CSAD_MOUSE
ID CSAD_MOUSE Reviewed; 493 AA.
AC Q9DBE0; Q8K566;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Cysteine sulfinic acid decarboxylase {ECO:0000303|PubMed:11997111};
DE EC=4.1.1.29 {ECO:0000269|PubMed:26327310};
DE AltName: Full=Aspartate 1-decarboxylase {ECO:0000305|PubMed:26327310};
DE EC=4.1.1.11 {ECO:0000269|PubMed:26327310};
DE AltName: Full=Cysteine-sulfinate decarboxylase;
DE AltName: Full=Sulfinoalanine decarboxylase;
GN Name=Csad {ECO:0000303|PubMed:26327310};
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 [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11997111; DOI=10.1016/s0167-4781(01)00364-5;
RA Park E., Park S.Y., Wang C., Xu J., LaFauci G., Schuller-Levis G.;
RT "Cloning of murine cysteine sulfinic acid decarboxylase and its mRNA
RT expression in murine tissues.";
RL Biochim. Biophys. Acta 1574:403-406(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Pancreas, and Spleen;
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 [4]
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).
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 3-
CC sulfino-L-alanine. 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:0000250};
CC -!- ACTIVITY REGULATION: Activated by Mn(2+). Inhibited by bis-
CC carboxymethyl-trithiocarbonate, ethylxanthogenacetic acid and 2,5-
CC disulfoaniline. Not affected by Li(+) within 0.05-40 mM concentration
CC range. {ECO:0000269|PubMed:26327310}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.20 mM for 3-sulfino-L-alanine (cysteine sulfinic acid)
CC {ECO:0000269|PubMed:26327310};
CC KM=93 mM for L-aspartate {ECO:0000269|PubMed:26327310};
CC Vmax=7.22 umol/min/mg enzyme with 3-sulfino-L-alanine (cysteine
CC sulfinic acid) as substrate {ECO:0000269|PubMed:26327310};
CC Vmax=0.16 umol/min/mg enzyme with L-aspartate as substrate
CC {ECO:0000269|PubMed:26327310};
CC Note=kcat is 6.6 sec(-1) with 3-sulfino-L-alanine (cysteine sulfinic
CC acid) as substrate. kcat is 0.14 sec(-1) with L-aspartate as
CC substrate. {ECO:0000269|PubMed:26327310};
CC -!- PATHWAY: Organosulfur biosynthesis; taurine biosynthesis; hypotaurine
CC from L-cysteine: step 2/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:26327310}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney and liver not detected in
CC lymphoid tissues and lung. Expressed in kidney, liver and brain. 7 and
CC 4 times higher expression in kidney and liver than in brain,
CC respectively. Low level of detection in skeletal muscle. Expressed in
CC brain, olfactory bulb, liver, skeletal muscle and kidney with the
CC highest expression in liver and lowest in skeletal muscle (at protein
CC level) (PubMed:26327310). {ECO:0000269|PubMed:11997111,
CC ECO:0000269|PubMed:26327310}.
CC -!- DEVELOPMENTAL STAGE: Expression in the brain decreases with age as
CC detected from 17 dpc to 12 months. {ECO:0000269|PubMed:26327310}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; AY033912; AAK60398.1; -; mRNA.
DR EMBL; AK005015; BAB23747.1; -; mRNA.
DR CCDS; CCDS27873.1; -.
DR RefSeq; NP_659191.1; NM_144942.4.
DR RefSeq; XP_006521062.1; XM_006520999.3.
DR PDB; 6ZEK; X-ray; 2.10 A; A/B/C/D=1-493.
DR PDB; 7A0A; X-ray; 2.80 A; A/B/C/D=1-493.
DR PDBsum; 6ZEK; -.
DR PDBsum; 7A0A; -.
DR AlphaFoldDB; Q9DBE0; -.
DR SASBDB; Q9DBE0; -.
DR SMR; Q9DBE0; -.
DR BioGRID; 232920; 2.
DR STRING; 10090.ENSMUSP00000023805; -.
DR iPTMnet; Q9DBE0; -.
DR PhosphoSitePlus; Q9DBE0; -.
DR SwissPalm; Q9DBE0; -.
DR EPD; Q9DBE0; -.
DR jPOST; Q9DBE0; -.
DR MaxQB; Q9DBE0; -.
DR PaxDb; Q9DBE0; -.
DR PeptideAtlas; Q9DBE0; -.
DR PRIDE; Q9DBE0; -.
DR ProteomicsDB; 279068; -.
DR Antibodypedia; 26909; 185 antibodies from 25 providers.
DR DNASU; 246277; -.
DR Ensembl; ENSMUST00000023805; ENSMUSP00000023805; ENSMUSG00000023044.
DR GeneID; 246277; -.
DR KEGG; mmu:246277; -.
DR UCSC; uc007xuu.1; mouse.
DR CTD; 51380; -.
DR MGI; MGI:2180098; Csad.
DR VEuPathDB; HostDB:ENSMUSG00000023044; -.
DR eggNOG; KOG0629; Eukaryota.
DR GeneTree; ENSGT00940000158240; -.
DR HOGENOM; CLU_011856_0_0_1; -.
DR InParanoid; Q9DBE0; -.
DR OMA; PDCKQKG; -.
DR OrthoDB; 810772at2759; -.
DR PhylomeDB; Q9DBE0; -.
DR TreeFam; TF314688; -.
DR BRENDA; 4.1.1.29; 3474.
DR UniPathway; UPA00012; UER00538.
DR BioGRID-ORCS; 246277; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Csad; mouse.
DR PRO; PR:Q9DBE0; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9DBE0; protein.
DR Bgee; ENSMUSG00000023044; Expressed in right kidney and 257 other tissues.
DR ExpressionAtlas; Q9DBE0; baseline and differential.
DR Genevisible; Q9DBE0; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0019449; P:L-cysteine catabolic process to hypotaurine; ISS:UniProtKB.
DR GO; GO:0019452; P:L-cysteine catabolic process to taurine; ISS:UniProtKB.
DR GO; GO:0042412; P:taurine biosynthetic process; IMP:MGI.
DR GO; GO:0019530; P:taurine metabolic process; TAS:MGI.
DR Gene3D; 3.40.640.10; -; 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 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; Decarboxylase; Lyase; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..493
FT /note="Cysteine sulfinic acid decarboxylase"
FT /id="PRO_0000147007"
FT MOD_RES 305
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 160
FT /note="M -> I (in Ref. 1; AAK60398)"
FT /evidence="ECO:0000305"
FT HELIX 14..31
FT /evidence="ECO:0007829|PDB:6ZEK"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:6ZEK"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:6ZEK"
FT HELIX 49..56
FT /evidence="ECO:0007829|PDB:6ZEK"
FT HELIX 67..80
FT /evidence="ECO:0007829|PDB:6ZEK"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:6ZEK"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:6ZEK"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:6ZEK"
FT HELIX 122..139
FT /evidence="ECO:0007829|PDB:6ZEK"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:6ZEK"
FT HELIX 152..167
FT /evidence="ECO:0007829|PDB:6ZEK"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:6ZEK"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:6ZEK"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:6ZEK"
FT HELIX 193..200
FT /evidence="ECO:0007829|PDB:6ZEK"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:6ZEK"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:6ZEK"
FT HELIX 221..233
FT /evidence="ECO:0007829|PDB:6ZEK"
FT STRAND 237..246
FT /evidence="ECO:0007829|PDB:6ZEK"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:6ZEK"
FT HELIX 256..266
FT /evidence="ECO:0007829|PDB:6ZEK"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:6ZEK"
FT HELIX 277..282
FT /evidence="ECO:0007829|PDB:6ZEK"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:6ZEK"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:6ZEK"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:6ZEK"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:6ZEK"
FT TURN 303..306
FT /evidence="ECO:0007829|PDB:7A0A"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:6ZEK"
FT HELIX 324..329
FT /evidence="ECO:0007829|PDB:6ZEK"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:6ZEK"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:6ZEK"
FT HELIX 362..397
FT /evidence="ECO:0007829|PDB:6ZEK"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:6ZEK"
FT STRAND 408..416
FT /evidence="ECO:0007829|PDB:6ZEK"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:6ZEK"
FT HELIX 430..434
FT /evidence="ECO:0007829|PDB:6ZEK"
FT HELIX 437..448
FT /evidence="ECO:0007829|PDB:6ZEK"
FT STRAND 452..456
FT /evidence="ECO:0007829|PDB:6ZEK"
FT STRAND 464..468
FT /evidence="ECO:0007829|PDB:6ZEK"
FT HELIX 476..490
FT /evidence="ECO:0007829|PDB:6ZEK"
SQ SEQUENCE 493 AA; 55145 MW; BA92298DA0086A02 CRC64;
MADSKPLRTL DGDPVAVEAL LQDVFGIVVD EAILKGTSAS EKVCEWKEPE ELKQLLDLEL
QSQGESREQI LERCRTVIHY SVKTGHPRFF NQLFSGLDPH ALAGRIITES LNTSQYTYEI
APVFVLMEEE VLKKLRALVG WNSGDGVFCP GGSISNMYAM NLARFQRYPD CKQRGLRALP
PLALFTSKEC HYSITKGAAF LGLGTDSVRV VKADERGRMI PEDLERQIIL AEAEGSVPFL
VSATSGTTVL GAFDPLDAIA DVCQRHGLWF HVDAAWGGSV LLSRTHRHLL DGIQRADSVA
WNPHKLLAAG LQCSALLLRD TSNLLKRCHG SQASYLFQQD KFYDVALDTG DKVVQCGRRV
DCLKLWLMWK AQGGQGLERR IDQAFALTRY LVEEIKKREG FELVMEPEFV NVCFWFVPPS
LRGKKESPDY SQRLSQVAPV LKERMVKKGT MMIGYQPHGT RANFFRMVVA NPILAQADID
FLLGELELLG QDL
