CSAD_RAT
ID CSAD_RAT Reviewed; 493 AA.
AC Q64611; Q546T1; Q64577; Q9R1F6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Cysteine sulfinic acid decarboxylase;
DE EC=4.1.1.29 {ECO:0000250|UniProtKB:Q9DBE0};
DE AltName: Full=Aspartate 1-decarboxylase {ECO:0000305};
DE EC=4.1.1.11 {ECO:0000250|UniProtKB:Q9DBE0};
DE AltName: Full=Cysteine-sulfinate decarboxylase;
DE AltName: Full=Sulfinoalanine decarboxylase;
GN Name=Csad; Synonyms=Csd;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=7772604; DOI=10.1016/0167-4781(95)00058-o;
RA Kaisaki P.J., Jerkins A.A., Goodspeed D.C., Steele R.D.;
RT "Cloning and characterization of rat cysteine sulfinic acid
RT decarboxylase.";
RL Biochim. Biophys. Acta 1262:79-82(1995).
RN [2]
RP ERRATUM OF PUBMED:7772604.
RA Kaisaki P.J., Jerkins A.A., Goodspeed D.C., Steele R.D.;
RL Biochim. Biophys. Acta 1263:179-179(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8679699; DOI=10.1016/0167-4781(96)00068-1;
RA Reymond I., Sergeant A., Tappaz M.;
RT "Molecular cloning and sequence analysis of the cDNA encoding rat liver
RT cysteine sulfinate decarboxylase (CSD).";
RL Biochim. Biophys. Acta 1307:152-156(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=10461879; DOI=10.1046/j.1471-4159.1999.0730903.x;
RA Tappaz M., Bitoun M., Reymond I., Sergeant A.;
RT "Characterization of the cDNA coding for rat brain cysteine sulfinate
RT decarboxylase: brain and liver enzymes are identical proteins encoded by
RT two distinct mRNAs.";
RL J. Neurochem. 73:903-912(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-233.
RC STRAIN=Wistar;
RA Pritchard J.E., Ramsden D.B.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q9DBE0}.
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:0000250|UniProtKB:Q9DBE0};
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:0000250|UniProtKB:Q9DBE0};
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:0000250|UniProtKB:Q9DBE0};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- PATHWAY: Organosulfur biosynthesis; taurine biosynthesis; hypotaurine
CC from L-cysteine: step 2/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9DBE0}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, liver and kidney.
CC {ECO:0000269|PubMed:10461879}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; M64755; AAC42063.1; -; mRNA.
DR EMBL; X94152; CAA63868.1; -; mRNA.
DR EMBL; AJ132661; CAB54561.1; -; mRNA.
DR EMBL; BC081804; AAH81804.1; -; mRNA.
DR EMBL; AF115343; AAD47908.1; -; Genomic_DNA.
DR PIR; S71489; S71489.
DR RefSeq; NP_068518.1; NM_021750.2.
DR RefSeq; XP_006242500.1; XM_006242438.3.
DR RefSeq; XP_006242501.1; XM_006242439.2.
DR RefSeq; XP_006242502.1; XM_006242440.3.
DR RefSeq; XP_006242504.1; XM_006242442.3.
DR RefSeq; XP_008764004.1; XM_008765782.2.
DR RefSeq; XP_017450565.1; XM_017595076.1.
DR AlphaFoldDB; Q64611; -.
DR SMR; Q64611; -.
DR STRING; 10116.ENSRNOP00000016205; -.
DR iPTMnet; Q64611; -.
DR PhosphoSitePlus; Q64611; -.
DR PaxDb; Q64611; -.
DR PRIDE; Q64611; -.
DR Ensembl; ENSRNOT00000079678; ENSRNOP00000073508; ENSRNOG00000011573.
DR GeneID; 60356; -.
DR KEGG; rno:60356; -.
DR UCSC; RGD:621030; rat.
DR CTD; 51380; -.
DR RGD; 621030; Csad.
DR eggNOG; KOG0629; Eukaryota.
DR GeneTree; ENSGT00940000158240; -.
DR HOGENOM; CLU_011856_0_0_1; -.
DR InParanoid; Q64611; -.
DR OMA; PDCKQKG; -.
DR OrthoDB; 810772at2759; -.
DR PhylomeDB; Q64611; -.
DR TreeFam; TF314688; -.
DR BioCyc; MetaCyc:MON-13316; -.
DR UniPathway; UPA00012; UER00538.
DR PRO; PR:Q64611; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000011573; Expressed in liver and 19 other tissues.
DR ExpressionAtlas; Q64611; baseline and differential.
DR Genevisible; Q64611; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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; IDA:UniProtKB.
DR GO; GO:0019449; P:L-cysteine catabolic process to hypotaurine; IDA:UniProtKB.
DR GO; GO:0019452; P:L-cysteine catabolic process to taurine; IDA:UniProtKB.
DR GO; GO:0042412; P:taurine biosynthetic process; ISO:RGD.
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 Decarboxylase; Direct protein sequencing; Lyase; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..493
FT /note="Cysteine sulfinic acid decarboxylase"
FT /id="PRO_0000147008"
FT MOD_RES 305
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 178
FT /note="A -> V (in Ref. 1; AAC42063)"
FT /evidence="ECO:0000305"
FT CONFLICT 458..493
FT /note="HGTRANFFRMVVANPILVQADIDFLLGELERLGQDL -> MGPGPTSSEWWW
FT PTPYWSRPI (in Ref. 1; AAC42063)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 55249 MW; 31B7AA2F48CEC58C CRC64;
MADSKPLRTL DGDPVAVEAL LRDVFGIVVD EAIRKGTNAS EKVCEWKEPE ELKQLLDLEL
QSQGESRERI LERCRAVIHY SVKTGHPRFF NQLFSGLDPH ALAGRIITES LNTSQYTYEI
APVFVLMEEE VLKKLRALVG WNTGDGVFCP GGSISNMYAI NLARFQRYPD CKQRGLRALP
PLALFTSKEC HYSITKGAAF LGLGTDSVRV VKADERGKMI PEDLERQISL AEAEGSVPFL
VSATSGTTVL GAFDPLDAIA DVCQRHGLWL HVDAAWGGSV LLSRTHRHLL DGIQRADSVA
WNPHKLLAAG LQCSALLLRD TSNLLKRCHG SQASYLFQQD KFYNVALDTG DKVVQCGRRV
DCLKLWLMWK AQGGQGLEWR IDQAFALTRY LVEEIKKREG FELVMEPEFV NVCFWFVPPS
LRGKKESPDY SQRLSQVAPV LKERMVKKGT MMIGYQPHGT RANFFRMVVA NPILVQADID
FLLGELERLG QDL
