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 27-MAR-2024, entry version 182. 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}; 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; 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; 62. 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; 9606-ENSP00000361642; -. DR PeptideAtlas; Q9HAB8; -. DR ProteomicsDB; 65473; -. DR ProteomicsDB; 81390; -. [Q9HAB8-1] DR Pumba; Q9HAB8; -. DR TopDownProteomics; Q9HAB8-1; -. [Q9HAB8-1] DR Antibodypedia; 32205; 118 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 AGR; HGNC:25686; -. 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; LERYQHH; -. DR OrthoDB; 2917677at2759; -. DR PhylomeDB; Q9HAB8; -. DR TreeFam; TF105615; -. DR BioCyc; MetaCyc:HS13229-MONOMER; -. 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; 110 hits in 1159 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 197 other cell types or tissues. DR ExpressionAtlas; Q9HAB8; baseline and differential. 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; CoaB-like; 1. DR InterPro; IPR035929; CoaB-like_sf. DR InterPro; IPR007085; DNA/pantothenate-metab_flavo_C. DR PANTHER; PTHR12290; CORNICHON-RELATED; 1. DR PANTHER; PTHR12290:SF2; PHOSPHOPANTOTHENATE--CYSTEINE LIGASE; 1. DR Pfam; PF04127; DFP; 2. DR SUPFAM; SSF102645; CoaB-like; 1. DR Genevisible; Q9HAB8; HS. 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 FT phosphopantothenate--cysteine ligase activity; decreased FT protein abundance in patient fibroblasts)" FT /evidence="ECO:0000269|PubMed:29754768" FT /id="VAR_081990" FT VARIANT 180 FT /note="A -> P (in CMD2C; loss of FT phosphopantothenate--cysteine ligase activity; decreased FT protein abundance in patient fibroblasts; FT dbSNP:rs1557776329)" FT /evidence="ECO:0000269|PubMed:29754768" FT /id="VAR_081991" FT VARIANT 233 FT /note="E -> V (in CMD2C; decreased FT phosphopantothenate--cysteine ligase activity; decreased FT protein abundance in patient fibroblasts; FT 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 //