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Protein

Cysteine sulfinic acid decarboxylase

Gene

Csad

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

3-sulfino-L-alanine = hypotaurine + CO2.

Cofactori

Pathwayi: taurine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes hypotaurine from L-cysteine.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Cysteine dioxygenase type 1 (Cdo1)
  2. Cysteine sulfinic acid decarboxylase (Csad)
This subpathway is part of the pathway taurine biosynthesis, which is itself part of Organosulfur biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes hypotaurine from L-cysteine, the pathway taurine biosynthesis and in Organosulfur biosynthesis.

GO - Molecular functioni

  • carboxy-lyase activity Source: MGI
  • pyridoxal phosphate binding Source: InterPro
  • sulfinoalanine decarboxylase activity Source: UniProtKB-EC

GO - Biological processi

  • L-cysteine catabolic process to taurine Source: MGI
  • taurine biosynthetic process Source: MGI
  • taurine metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi4.1.1.29. 3474.
UniPathwayiUPA00012; UER00538.

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine sulfinic acid decarboxylase (EC:4.1.1.29)
Alternative name(s):
Cysteine-sulfinate decarboxylase
Sulfinoalanine decarboxylase
Gene namesi
Name:Csad
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:2180098. Csad.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 493493Cysteine sulfinic acid decarboxylasePRO_0000147007Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei305 – 3051N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

EPDiQ9DBE0.
MaxQBiQ9DBE0.
PaxDbiQ9DBE0.
PeptideAtlasiQ9DBE0.
PRIDEiQ9DBE0.

PTM databases

iPTMnetiQ9DBE0.
PhosphoSiteiQ9DBE0.
SwissPalmiQ9DBE0.

Expressioni

Tissue specificityi

Expressed in kidney and liver not detected in lymphoid tissues and lung.1 Publication

Gene expression databases

BgeeiQ9DBE0.
CleanExiMM_CSAD.
GenevisibleiQ9DBE0. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ9DBE0. 2 interactions.
MINTiMINT-1869237.
STRINGi10090.ENSMUSP00000023805.

Structurei

3D structure databases

ProteinModelPortaliQ9DBE0.
SMRiQ9DBE0. Positions 7-493.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the group II decarboxylase family.Curated

Phylogenomic databases

eggNOGiKOG0629. Eukaryota.
COG0076. LUCA.
GeneTreeiENSGT00760000119205.
HOGENOMiHOG000005382.
HOVERGENiHBG004980.
InParanoidiQ9DBE0.
KOiK01594.
OMAiISNMYAV.
OrthoDBiEOG7H1JM3.
PhylomeDBiQ9DBE0.
TreeFamiTF314688.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR021115. Pyridoxal-P_BS.
[Graphical view]
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9DBE0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADSKPLRTL DGDPVAVEAL LQDVFGIVVD EAILKGTSAS EKVCEWKEPE
60 70 80 90 100
ELKQLLDLEL QSQGESREQI LERCRTVIHY SVKTGHPRFF NQLFSGLDPH
110 120 130 140 150
ALAGRIITES LNTSQYTYEI APVFVLMEEE VLKKLRALVG WNSGDGVFCP
160 170 180 190 200
GGSISNMYAM NLARFQRYPD CKQRGLRALP PLALFTSKEC HYSITKGAAF
210 220 230 240 250
LGLGTDSVRV VKADERGRMI PEDLERQIIL AEAEGSVPFL VSATSGTTVL
260 270 280 290 300
GAFDPLDAIA DVCQRHGLWF HVDAAWGGSV LLSRTHRHLL DGIQRADSVA
310 320 330 340 350
WNPHKLLAAG LQCSALLLRD TSNLLKRCHG SQASYLFQQD KFYDVALDTG
360 370 380 390 400
DKVVQCGRRV DCLKLWLMWK AQGGQGLERR IDQAFALTRY LVEEIKKREG
410 420 430 440 450
FELVMEPEFV NVCFWFVPPS LRGKKESPDY SQRLSQVAPV LKERMVKKGT
460 470 480 490
MMIGYQPHGT RANFFRMVVA NPILAQADID FLLGELELLG QDL
Length:493
Mass (Da):55,145
Last modified:June 1, 2001 - v1
Checksum:iBA92298DA0086A02
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti160 – 1601M → I in AAK60398 (PubMed:11997111).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY033912 mRNA. Translation: AAK60398.1.
AK005015 mRNA. Translation: BAB23747.1.
CCDSiCCDS27873.1.
RefSeqiNP_659191.1. NM_144942.4.
XP_006521062.1. XM_006520999.2.
XP_006521063.1. XM_006521000.2.
XP_006521064.1. XM_006521001.2.
XP_006521066.1. XM_006521003.2.
XP_006521067.1. XM_006521004.2.
XP_006521071.1. XM_006521008.2.
XP_011243941.1. XM_011245639.1.
XP_011243942.1. XM_011245640.1.
XP_011243943.1. XM_011245641.1.
UniGeneiMm.296382.

Genome annotation databases

EnsembliENSMUST00000023805; ENSMUSP00000023805; ENSMUSG00000023044.
GeneIDi246277.
KEGGimmu:246277.
UCSCiuc007xuu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY033912 mRNA. Translation: AAK60398.1.
AK005015 mRNA. Translation: BAB23747.1.
CCDSiCCDS27873.1.
RefSeqiNP_659191.1. NM_144942.4.
XP_006521062.1. XM_006520999.2.
XP_006521063.1. XM_006521000.2.
XP_006521064.1. XM_006521001.2.
XP_006521066.1. XM_006521003.2.
XP_006521067.1. XM_006521004.2.
XP_006521071.1. XM_006521008.2.
XP_011243941.1. XM_011245639.1.
XP_011243942.1. XM_011245640.1.
XP_011243943.1. XM_011245641.1.
UniGeneiMm.296382.

3D structure databases

ProteinModelPortaliQ9DBE0.
SMRiQ9DBE0. Positions 7-493.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9DBE0. 2 interactions.
MINTiMINT-1869237.
STRINGi10090.ENSMUSP00000023805.

PTM databases

iPTMnetiQ9DBE0.
PhosphoSiteiQ9DBE0.
SwissPalmiQ9DBE0.

Proteomic databases

EPDiQ9DBE0.
MaxQBiQ9DBE0.
PaxDbiQ9DBE0.
PeptideAtlasiQ9DBE0.
PRIDEiQ9DBE0.

Protocols and materials databases

DNASUi246277.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023805; ENSMUSP00000023805; ENSMUSG00000023044.
GeneIDi246277.
KEGGimmu:246277.
UCSCiuc007xuu.1. mouse.

Organism-specific databases

CTDi51380.
MGIiMGI:2180098. Csad.

Phylogenomic databases

eggNOGiKOG0629. Eukaryota.
COG0076. LUCA.
GeneTreeiENSGT00760000119205.
HOGENOMiHOG000005382.
HOVERGENiHBG004980.
InParanoidiQ9DBE0.
KOiK01594.
OMAiISNMYAV.
OrthoDBiEOG7H1JM3.
PhylomeDBiQ9DBE0.
TreeFamiTF314688.

Enzyme and pathway databases

UniPathwayiUPA00012; UER00538.
BRENDAi4.1.1.29. 3474.

Miscellaneous databases

PROiQ9DBE0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBE0.
CleanExiMM_CSAD.
GenevisibleiQ9DBE0. MM.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR002129. PyrdxlP-dep_de-COase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR021115. Pyridoxal-P_BS.
[Graphical view]
PfamiPF00282. Pyridoxal_deC. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00392. DDC_GAD_HDC_YDC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of murine cysteine sulfinic acid decarboxylase and its mRNA expression in murine tissues."
    Park E., Park S.Y., Wang C., Xu J., LaFauci G., Schuller-Levis G.
    Biochim. Biophys. Acta 1574:403-406(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Kidney, Liver, Lung, Pancreas and Spleen.

Entry informationi

Entry nameiCSAD_MOUSE
AccessioniPrimary (citable) accession number: Q9DBE0
Secondary accession number(s): Q8K566
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 13, 2002
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.