PPCS_MOUSE
ID PPCS_MOUSE Reviewed; 311 AA.
AC Q8VDG5; Q3TVW0; Q9D376; Q9DA06;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Phosphopantothenate--cysteine ligase;
DE EC=6.3.2.51 {ECO:0000250|UniProtKB:Q9HAB8};
DE AltName: Full=Phosphopantothenoylcysteine synthetase;
DE Short=PPC synthetase;
GN Name=Ppcs; Synonyms=Coab;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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=Heart, Kidney, Liver, Spleen, and Testis;
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 second step in the biosynthesis of coenzyme A
CC from vitamin B5, where cysteine is conjugated to 4'-phosphopantothenate
CC to form 4-phosphopantothenoylcysteine. Has a preference for ATP over
CC CTP as a cosubstrate. {ECO:0000250|UniProtKB:Q9HAB8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-4'-phosphopantothenate + ATP + L-cysteine = AMP +
CC diphosphate + H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine;
CC Xref=Rhea:RHEA:25156, ChEBI:CHEBI:10986, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:59458, ChEBI:CHEBI:456215; EC=6.3.2.51;
CC Evidence={ECO:0000250|UniProtKB:Q9HAB8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25157;
CC Evidence={ECO:0000250|UniProtKB:Q9HAB8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-4'-phosphopantothenate + CTP + L-cysteine = CMP +
CC diphosphate + H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine;
CC Xref=Rhea:RHEA:19397, ChEBI:CHEBI:10986, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:35235, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:59458, ChEBI:CHEBI:60377;
CC Evidence={ECO:0000250|UniProtKB:Q9HAB8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19398;
CC Evidence={ECO:0000250|UniProtKB:Q9HAB8};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 2/5. {ECO:0000250|UniProtKB:Q9HAB8}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9HAB8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VDG5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VDG5-2; Sequence=VSP_010244;
CC -!- MISCELLANEOUS: The mammalian enzyme has a preference for ATP over CTP,
CC in contrast to the E.coli ortholog. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PPC synthetase family. {ECO:0000305}.
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DR EMBL; AK006290; BAB24509.1; -; mRNA.
DR EMBL; AK159952; BAE35508.1; -; mRNA.
DR EMBL; BC021894; AAH21894.1; -; mRNA.
DR CCDS; CCDS18581.1; -. [Q8VDG5-1]
DR CCDS; CCDS89823.1; -. [Q8VDG5-2]
DR RefSeq; NP_080770.2; NM_026494.3. [Q8VDG5-1]
DR RefSeq; XP_017175397.1; XM_017319908.1.
DR AlphaFoldDB; Q8VDG5; -.
DR SMR; Q8VDG5; -.
DR STRING; 10090.ENSMUSP00000030385; -.
DR iPTMnet; Q8VDG5; -.
DR PhosphoSitePlus; Q8VDG5; -.
DR REPRODUCTION-2DPAGE; IPI00135484; -.
DR EPD; Q8VDG5; -.
DR jPOST; Q8VDG5; -.
DR MaxQB; Q8VDG5; -.
DR PaxDb; Q8VDG5; -.
DR PeptideAtlas; Q8VDG5; -.
DR PRIDE; Q8VDG5; -.
DR ProteomicsDB; 291710; -. [Q8VDG5-1]
DR ProteomicsDB; 291711; -. [Q8VDG5-2]
DR Antibodypedia; 32205; 90 antibodies from 23 providers.
DR DNASU; 106564; -.
DR Ensembl; ENSMUST00000030385; ENSMUSP00000030385; ENSMUSG00000028636. [Q8VDG5-1]
DR Ensembl; ENSMUST00000106316; ENSMUSP00000101923; ENSMUSG00000028636. [Q8VDG5-2]
DR GeneID; 106564; -.
DR KEGG; mmu:106564; -.
DR UCSC; uc008uml.1; mouse. [Q8VDG5-2]
DR UCSC; uc008umm.1; mouse. [Q8VDG5-1]
DR CTD; 79717; -.
DR MGI; MGI:1915237; Ppcs.
DR VEuPathDB; HostDB:ENSMUSG00000028636; -.
DR eggNOG; KOG2728; Eukaryota.
DR GeneTree; ENSGT00950000182834; -.
DR HOGENOM; CLU_042326_2_0_1; -.
DR InParanoid; Q8VDG5; -.
DR OMA; WEVVFVT; -.
DR OrthoDB; 1292767at2759; -.
DR PhylomeDB; Q8VDG5; -.
DR TreeFam; TF105615; -.
DR Reactome; R-MMU-196783; Coenzyme A biosynthesis.
DR UniPathway; UPA00241; UER00353.
DR BioGRID-ORCS; 106564; 22 hits in 77 CRISPR screens.
DR PRO; PR:Q8VDG5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8VDG5; protein.
DR Bgee; ENSMUSG00000028636; Expressed in right kidney and 227 other tissues.
DR Genevisible; Q8VDG5; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004632; F:phosphopantothenate--cysteine ligase activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; ISO:MGI.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; ISO:MGI.
DR GO; GO:0003015; P:heart process; ISO:MGI.
DR Gene3D; 3.40.50.10300; -; 1.
DR InterPro; IPR035929; CoaB-like_sf.
DR InterPro; IPR007085; DNA/pantothenate-metab_flavo_C.
DR Pfam; PF04127; DFP; 2.
DR SUPFAM; SSF102645; SSF102645; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Ligase; Nucleotide-binding;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9HAB8"
FT CHAIN 2..311
FT /note="Phosphopantothenate--cysteine ligase"
FT /id="PRO_0000182041"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAB8"
FT VAR_SEQ 1..173
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010244"
SQ SEQUENCE 311 AA; 33794 MW; 082E03CB2E3A11E6 CRC64;
MAEMDLVAEL PRPAGAARWA EVMARFAARL GEQGRRVVLI TSGGTKVPLE ARAVRFLDNF
SSGRRGAASA EVFLAAGYGV LFLYRARSAF PYAHRFPPQA WLSALRPSGP AQSGKLSLEA
EENALPGFAA ALQSYQEAAA AGTFLAVEFT TLADYLHLLQ AAALALSPLG SSAMFYLAAA
VSDFYIPVSE MPEHKIHSSG GPLQITMKMV PKMLSPLVKD WAPKAFVVSF KLETDPDIII
SRARNALEVY QHQVVVANIL ESIKSFVIIV TKDSETELLL SEEEVAKGLV IEEKIVDDLR
SRHTAFICDK N
