ERHGLWLHVD ASWGGSALVS RKHRRLLHGI HRADSVAWNP
HKMLMAGIQC SALLVKDKSD LLKKCYSAKA TYLFQQDKFY DVSYDTGDKS IQCSRRPDAF
KFWMTWKALG TSGLEERVNR AFALSRYLVD EIKKREGFKL LMEPEYTNVC FWYIPPSLRE
MEEGPEFWRK LSLVAPAIKE KMMKKGSLML GYQPHRGKVN FFRQVVISPQ VSREDMDFLL
DEIDSLGRDM
