COAC_MOUSE
ID COAC_MOUSE Reviewed; 204 AA.
AC Q8BZB2;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Phosphopantothenoylcysteine decarboxylase;
DE Short=PPC-DC;
DE EC=4.1.1.36 {ECO:0000250|UniProtKB:Q96CD2};
DE AltName: Full=CoaC;
GN Name=Ppcdc; Synonyms=Coac;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Eye, and Lung;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Lung;
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).
CC -!- FUNCTION: Catalyzes the decarboxylation of the cysteine moiety of 4-
CC phosphopantothenoylcysteine to form 4'-phosphopantotheine and this
CC reaction forms part of the biosynthesis of coenzyme A.
CC {ECO:0000250|UniProtKB:Q96CD2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine = (R)-4'-
CC phosphopantetheine + CO2; Xref=Rhea:RHEA:16793, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:59458, ChEBI:CHEBI:61723; EC=4.1.1.36;
CC Evidence={ECO:0000250|UniProtKB:Q96CD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16794;
CC Evidence={ECO:0000250|UniProtKB:Q96CD2};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q96CD2};
CC Note=Binds 1 FMN per subunit. {ECO:0000250|UniProtKB:Q96CD2};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 3/5. {ECO:0000250|UniProtKB:Q96CD2}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q96CD2}.
CC -!- SIMILARITY: Belongs to the HFCD (homooligomeric flavin containing Cys
CC decarboxylase) superfamily. {ECO:0000305}.
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DR EMBL; AK036042; BAC29285.1; -; mRNA.
DR EMBL; BC052928; AAH52928.1; -; mRNA.
DR EMBL; BC089351; AAH89351.1; -; mRNA.
DR CCDS; CCDS23221.1; -.
DR RefSeq; NP_789801.1; NM_176831.4.
DR RefSeq; XP_006511423.1; XM_006511360.3.
DR RefSeq; XP_006511424.1; XM_006511361.3.
DR RefSeq; XP_006511425.1; XM_006511362.3.
DR RefSeq; XP_006511426.1; XM_006511363.3.
DR RefSeq; XP_011241091.1; XM_011242789.2.
DR RefSeq; XP_017169007.1; XM_017313518.1.
DR AlphaFoldDB; Q8BZB2; -.
DR SMR; Q8BZB2; -.
DR BioGRID; 211734; 3.
DR STRING; 10090.ENSMUSP00000082856; -.
DR iPTMnet; Q8BZB2; -.
DR PhosphoSitePlus; Q8BZB2; -.
DR SwissPalm; Q8BZB2; -.
DR EPD; Q8BZB2; -.
DR MaxQB; Q8BZB2; -.
DR PaxDb; Q8BZB2; -.
DR PeptideAtlas; Q8BZB2; -.
DR PRIDE; Q8BZB2; -.
DR ProteomicsDB; 285234; -.
DR Antibodypedia; 14730; 115 antibodies from 19 providers.
DR Ensembl; ENSMUST00000085709; ENSMUSP00000082856; ENSMUSG00000063849.
DR GeneID; 66812; -.
DR KEGG; mmu:66812; -.
DR UCSC; uc009put.1; mouse.
DR CTD; 60490; -.
DR MGI; MGI:1914062; Ppcdc.
DR VEuPathDB; HostDB:ENSMUSG00000063849; -.
DR eggNOG; KOG0672; Eukaryota.
DR GeneTree; ENSGT00440000038107; -.
DR HOGENOM; CLU_033319_3_2_1; -.
DR InParanoid; Q8BZB2; -.
DR OMA; NTRMYDH; -.
DR OrthoDB; 1225808at2759; -.
DR PhylomeDB; Q8BZB2; -.
DR TreeFam; TF315740; -.
DR BioCyc; MOUSE:MON3DJ-561; -.
DR Reactome; R-MMU-196783; Coenzyme A biosynthesis.
DR UniPathway; UPA00241; UER00354.
DR BioGRID-ORCS; 66812; 18 hits in 75 CRISPR screens.
DR ChiTaRS; Ppcdc; mouse.
DR PRO; PR:Q8BZB2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BZB2; protein.
DR Bgee; ENSMUSG00000063849; Expressed in granulocyte and 228 other tissues.
DR ExpressionAtlas; Q8BZB2; baseline and differential.
DR Genevisible; Q8BZB2; MM.
DR GO; GO:0071513; C:phosphopantothenoylcysteine decarboxylase complex; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0004633; F:phosphopantothenoylcysteine decarboxylase activity; ISS:UniProtKB.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; ISO:MGI.
DR Gene3D; 3.40.50.1950; -; 1.
DR InterPro; IPR036551; Flavin_trans-like.
DR InterPro; IPR003382; Flavoprotein.
DR Pfam; PF02441; Flavoprotein; 1.
DR SUPFAM; SSF52507; SSF52507; 1.
PE 1: Evidence at protein level;
KW Coenzyme A biosynthesis; Decarboxylase; Flavoprotein; FMN; Lyase;
KW Reference proteome.
FT CHAIN 1..204
FT /note="Phosphopantothenoylcysteine decarboxylase"
FT /id="PRO_0000182031"
FT ACT_SITE 173
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q96CD2"
FT BINDING 53
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q96CD2"
FT BINDING 104..107
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q96CD2"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 204 AA; 22344 MW; 8BA847F773F80ABC CRC64;
MEPKAPCPAA VPSEERKFRV LVGVTGSVAA LKLPLLVSKL LDVPGLEVTV VTTERAKHFY
SPQDVPVTLY SDADEWEMWK RRSDPVLHID LRRWADLMLV APLDANTLGK VASGICDNLL
TCVIRAWDLN KPLLFCPAMN TAMWEHPLTA QQVAQLKAFG YVEIPCVSKK LVCGDQGLGA
MAEVETIVAK VQAVLSQHGS IQQS
