COASY_HUMAN
ID COASY_HUMAN Reviewed; 564 AA.
AC Q13057; B2RA78; B4DLU0; Q6GS23; Q8NBM7; Q8NEW1; Q8WXD4; Q9NRM3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 4.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Bifunctional coenzyme A synthase {ECO:0000305};
DE Short=CoA synthase;
DE AltName: Full=NBP;
DE AltName: Full=POV-2;
DE Includes:
DE RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000305};
DE EC=2.7.7.3 {ECO:0000269|PubMed:24360804};
DE AltName: Full=Dephospho-CoA pyrophosphorylase;
DE AltName: Full=Pantetheine-phosphate adenylyltransferase;
DE Short=PPAT;
DE Includes:
DE RecName: Full=Dephospho-CoA kinase {ECO:0000305};
DE Short=DPCK;
DE EC=2.7.1.24 {ECO:0000269|PubMed:24360804};
DE AltName: Full=Dephosphocoenzyme A kinase;
DE Short=DPCOAK;
GN Name=COASY {ECO:0000312|HGNC:HGNC:29932}; ORFNames=PSEC0106;
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] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP VARIANT TYR-55.
RX PubMed=11923312; DOI=10.1074/jbc.m201708200;
RA Daugherty M., Polanuyer B., Farrell M., Scholle M., Lykidis A.,
RA de Crecy-Lagard V., Osterman A.;
RT "Complete reconstitution of the human coenzyme A biosynthetic pathway via
RT comparative genomics.";
RL J. Biol. Chem. 277:21431-21439(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBUNIT.
RX PubMed=11994049; DOI=10.1042/bj20020569;
RA Aghajanian S., Worrall D.M.;
RT "Identification and characterization of the gene encoding the human
RT phosphopantetheine adenylyltransferase and dephospho-CoA kinase
RT bifunctional enzyme (CoA synthase).";
RL Biochem. J. 365:13-18(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
RA Ota T., Nishikawa T., Suzuki Y., Kawai-Hio Y., Hayashi K., Ishii S.,
RA Saito K., Yamamoto J., Wakamatsu A., Nagai T., Nakamura Y., Nagahari K.,
RA Sugano S., Isogai T.;
RT "HRI human cDNA sequencing project.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP TYR-55.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT TYR-55.
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT TYR-55.
RC TISSUE=Colon, Muscle, and Uterus;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 165-564 (ISOFORMS 1/2).
RA Zhu Y.-B., Han Y.;
RT "Molecular cloning of a NBP gene cDNA.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 332-564 (ISOFORMS 1/2).
RC TISSUE=Ovary;
RX PubMed=8529999; DOI=10.1007/bf00197407;
RA Montagna M., Serova O., Sylla B.S., Feunteun J., Lenoir G.M.;
RT "A 100-kb physical and transcriptional map around the EDH17B2 gene:
RT identification of three novel genes and a pseudogene of a human homologue
RT of the rat PRL-1 tyrosine phosphatase.";
RL Hum. Genet. 96:532-538(1995).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 340-564 (ISOFORMS 1/2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP ALTERNATIVE SPLICING.
RX PubMed=16460672; DOI=10.1016/j.bbrc.2006.01.051;
RA Nemazanyy I., Panasyuk G., Breus O., Zhyvoloup A., Filonenko V., Gout I.T.;
RT "Identification of a novel CoA synthase isoform, which is primarily
RT expressed in the brain.";
RL Biochem. Biophys. Res. Commun. 341:995-1000(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178 AND SER-183, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, VARIANTS NBIA6
RP 59-GLN--ASP-564 DEL AND CYS-499, AND CHARACTERIZATION OF VARIANTS NBIA6
RP 59-GLN--ASP-564 DEL AND CYS-499.
RX PubMed=24360804; DOI=10.1016/j.ajhg.2013.11.008;
RA Dusi S., Valletta L., Haack T.B., Tsuchiya Y., Venco P., Pasqualato S.,
RA Goffrini P., Tigano M., Demchenko N., Wieland T., Schwarzmayr T.,
RA Strom T.M., Invernizzi F., Garavaglia B., Gregory A., Sanford L.,
RA Hamada J., Bettencourt C., Houlden H., Chiapparini L., Zorzi G.,
RA Kurian M.A., Nardocci N., Prokisch H., Hayflick S., Gout I., Tiranti V.;
RT "Exome sequence reveals mutations in CoA synthase as a cause of
RT neurodegeneration with brain iron accumulation.";
RL Am. J. Hum. Genet. 94:11-22(2014).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP INVOLVEMENT IN PCH12.
RX PubMed=30089828; DOI=10.1038/s41431-018-0233-0;
RA van Dijk T., Ferdinandusse S., Ruiter J.P.N., Alders M., Mathijssen I.B.,
RA Parboosingh J.S., Innes A.M., Meijers-Heijboer H., Poll-The B.T.,
RA Bernier F.P., Wanders R.J.A., Lamont R.E., Baas F.;
RT "Biallelic loss of function variants in COASY cause prenatal onset
RT pontocerebellar hypoplasia, microcephaly, and arthrogryposis.";
RL Eur. J. Hum. Genet. 26:1752-1758(2018).
RN [19]
RP VARIANTS NBIA6 VAL-214 AND CYS-499.
RX PubMed=28489334; DOI=10.1002/ajmg.a.38252;
RA Evers C., Seitz A., Assmann B., Opladen T., Karch S., Hinderhofer K.,
RA Granzow M., Paramasivam N., Eils R., Diessl N., Bartram C.R., Moog U.;
RT "Diagnosis of CoPAN by whole exome sequencing: Waking up a sleeping tiger's
RT eye.";
RL Am. J. Med. Genet. A 173:1878-1886(2017).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the fourth and fifth
CC sequential steps of CoA biosynthetic pathway. The fourth reaction is
CC catalyzed by the phosphopantetheine adenylyltransferase, coded by the
CC coaD domain; the fifth reaction is catalyzed by the dephospho-CoA
CC kinase, coded by the coaE domain. May act as a point of CoA
CC biosynthesis regulation. {ECO:0000269|PubMed:11923312,
CC ECO:0000269|PubMed:24360804}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA +
CC diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328,
CC ChEBI:CHEBI:61723; EC=2.7.7.3;
CC Evidence={ECO:0000269|PubMed:24360804};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19802;
CC Evidence={ECO:0000269|PubMed:24360804};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-dephospho-CoA + ATP = ADP + CoA + H(+);
CC Xref=Rhea:RHEA:18245, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57328, ChEBI:CHEBI:456216;
CC EC=2.7.1.24; Evidence={ECO:0000269|PubMed:24360804};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18246;
CC Evidence={ECO:0000269|PubMed:24360804};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.6 mM for 4'-phosphopantetheine;
CC KM=145 mM for ATP (in the PPAT reaction);
CC KM=16.7 mM for dephospho-CoA;
CC KM=34.4 mM for ATP (in the DPCK reaction);
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 4/5.
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 5/5. {ECO:0000269|PubMed:24360804}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11994049}.
CC -!- INTERACTION:
CC Q13057; Q6P2E9: EDC4; NbExp=3; IntAct=EBI-745967, EBI-1006038;
CC Q13057-2; Q8N137: CNTROB; NbExp=3; IntAct=EBI-10227704, EBI-947360;
CC Q13057-2; Q8N8K9: KIAA1958; NbExp=3; IntAct=EBI-10227704, EBI-10181113;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24360804}.
CC Mitochondrion matrix {ECO:0000269|PubMed:24360804}. Note=The protein is
CC mainly present in the mitochondrial matrix, probably anchored to the
CC inner mitochondrial membrane, but is also present in cell lysate.
CC {ECO:0000269|PubMed:24360804}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=CoASy alpha;
CC IsoId=Q13057-1; Sequence=Displayed;
CC Name=2; Synonyms=CoASy beta;
CC IsoId=Q13057-2; Sequence=VSP_036404;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined including brain,
CC heart, skeletal muscle, colon, thymus, spleen, kidney, liver, small
CC intestine, placenta, lung and peripheral blood leukocyte. Lowest
CC expression in peripheral blood leukocytes and highest in kidney and
CC liver. Isoform 2 is expressed mainly in the brain.
CC {ECO:0000269|PubMed:11923312}.
CC -!- DISEASE: Neurodegeneration with brain iron accumulation 6 (NBIA6)
CC [MIM:615643]: A neurodegenerative disorder associated with iron
CC accumulation in the brain, primarily in the basal ganglia. It is
CC characterized by progressive motor and cognitive dysfunction beginning
CC in childhood or young adulthood. Patients show extrapyramidal motor
CC signs, such as spasticity, dystonia, and parkinsonism.
CC {ECO:0000269|PubMed:24360804, ECO:0000269|PubMed:28489334}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Pontocerebellar hypoplasia 12 (PCH12) [MIM:618266]: A form of
CC pontocerebellar hypoplasia, a disorder characterized by structural
CC defects of the pons and cerebellum, evident upon brain imaging. PCH12
CC is an autosomal recessive form characterized by onset in utero and
CC death in infancy. Brain imaging shows microcephaly, cerebellar
CC hypoplasia, micrognathia, and multiple contractures.
CC {ECO:0000269|PubMed:30089828}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: In the central section; belongs to the eukaryotic CoaD
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA69699.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF87955.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH06354.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH20985.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AK075415; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF453478; AAL50813.1; -; mRNA.
DR EMBL; AY094602; AAM19996.1; -; mRNA.
DR EMBL; AK075415; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK297153; BAG59652.1; -; mRNA.
DR EMBL; AK314076; BAG36775.1; -; mRNA.
DR EMBL; AC067852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471152; EAW60840.1; -; Genomic_DNA.
DR EMBL; BC006354; AAH06354.1; ALT_INIT; mRNA.
DR EMBL; BC020985; AAH20985.1; ALT_INIT; mRNA.
DR EMBL; BC067254; AAH67254.1; -; mRNA.
DR EMBL; AF208536; AAF87955.1; ALT_INIT; mRNA.
DR EMBL; U18919; AAA69699.1; ALT_FRAME; mRNA.
DR EMBL; BT007168; AAP35832.1; -; mRNA.
DR CCDS; CCDS11429.1; -. [Q13057-1]
DR CCDS; CCDS45685.1; -. [Q13057-2]
DR RefSeq; NP_001035994.1; NM_001042529.2. [Q13057-1]
DR RefSeq; NP_001035997.2; NM_001042532.3. [Q13057-2]
DR RefSeq; NP_079509.5; NM_025233.6. [Q13057-1]
DR RefSeq; XP_006722179.1; XM_006722116.3. [Q13057-2]
DR RefSeq; XP_011523602.1; XM_011525300.1. [Q13057-1]
DR RefSeq; XP_016880657.1; XM_017025168.1.
DR AlphaFoldDB; Q13057; -.
DR BioGRID; 123254; 95.
DR IntAct; Q13057; 19.
DR MINT; Q13057; -.
DR STRING; 9606.ENSP00000464814; -.
DR BindingDB; Q13057; -.
DR ChEMBL; CHEMBL4105867; -.
DR iPTMnet; Q13057; -.
DR PhosphoSitePlus; Q13057; -.
DR BioMuta; COASY; -.
DR DMDM; 32363505; -.
DR EPD; Q13057; -.
DR jPOST; Q13057; -.
DR MassIVE; Q13057; -.
DR MaxQB; Q13057; -.
DR PaxDb; Q13057; -.
DR PeptideAtlas; Q13057; -.
DR PRIDE; Q13057; -.
DR ProteomicsDB; 59124; -. [Q13057-1]
DR ProteomicsDB; 59125; -. [Q13057-2]
DR Antibodypedia; 16973; 316 antibodies from 30 providers.
DR DNASU; 80347; -.
DR Ensembl; ENST00000393818.3; ENSP00000377406.1; ENSG00000068120.15. [Q13057-1]
DR Ensembl; ENST00000421097.6; ENSP00000393564.2; ENSG00000068120.15. [Q13057-1]
DR Ensembl; ENST00000590958.5; ENSP00000464814.1; ENSG00000068120.15. [Q13057-2]
DR GeneID; 80347; -.
DR KEGG; hsa:80347; -.
DR MANE-Select; ENST00000393818.3; ENSP00000377406.1; NM_025233.7; NP_079509.5.
DR UCSC; uc002hzz.5; human. [Q13057-1]
DR CTD; 80347; -.
DR DisGeNET; 80347; -.
DR GeneCards; COASY; -.
DR GeneReviews; COASY; -.
DR HGNC; HGNC:29932; COASY.
DR HPA; ENSG00000068120; Low tissue specificity.
DR MalaCards; COASY; -.
DR MIM; 609855; gene.
DR MIM; 615643; phenotype.
DR MIM; 618266; phenotype.
DR neXtProt; NX_Q13057; -.
DR OpenTargets; ENSG00000068120; -.
DR Orphanet; 397725; COASY protein-associated neurodegeneration.
DR PharmGKB; PA134867942; -.
DR VEuPathDB; HostDB:ENSG00000068120; -.
DR eggNOG; KOG3220; Eukaryota.
DR eggNOG; KOG3351; Eukaryota.
DR GeneTree; ENSGT00550000075078; -.
DR HOGENOM; CLU_027827_1_0_1; -.
DR InParanoid; Q13057; -.
DR OMA; VIDCDKV; -.
DR OrthoDB; 1543581at2759; -.
DR PhylomeDB; Q13057; -.
DR BioCyc; MetaCyc:HS00931-MON; -.
DR BRENDA; 2.7.1.24; 2681.
DR BRENDA; 2.7.7.3; 2681.
DR PathwayCommons; Q13057; -.
DR Reactome; R-HSA-196783; Coenzyme A biosynthesis.
DR SABIO-RK; Q13057; -.
DR SignaLink; Q13057; -.
DR UniPathway; UPA00241; UER00355.
DR UniPathway; UPA00241; UER00356.
DR BioGRID-ORCS; 80347; 409 hits in 1089 CRISPR screens.
DR ChiTaRS; COASY; human.
DR GeneWiki; COASY; -.
DR GenomeRNAi; 80347; -.
DR Pharos; Q13057; Tbio.
DR PRO; PR:Q13057; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q13057; protein.
DR Bgee; ENSG00000068120; Expressed in mucosa of transverse colon and 188 other tissues.
DR ExpressionAtlas; Q13057; baseline and differential.
DR Genevisible; Q13057; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004140; F:dephospho-CoA kinase activity; IDA:UniProtKB.
DR GO; GO:0004595; F:pantetheine-phosphate adenylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00376; Dephospho_CoA_kinase; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR001977; Depp_CoAkinase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF01121; CoaE; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00152; TIGR00152; 1.
DR PROSITE; PS51219; DPCK; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Coenzyme A biosynthesis; Cytoplasm;
KW Disease variant; Kinase; Mitochondrion; Multifunctional enzyme;
KW Neurodegeneration; Nucleotide-binding; Nucleotidyltransferase;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..564
FT /note="Bifunctional coenzyme A synthase"
FT /id="PRO_0000173039"
FT DOMAIN 360..563
FT /note="DPCK"
FT REGION 180..358
FT /note="Phosphopantetheine adenylyltransferase"
FT BINDING 365..372
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1
FT /note="M -> MRTPRLRAQPRGAVYQAPSPPPAPVGLGSM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036404"
FT VARIANT 55
FT /note="S -> Y (in dbSNP:rs615942)"
FT /evidence="ECO:0000269|PubMed:11923312,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.6"
FT /id="VAR_030299"
FT VARIANT 59..564
FT /note="Missing (in NBIA6; reduced protein abundance)"
FT /evidence="ECO:0000269|PubMed:24360804"
FT /id="VAR_082222"
FT VARIANT 214
FT /note="A -> V (in NBIA6; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28489334"
FT /id="VAR_082223"
FT VARIANT 499
FT /note="R -> C (in NBIA6; reduced protein abundance; loss of
FT dephospho-CoA kinase activity; dbSNP:rs140709867)"
FT /evidence="ECO:0000269|PubMed:24360804,
FT ECO:0000269|PubMed:28489334"
FT /id="VAR_070975"
FT CONFLICT 41
FT /note="L -> P (in Ref. 4; BAG36775)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 564 AA; 62329 MW; 7DC9E93B356C5DB7 CRC64;
MAVFRSGLLV LTTPLASLAP RLASILTSAA RLVNHTLYVH LQPGMSLEGP AQPQSSPVQA
TFEVLDFITH LYAGADVHRH LDVRILLTNI RTKSTFLPPL PTSVQNLAHP PEVVLTDFQT
LDGSQYNPVK QQLVRYATSC YSCCPRLASV LLYSDYGIGE VPVEPLDVPL PSTIRPASPV
AGSPKQPVRG YYRGAVGGTF DRLHNAHKVL LSVACILAQE QLVVGVADKD LLKSKLLPEL
LQPYTERVEH LSEFLVDIKP SLTFDVIPLL DPYGPAGSDP SLEFLVVSEE TYRGGMAINR
FRLENDLEEL ALYQIQLLKD LRHTENEEDK VSSSSFRQRM LGNLLRPPYE RPELPTCLYV
IGLTGISGSG KSSIAQRLKG LGAFVIDSDH LGHRAYAPGG PAYQPVVEAF GTDILHKDGI
INRKVLGSRV FGNKKQLKIL TDIMWPIIAK LAREEMDRAV AEGKRVCVID AAVLLEAGWQ
NLVHEVWTAV IPETEAVRRI VERDGLSEAA AQSRLQSQMS GQQLVEQSHV VLSTLWEPHI
TQRQVEKAWA LLQKRIPKTH QALD
