PPCS_HUMAN
ID PPCS_HUMAN Reviewed; 311 AA.
AC Q9HAB8; Q3KQT2; Q5VVM0;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Phosphopantothenate--cysteine ligase;
DE EC=6.3.2.51 {ECO:0000269|PubMed:11923312, ECO:0000269|PubMed:29754768};
DE AltName: Full=Phosphopantothenoylcysteine synthetase;
DE Short=PPC synthetase;
GN Name=PPCS; Synonyms=COAB;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Ovary tumor, 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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
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 [5]
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP IDENTIFICATION BY 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 [9]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION, AND HOMODIMERIZATION.
RX PubMed=12906824; DOI=10.1016/s0969-2126(03)00146-1;
RA Manoj N., Strauss E., Begley T.P., Ealick S.E.;
RT "Structure of human phosphopantothenoylcysteine synthetase at 2.3 A
RT resolution.";
RL Structure 11:927-936(2003).
RN [10]
RP VARIANTS CMD2C 107-PRO--ALA-111 DEL; PRO-180 AND VAL-233, CHARACTERIZATION
RP OF VARIANTS CMD2C 107-PRO--ALA-111 DEL; PRO-180 AND VAL-233, INVOLVEMENT IN
RP CMD2C, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND HOMODIMERIZATION.
RX PubMed=29754768; DOI=10.1016/j.ajhg.2018.03.022;
RA Iuso A., Wiersma M., Schueller H.J., Pode-Shakked B., Marek-Yagel D.,
RA Grigat M., Schwarzmayr T., Berutti R., Alhaddad B., Kanon B.,
RA Grzeschik N.A., Okun J.G., Perles Z., Salem Y., Barel O., Vardi A.,
RA Rubinshtein M., Tirosh T., Dubnov-Raz G., Messias A.C., Terrile C.,
RA Barshack I., Volkov A., Avivi C., Eyal E., Mastantuono E., Kumbar M.,
RA Abudi S., Braunisch M., Strom T.M., Meitinger T., Hoffmann G.F.,
RA Prokisch H., Haack T.B., Brundel B.J.J.M., Haas D., Sibon O.C.M.,
RA Anikster Y.;
RT "Mutations in PPCS, encoding phosphopantothenoylcysteine synthetase, cause
RT autosomal-recessive dilated cardiomyopathy.";
RL Am. J. Hum. Genet. 102:1018-1030(2018).
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 (PubMed:11923312,
CC PubMed:12906824, PubMed:29754768). Has a preference for ATP over CTP as
CC a cosubstrate (PubMed:11923312). {ECO:0000269|PubMed:11923312,
CC ECO:0000269|PubMed:12906824, ECO:0000269|PubMed:29754768}.
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:0000269|PubMed:11923312, ECO:0000269|PubMed:29754768};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25157;
CC Evidence={ECO:0000305|PubMed:11923312};
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:0000269|PubMed:11923312};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19398;
CC Evidence={ECO:0000305|PubMed:11923312};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 2/5. {ECO:0000269|PubMed:11923312,
CC ECO:0000269|PubMed:29754768}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12906824,
CC ECO:0000269|PubMed:29754768}.
CC -!- INTERACTION:
CC Q9HAB8; Q9HAB8: PPCS; NbExp=3; IntAct=EBI-2827176, EBI-2827176;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9HAB8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HAB8-2; Sequence=VSP_045796;
CC -!- DISEASE: Cardiomyopathy, dilated 2C (CMD2C) [MIM:618189]: A form of
CC dilated cardiomyopathy, a disorder characterized by ventricular
CC dilation and impaired systolic function, resulting in congestive heart
CC failure and arrhythmia. Patients are at risk of premature death. CMD2C
CC is an autosomal recessive form with variable severity and age of onset
CC ranging from 2 to 20 years. Death in infancy or early childhood may
CC occur in severely affected children. {ECO:0000269|PubMed:29754768}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the PPC synthetase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13931.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK021900; BAB13931.1; ALT_FRAME; mRNA.
DR EMBL; AL445669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012383; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC104938; AAI04939.1; -; mRNA.
DR EMBL; BC106064; AAI06065.1; -; mRNA.
DR EMBL; BC112015; AAI12016.1; -; mRNA.
DR CCDS; CCDS41311.1; -. [Q9HAB8-1]
DR CCDS; CCDS41312.1; -. [Q9HAB8-2]
DR RefSeq; NP_001070915.1; NM_001077447.2. [Q9HAB8-2]
DR RefSeq; NP_001274435.1; NM_001287506.1. [Q9HAB8-2]
DR RefSeq; NP_001274437.1; NM_001287508.1. [Q9HAB8-2]
DR RefSeq; NP_001274438.1; NM_001287509.1. [Q9HAB8-2]
DR RefSeq; NP_001274439.1; NM_001287510.1. [Q9HAB8-2]
DR RefSeq; NP_001274440.1; NM_001287511.1.
DR RefSeq; NP_078940.2; NM_024664.3. [Q9HAB8-1]
DR PDB; 1P9O; X-ray; 2.30 A; A/B=1-311.
DR PDB; 7EDZ; X-ray; 1.95 A; A/B/C/D=1-311.
DR PDBsum; 1P9O; -.
DR PDBsum; 7EDZ; -.
DR AlphaFoldDB; Q9HAB8; -.
DR SMR; Q9HAB8; -.
DR BioGRID; 122833; 52.
DR IntAct; Q9HAB8; 2.
DR STRING; 9606.ENSP00000361642; -.
DR GlyGen; Q9HAB8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9HAB8; -.
DR PhosphoSitePlus; Q9HAB8; -.
DR BioMuta; PPCS; -.
DR DMDM; 47117318; -.
DR EPD; Q9HAB8; -.
DR jPOST; Q9HAB8; -.
DR MassIVE; Q9HAB8; -.
DR MaxQB; Q9HAB8; -.
DR PaxDb; Q9HAB8; -.
DR PeptideAtlas; Q9HAB8; -.
DR PRIDE; Q9HAB8; -.
DR ProteomicsDB; 65473; -.
DR ProteomicsDB; 81390; -. [Q9HAB8-1]
DR TopDownProteomics; Q9HAB8-1; -. [Q9HAB8-1]
DR Antibodypedia; 32205; 90 antibodies from 23 providers.
DR DNASU; 79717; -.
DR Ensembl; ENST00000372561.4; ENSP00000361642.3; ENSG00000127125.9. [Q9HAB8-1]
DR Ensembl; ENST00000372562.1; ENSP00000361643.1; ENSG00000127125.9. [Q9HAB8-2]
DR GeneID; 79717; -.
DR KEGG; hsa:79717; -.
DR MANE-Select; ENST00000372561.4; ENSP00000361642.3; NM_024664.4; NP_078940.2.
DR UCSC; uc001chl.5; human. [Q9HAB8-1]
DR CTD; 79717; -.
DR DisGeNET; 79717; -.
DR GeneCards; PPCS; -.
DR HGNC; HGNC:25686; PPCS.
DR HPA; ENSG00000127125; Low tissue specificity.
DR MalaCards; PPCS; -.
DR MIM; 609853; gene.
DR MIM; 618189; phenotype.
DR neXtProt; NX_Q9HAB8; -.
DR OpenTargets; ENSG00000127125; -.
DR Orphanet; 154; Familial isolated dilated cardiomyopathy.
DR PharmGKB; PA142671158; -.
DR VEuPathDB; HostDB:ENSG00000127125; -.
DR eggNOG; KOG2728; Eukaryota.
DR GeneTree; ENSGT00950000182834; -.
DR HOGENOM; CLU_042326_3_0_1; -.
DR InParanoid; Q9HAB8; -.
DR OMA; WEVVFVT; -.
DR OrthoDB; 185685at2759; -.
DR PhylomeDB; Q9HAB8; -.
DR TreeFam; TF105615; -.
DR BioCyc; MetaCyc:HS13229-MON; -.
DR BRENDA; 6.3.2.51; 2681.
DR PathwayCommons; Q9HAB8; -.
DR Reactome; R-HSA-196783; Coenzyme A biosynthesis.
DR SignaLink; Q9HAB8; -.
DR UniPathway; UPA00241; UER00353.
DR BioGRID-ORCS; 79717; 97 hits in 1078 CRISPR screens.
DR EvolutionaryTrace; Q9HAB8; -.
DR GeneWiki; Phosphopantothenate%E2%80%94cysteine_ligase; -.
DR GenomeRNAi; 79717; -.
DR Pharos; Q9HAB8; Tbio.
DR PRO; PR:Q9HAB8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9HAB8; protein.
DR Bgee; ENSG00000127125; Expressed in right adrenal gland cortex and 195 other tissues.
DR ExpressionAtlas; Q9HAB8; baseline and differential.
DR Genevisible; Q9HAB8; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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; IPI:IntAct.
DR GO; GO:0004632; F:phosphopantothenate--cysteine ligase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IMP:UniProtKB.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IMP:UniProtKB.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IDA:UniProtKB.
DR GO; GO:0003015; P:heart process; IMP:UniProtKB.
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 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Cardiomyopathy; Disease variant; Ligase; Nucleotide-binding;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..311
FT /note="Phosphopantothenate--cysteine ligase"
FT /id="PRO_0000182040"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT VAR_SEQ 1..173
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045796"
FT VARIANT 107..111
FT /note="Missing (in CMD2C; decreased phosphopantothenate--
FT cysteine ligase activity; decreased protein abundance in
FT patient fibroblasts)"
FT /evidence="ECO:0000269|PubMed:29754768"
FT /id="VAR_081990"
FT VARIANT 180
FT /note="A -> P (in CMD2C; loss of phosphopantothenate--
FT cysteine ligase activity; decreased protein abundance in
FT patient fibroblasts; dbSNP:rs1557776329)"
FT /evidence="ECO:0000269|PubMed:29754768"
FT /id="VAR_081991"
FT VARIANT 233
FT /note="E -> V (in CMD2C; decreased phosphopantothenate--
FT cysteine ligase activity; decreased protein abundance in
FT patient fibroblasts; dbSNP:rs1557778277)"
FT /evidence="ECO:0000269|PubMed:29754768"
FT /id="VAR_081992"
FT HELIX 16..32
FT /evidence="ECO:0007829|PDB:7EDZ"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:7EDZ"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:7EDZ"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:7EDZ"
FT HELIX 64..75
FT /evidence="ECO:0007829|PDB:7EDZ"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:7EDZ"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:7EDZ"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:7EDZ"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:7EDZ"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:1P9O"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:7EDZ"
FT HELIX 128..141
FT /evidence="ECO:0007829|PDB:7EDZ"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:7EDZ"
FT HELIX 152..166
FT /evidence="ECO:0007829|PDB:7EDZ"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:7EDZ"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:7EDZ"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:7EDZ"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:7EDZ"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:7EDZ"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:1P9O"
FT HELIX 214..219
FT /evidence="ECO:0007829|PDB:7EDZ"
FT STRAND 225..234
FT /evidence="ECO:0007829|PDB:7EDZ"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:7EDZ"
FT HELIX 239..250
FT /evidence="ECO:0007829|PDB:7EDZ"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:7EDZ"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:7EDZ"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:7EDZ"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:7EDZ"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:7EDZ"
FT HELIX 282..286
FT /evidence="ECO:0007829|PDB:7EDZ"
FT HELIX 291..308
FT /evidence="ECO:0007829|PDB:7EDZ"
SQ SEQUENCE 311 AA; 34005 MW; D3B337D3250D7170 CRC64;
MAEMDPVAEF PQPPGAARWA EVMARFAARL GAQGRRVVLV TSGGTKVPLE ARPVRFLDNF
SSGRRGATSA EAFLAAGYGV LFLYRARSAF PYAHRFPPQT WLSALRPSGP ALSGLLSLEA
EENALPGFAE ALRSYQEAAA AGTFLAVEFT TLADYLHLLQ AAAQALNPLG PSAMFYLAAA
VSDFYVPVSE MPEHKIQSSG GPLQITMKMV PKLLSPLVKD WAPKAFIISF KLETDPAIVI
NRARKALEIY QHQVVVANIL ESRQSFVFIV TKDSETKLLL SEEEIEKGVE IEEKIVDNLQ
SRHTAFIGDR N
