LOCUS       NP_001292911             563 aa            linear   ROD 08-MAY-2025
DEFINITION  bifunctional coenzyme A synthase isoform 1 precursor [Mus
            musculus].
ACCESSION   NP_001292911
VERSION     NP_001292911.1
DBSOURCE    REFSEQ: accession NM_001305982.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Cavestro,C., D'Amato,M., Colombo,M.N., Cascone,F., Moro,A.S.,
            Levi,S., Tiranti,V. and Di Meo,I.
  TITLE     CoA synthase plays a critical role in neurodevelopment and
            neurodegeneration
  JOURNAL   Front Cell Neurosci 18, 1458475 (2024)
   PUBMED   39301217
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 563)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 563)
  AUTHORS   Di Meo,I., Cavestro,C., Pedretti,S., Fu,T., Ligorio,S.,
            Manocchio,A., Lavermicocca,L., Santambrogio,P., Ripamonti,M.,
            Levi,S., Ayciriex,S., Mitro,N. and Tiranti,V.
  TITLE     Neuronal Ablation of CoA Synthase Causes Motor Deficits, Iron
            Dyshomeostasis, and Mitochondrial Dysfunctions in a CoPAN Mouse
            Model
  JOURNAL   Int J Mol Sci 21 (24), 9707 (2020)
   PUBMED   33352696
  REMARK    GeneRIF: Neuronal Ablation of CoA Synthase Causes Motor Deficits,
            Iron Dyshomeostasis, and Mitochondrial Dysfunctions in a CoPAN
            Mouse Model.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 563)
  AUTHORS   Zhyvoloup,A., Nemazanyy,I., Panasyuk,G., Valovka,T., Fenton,T.,
            Rebholz,H., Wang,M.L., Foxon,R., Lyzogubov,V., Usenko,V.,
            Kyyamova,R., Gorbenko,O., Matsuka,G., Filonenko,V. and Gout,I.T.
  TITLE     Subcellular localization and regulation of coenzyme A synthase
  JOURNAL   J Biol Chem 278 (50), 50316-50321 (2003)
   PUBMED   14514684
REFERENCE   5  (residues 1 to 563)
  AUTHORS   Aghajanian,S. and Worrall,D.M.
  TITLE     Identification and characterization of the gene encoding the human
            phosphopantetheine adenylyltransferase and dephospho-CoA kinase
            bifunctional enzyme (CoA synthase)
  JOURNAL   Biochem J 365 (Pt 1), 13-18 (2002)
   PUBMED   11994049
REFERENCE   6  (residues 1 to 563)
  AUTHORS   Zhyvoloup,A., Nemazanyy,I., Babich,A., Panasyuk,G., Pobigailo,N.,
            Vudmaska,M., Naidenov,V., Kukharenko,O., Palchevskii,S.,
            Savinska,L., Ovcharenko,G., Verdier,F., Valovka,T., Fenton,T.,
            Rebholz,H., Wang,M.L., Shepherd,P., Matsuka,G., Filonenko,V. and
            Gout,I.T.
  TITLE     Molecular cloning of CoA Synthase. The missing link in CoA
            biosynthesis
  JOURNAL   J Biol Chem 277 (25), 22107-22110 (2002)
   PUBMED   11980892
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX255926.10.
            
            Summary: This gene encodes the bifunctional protein coenzyme A
            (CoA) synthase which carries out the last two steps in the
            biosynthesis of CoA from pantothenic acid (vitamin B5). The
            phosphopantetheine adenylyltransferase domain of this protein
            catalyzes the conversion of phosphopantetheine into dephospho-CoA
            while its dephospho-CoA kinase domain completes the final step by
            phosphorylating dephospho-CoA to form CoA. [provided by RefSeq, Apr
            2015].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK159405.1, BC064753.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 64.17 cM"
     Protein         1..563
                     /product="bifunctional coenzyme A synthase isoform 1
                     precursor"
                     /EC_number="2.7.7.3"
                     /EC_number="2.7.1.24"
                     /note="bifunctional coenzyme A synthase;
                     4'-phosphopantetheine adenylyltransferase and
                     dephospho-CoA kinase; CoA synthase"
                     /calculated_mol_wt=60067
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1974
     Site            177
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13057; propagated from
                     UniProtKB/Swiss-Prot (Q9DBL7.2)"
     Region          179..357
                     /region_name="Phosphopantetheine adenylyltransferase"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9DBL7.2)"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13057; propagated from
                     UniProtKB/Swiss-Prot (Q9DBL7.2)"
     Region          192..338
                     /region_name="PPAT_CoAS"
                     /note="phosphopantetheine adenylyltransferase domain of
                     eukaryotic and archaeal bifunctional enzymes; cd02164"
                     /db_xref="CDD:173915"
     Site            order(197..198,226,286)
                     /site_type="active"
                     /db_xref="CDD:173915"
     Site            203..206
                     /site_type="other"
                     /note="(T/H)XGH motif"
                     /db_xref="CDD:173915"
     Region          359..535
                     /region_name="DPCK"
                     /note="Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24)
                     catalyzes the phosphorylation of dephosphocoenzyme A
                     (dCoA) to yield CoA, which is the final step in CoA
                     biosynthesis; cd02022"
                     /db_xref="CDD:238980"
     Site            order(363,388,444,471..472,517)
                     /site_type="other"
                     /note="CoA-binding site [chemical binding]"
                     /db_xref="CDD:238980"
     Site            order(364..366,369..370,498,533)
                     /site_type="other"
                     /note="ATP-binding [chemical binding]"
                     /db_xref="CDD:238980"
     CDS             1..563
                     /gene="Coasy"
                     /gene_synonym="1300003G02Rik; Dpck; Ppat; Ukr1"
                     /coded_by="NM_001305982.2:88..1779"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS25446.1"
                     /db_xref="GeneID:71743"
                     /db_xref="MGI:MGI:1918993"
ORIGIN      
        1 mavfrsgllv lttplatlaa rlppiltsas rlvnhtlyvh lqpgmnlggp aqpqaspvqa
       61 tfevldfith lytgadlhrh ldvrilltni qtkstflpvl ssvqnlahpp evvltdfqtl
      121 dgsqynpvkq qleryatscy scspqlasvl lypdygtgel pleppnallp stirpaspva
      181 rsprqpvrgy hrgavggtfd rlhnahkvll svacvlaqeq lvvgvadkdl lkskllpell
      241 qpyaervehl teflvdikps ltfelvplld pygpagsdpt leflvvseet yrggmavnrf
      301 rlengkeela lyqiqllkdq shneneedkv ssssfrqril gnllqppner pelpsglyvl
      361 gltgisgsgk ssvaqrlknl gayiidsdhl ghrayapggp ayqpvveafg tdilhkdgti
      421 nrkvlgsrvf gnkkqmkilt divwpviakl areemdvava kgktlcvida amlleagwqs
      481 mvhevwtvvi peteavrriv erdglseaaa qsrlqsqmsg qqlveqsnvv lstlweshvt
      541 qsqvekawnl lqkrlpkayq trn
//
