CSAD_HUMAN
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 03-AUG-2022, entry version 175.
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};
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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. [Q9Y600-3]
DR PDB; 2JIS; X-ray; 1.60 A; A/B=1-493.
DR PDBsum; 2JIS; -.
DR AlphaFoldDB; Q9Y600; -.
DR SMR; Q9Y600; -.
DR BioGRID; 119512; 16.
DR IntAct; Q9Y600; 11.
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; Q9Y600; -.
DR PeptideAtlas; Q9Y600; -.
DR PRIDE; Q9Y600; -.
DR ProteomicsDB; 86557; -. [Q9Y600-1]
DR ProteomicsDB; 86558; -. [Q9Y600-2]
DR ProteomicsDB; 86559; -. [Q9Y600-3]
DR Antibodypedia; 26909; 185 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 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; PDCKQKG; -.
DR OrthoDB; 810772at2759; -.
DR PhylomeDB; Q9Y600; -.
DR TreeFam; TF314688; -.
DR BioCyc; MetaCyc:HS06642-MON; -.
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; 15 hits in 1079 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 173 other tissues.
DR ExpressionAtlas; Q9Y600; baseline and differential.
DR Genevisible; Q9Y600; HS.
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; IBA:GO_Central.
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 Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
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
