ID CSAD_HUMAN Reviewed; 493 AA. AC Q9Y600; A8K0U4; Q4QQH9; Q9UNJ5; Q9Y601; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 2. DT 27-MAR-2024, entry version 184. DE RecName: Full=Cysteine sulfinic acid decarboxylase; DE EC=4.1.1.29 {ECO:0000250|UniProtKB:Q9DBE0}; DE AltName: Full=Aspartate 1-decarboxylase {ECO:0000250|UniProtKB:Q9DBE0}; 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 Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3). RC TISSUE=Brain; RA Pritchard J.E., Ramsden D.B.; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Amygdala; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). 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 [5] RP TISSUE SPECIFICITY. 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 (1.6 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, RP AND COFACTOR. RG Structural genomics consortium (SGC); RT "The crystal structure of human cysteine sulfinic acid decarboxylase RT (CSAD)."; RL Submitted (AUG-2007) to the PDB data bank. 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 Evidence={ECO:0000269|Ref.6}; CC -!- PATHWAY: Organosulfur biosynthesis; taurine biosynthesis; hypotaurine CC from L-cysteine: step 2/2. CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.6}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=Long; CC IsoId=Q9Y600-1; Sequence=Displayed; CC Name=2; Synonyms=Short; CC IsoId=Q9Y600-2; Sequence=VSP_001307; CC Name=3; CC IsoId=Q9Y600-3; Sequence=VSP_039002; CC -!- TISSUE SPECIFICITY: Expressed in liver and brain. Also expressed in CC both astrocytes and neurons, but lower levels are expressed in CC astrocytes. {ECO:0000269|PubMed:26327310}. CC -!- SIMILARITY: Belongs to the group II decarboxylase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD32546.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH98278.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH98342.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH99717.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAI05919.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; 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; AF116546; AAD32544.1; -; mRNA. DR EMBL; AF116547; AAD32545.1; -; mRNA. DR EMBL; AF116548; AAD32546.1; ALT_INIT; mRNA. DR EMBL; AK289659; BAF82348.1; -; mRNA. DR EMBL; CH471054; EAW96670.1; -; Genomic_DNA. DR EMBL; BC098278; AAH98278.1; ALT_INIT; mRNA. DR EMBL; BC098342; AAH98342.1; ALT_INIT; mRNA. DR EMBL; BC099717; AAH99717.1; ALT_INIT; mRNA. DR EMBL; BC105918; AAI05919.1; ALT_INIT; mRNA. DR CCDS; CCDS58235.1; -. [Q9Y600-1] DR CCDS; CCDS8848.2; -. [Q9Y600-3] DR RefSeq; NP_001231634.1; NM_001244705.1. [Q9Y600-1] DR RefSeq; NP_057073.4; NM_015989.4. [Q9Y600-3] DR RefSeq; XP_011536748.1; XM_011538446.2. DR PDB; 2JIS; X-ray; 1.60 A; A/B=1-493. DR PDBsum; 2JIS; -. DR AlphaFoldDB; Q9Y600; -. DR SMR; Q9Y600; -. DR BioGRID; 119512; 18. DR IntAct; Q9Y600; 12. DR MINT; Q9Y600; -. DR STRING; 9606.ENSP00000267085; -. DR DrugBank; DB00151; Cysteine. DR DrugBank; DB00114; Pyridoxal phosphate. DR iPTMnet; Q9Y600; -. DR PhosphoSitePlus; Q9Y600; -. DR BioMuta; CSAD; -. DR DMDM; 116241317; -. DR MassIVE; Q9Y600; -. DR MaxQB; Q9Y600; -. DR PaxDb; 9606-ENSP00000267085; -. DR PeptideAtlas; Q9Y600; -. DR ProteomicsDB; 86557; -. [Q9Y600-1] DR ProteomicsDB; 86558; -. [Q9Y600-2] DR ProteomicsDB; 86559; -. [Q9Y600-3] DR Antibodypedia; 26909; 201 antibodies from 25 providers. DR DNASU; 51380; -. DR Ensembl; ENST00000267085.8; ENSP00000267085.3; ENSG00000139631.20. [Q9Y600-3] DR Ensembl; ENST00000379846.5; ENSP00000369175.1; ENSG00000139631.20. [Q9Y600-2] DR Ensembl; ENST00000444623.6; ENSP00000415485.1; ENSG00000139631.20. [Q9Y600-1] DR Ensembl; ENST00000453446.6; ENSP00000410648.2; ENSG00000139631.20. [Q9Y600-1] DR GeneID; 51380; -. DR KEGG; hsa:51380; -. DR MANE-Select; ENST00000444623.6; ENSP00000415485.1; NM_001244705.2; NP_001231634.1. DR UCSC; uc001sbz.4; human. [Q9Y600-1] DR AGR; HGNC:18966; -. DR CTD; 51380; -. DR DisGeNET; 51380; -. DR GeneCards; CSAD; -. DR HGNC; HGNC:18966; CSAD. DR HPA; ENSG00000139631; Low tissue specificity. DR MIM; 616569; gene. DR neXtProt; NX_Q9Y600; -. DR OpenTargets; ENSG00000139631; -. DR PharmGKB; PA38771; -. DR VEuPathDB; HostDB:ENSG00000139631; -. DR eggNOG; KOG0629; Eukaryota. DR GeneTree; ENSGT00940000158240; -. DR HOGENOM; CLU_011856_0_0_1; -. DR InParanoid; Q9Y600; -. DR OMA; CVDLHKW; -. DR OrthoDB; 888358at2759; -. DR PhylomeDB; Q9Y600; -. DR TreeFam; TF314688; -. DR BioCyc; MetaCyc:HS06642-MONOMER; -. DR BRENDA; 4.1.1.29; 2681. DR PathwayCommons; Q9Y600; -. DR Reactome; R-HSA-1614558; Degradation of cysteine and homocysteine. DR SignaLink; Q9Y600; -. DR SIGNOR; Q9Y600; -. DR UniPathway; UPA00012; UER00538. DR BioGRID-ORCS; 51380; 17 hits in 1159 CRISPR screens. DR ChiTaRS; CSAD; human. DR EvolutionaryTrace; Q9Y600; -. DR GenomeRNAi; 51380; -. DR Pharos; Q9Y600; Tbio. DR PRO; PR:Q9Y600; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q9Y600; Protein. DR Bgee; ENSG00000139631; Expressed in right uterine tube and 175 other cell types or tissues. DR ExpressionAtlas; Q9Y600; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0004068; F:aspartate 1-decarboxylase activity; IEA:UniProtKB-EC. 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; IBA:GO_Central. 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 PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1. DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1. DR Pfam; PF00282; Pyridoxal_deC; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR Genevisible; Q9Y600; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Decarboxylase; Lyase; KW Pyridoxal phosphate; Reference proteome. FT CHAIN 1..493 FT /note="Cysteine sulfinic acid decarboxylase" FT /id="PRO_0000147006" FT MOD_RES 305 FT /note="N6-(pyridoxal phosphate)lysine" FT VAR_SEQ 1 FT /note="M -> MSIPLKSSFLLSYLCTLPPALLSREILM (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1" FT /id="VSP_039002" FT VAR_SEQ 43..189 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1" FT /id="VSP_001307" FT CONFLICT 257 FT /note="E -> G (in Ref. 1; AAD32545)" FT /evidence="ECO:0000305" FT CONFLICT 377 FT /note="L -> P (in Ref. 1; AAD32546)" FT /evidence="ECO:0000305" FT CONFLICT 433 FT /note="R -> G (in Ref. 1; AAD32544)" FT /evidence="ECO:0000305" FT HELIX 14..31 FT /evidence="ECO:0007829|PDB:2JIS" FT TURN 32..34 FT /evidence="ECO:0007829|PDB:2JIS" FT HELIX 35..37 FT /evidence="ECO:0007829|PDB:2JIS" FT HELIX 49..56 FT /evidence="ECO:0007829|PDB:2JIS" FT HELIX 67..80 FT /evidence="ECO:0007829|PDB:2JIS" FT STRAND 89..93 FT /evidence="ECO:0007829|PDB:2JIS" FT HELIX 99..111 FT /evidence="ECO:0007829|PDB:2JIS" FT TURN 118..120 FT /evidence="ECO:0007829|PDB:2JIS" FT HELIX 122..139 FT /evidence="ECO:0007829|PDB:2JIS" FT STRAND 145..151 FT /evidence="ECO:0007829|PDB:2JIS" FT HELIX 152..167 FT /evidence="ECO:0007829|PDB:2JIS" FT HELIX 171..174 FT /evidence="ECO:0007829|PDB:2JIS" FT HELIX 176..178 FT /evidence="ECO:0007829|PDB:2JIS" FT STRAND 182..187 FT /evidence="ECO:0007829|PDB:2JIS" FT HELIX 193..200 FT /evidence="ECO:0007829|PDB:2JIS" FT HELIX 205..207 FT /evidence="ECO:0007829|PDB:2JIS" FT STRAND 208..211 FT /evidence="ECO:0007829|PDB:2JIS" FT HELIX 221..233 FT /evidence="ECO:0007829|PDB:2JIS" FT STRAND 237..246 FT /evidence="ECO:0007829|PDB:2JIS" FT TURN 248..250 FT /evidence="ECO:0007829|PDB:2JIS" FT HELIX 256..266 FT /evidence="ECO:0007829|PDB:2JIS" FT STRAND 269..274 FT /evidence="ECO:0007829|PDB:2JIS" FT HELIX 277..282 FT /evidence="ECO:0007829|PDB:2JIS" FT TURN 284..286 FT /evidence="ECO:0007829|PDB:2JIS" FT HELIX 287..290 FT /evidence="ECO:0007829|PDB:2JIS" FT HELIX 293..295 FT /evidence="ECO:0007829|PDB:2JIS" FT STRAND 297..301 FT /evidence="ECO:0007829|PDB:2JIS" FT STRAND 314..319 FT /evidence="ECO:0007829|PDB:2JIS" FT HELIX 324..329 FT /evidence="ECO:0007829|PDB:2JIS" FT HELIX 345..347 FT /evidence="ECO:0007829|PDB:2JIS" FT HELIX 350..352 FT /evidence="ECO:0007829|PDB:2JIS" FT HELIX 362..396 FT /evidence="ECO:0007829|PDB:2JIS" FT STRAND 401..405 FT /evidence="ECO:0007829|PDB:2JIS" FT STRAND 408..416 FT /evidence="ECO:0007829|PDB:2JIS" FT HELIX 419..421 FT /evidence="ECO:0007829|PDB:2JIS" FT HELIX 430..435 FT /evidence="ECO:0007829|PDB:2JIS" FT HELIX 437..448 FT /evidence="ECO:0007829|PDB:2JIS" FT STRAND 452..458 FT /evidence="ECO:0007829|PDB:2JIS" FT STRAND 461..468 FT /evidence="ECO:0007829|PDB:2JIS" FT HELIX 476..490 FT /evidence="ECO:0007829|PDB:2JIS" FT CONFLICT Q9Y600-3:9 FT /note="F -> S (in Ref. 4; AAH98342)" FT /evidence="ECO:0000305" SQ SEQUENCE 493 AA; 55023 MW; 09BA2028D942016E CRC64; MADSEALPSL AGDPVAVEAL LRAVFGVVVD EAIQKGTSVS QKVCEWKEPE ELKQLLDLEL RSQGESQKQI LERCRAVIRY SVKTGHPRFF NQLFSGLDPH ALAGRIITES LNTSQYTYEI APVFVLMEEE VLRKLRALVG WSSGDGIFCP GGSISNMYAV NLARYQRYPD CKQRGLRTLP PLALFTSKEC HYSIQKGAAF LGLGTDSVRV VKADERGKMV PEDLERQIGM AEAEGAVPFL VSATSGTTVL GAFDPLEAIA DVCQRHGLWL HVDAAWGGSV LLSQTHRHLL DGIQRADSVA WNPHKLLAAG LQCSALLLQD TSNLLKRCHG SQASYLFQQD KFYDVALDTG DKVVQCGRRV DCLKLWLMWK AQGDQGLERR IDQAFVLARY LVEEMKKREG FELVMEPEFV NVCFWFVPPS LRGKQESPDY HERLSKVAPV LKERMVKEGS MMIGYQPHGT RGNFFRVVVA NSALTCADMD FLLNELERLG QDL //