CLPP_HUMAN
ID CLPP_HUMAN Reviewed; 277 AA.
AC Q16740; B2R4W5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=ATP-dependent Clp protease proteolytic subunit, mitochondrial;
DE EC=3.4.21.92 {ECO:0000269|PubMed:11923310, ECO:0000269|PubMed:15522782, ECO:0000269|PubMed:22354088};
DE AltName: Full=Endopeptidase Clp;
DE Flags: Precursor;
GN Name=CLPP;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=8543061; DOI=10.1016/0014-5793(95)01353-9;
RA Bross P., Andresen B.S., Knudsen I., Kruse T.A., Gregersen N.;
RT "Human ClpP protease: cDNA sequence, tissue-specific expression and
RT chromosomal assignment of the gene.";
RL FEBS Lett. 377:249-252(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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 PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 57-69.
RC TISSUE=Leukemic T-cell;
RX PubMed=19892738; DOI=10.1073/pnas.0908958106;
RA Xu G., Shin S.B., Jaffrey S.R.;
RT "Global profiling of protease cleavage sites by chemoselective labeling of
RT protein N-termini.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
RN [5]
RP SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10525407; DOI=10.1006/jmbi.1999.3121;
RA de Sagarra M.R., Mayo I., Marco S., Rodriguez-Vilarino S., Oliva J.,
RA Carrascosa J.L., Castano J.G.;
RT "Mitochondrial localization and oligomeric structure of HClpP, the human
RT homologue of E. coli ClpP.";
RL J. Mol. Biol. 292:819-825(1999).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF SER-153, ACTIVE SITE,
RP AND ELECTRON MICROSCOPY.
RX PubMed=11923310; DOI=10.1074/jbc.m201642200;
RA Kang S.G., Ortega J., Singh S.K., Wang N., Huang N.N., Steven A.C.,
RA Maurizi M.R.;
RT "Functional proteolytic complexes of the human mitochondrial ATP-dependent
RT protease, hClpXP.";
RL J. Biol. Chem. 277:21095-21102(2002).
RN [7]
RP SUBUNIT, AND IDENTIFICATION IN A COMPLEX WITH CLPX.
RX PubMed=16115876; DOI=10.1074/jbc.m507240200;
RA Kang S.G., Dimitrova M.N., Ortega J., Ginsburg A., Maurizi M.R.;
RT "Human mitochondrial ClpP is a stable heptamer that assembles into a
RT tetradecamer in the presence of ClpX.";
RL J. Biol. Chem. 280:35424-35432(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-211, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
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 [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=22354088; DOI=10.1038/embor.2012.14;
RA Greene A.W., Grenier K., Aguileta M.A., Muise S., Farazifard R.,
RA Haque M.E., McBride H.M., Park D.S., Fon E.A.;
RT "Mitochondrial processing peptidase regulates PINK1 processing, import and
RT Parkin recruitment.";
RL EMBO Rep. 13:378-385(2012).
RN [12]
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 [13]
RP CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER LEU-56, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP SUBUNIT, INTERACTION WITH CLPX, AND MUTAGENESIS OF 58-LEU--ILE-61.
RX PubMed=15522782; DOI=10.1016/j.jsb.2004.07.004;
RA Kang S.G., Maurizi M.R., Thompson M., Mueser T., Ahvazi B.;
RT "Crystallography and mutagenesis point to an essential role for the N-
RT terminus of human mitochondrial ClpP.";
RL J. Struct. Biol. 148:338-352(2004).
RN [15]
RP VARIANTS PRLTS3 PRO-145 AND SER-147.
RX PubMed=23541340; DOI=10.1016/j.ajhg.2013.02.013;
RG University of Washington Center for Mendelian Genomics;
RA Jenkinson E.M., Rehman A.U., Walsh T., Clayton-Smith J., Lee K.,
RA Morell R.J., Drummond M.C., Khan S.N., Naeem M.A., Rauf B., Billington N.,
RA Schultz J.M., Urquhart J.E., Lee M.K., Berry A., Hanley N.A., Mehta S.,
RA Cilliers D., Clayton P.E., Kingston H., Smith M.J., Warner T.T.,
RA Black G.C., Trump D., Davis J.R., Ahmad W., Leal S.M., Riazuddin S.,
RA King M.C., Friedman T.B., Newman W.G.;
RT "Perrault syndrome is caused by recessive mutations in CLPP, encoding a
RT mitochondrial ATP-dependent chambered protease.";
RL Am. J. Hum. Genet. 92:605-613(2013).
RN [16]
RP VARIANT PRLTS3 ASP-229.
RX PubMed=25956234; DOI=10.1016/j.jns.2015.04.038;
RA Ahmed S., Jelani M., Alrayes N., Mohamoud H.S., Almramhi M.M., Anshasi W.,
RA Ahmed N.A., Wang J., Nasir J., Al-Aama J.Y.;
RT "Exome analysis identified a novel missense mutation in the CLPP gene in a
RT consanguineous Saudi family expanding the clinical spectrum of Perrault
RT Syndrome type-3.";
RL J. Neurol. Sci. 353:149-154(2015).
CC -!- FUNCTION: Protease component of the Clp complex that cleaves peptides
CC and various proteins in an ATP-dependent process. Has low peptidase
CC activity in the absence of CLPX. The Clp complex can degrade CSN1S1,
CC CSN2 and CSN3, as well as synthetic peptides (in vitro) and may be
CC responsible for a fairly general and central housekeeping function
CC rather than for the degradation of specific substrates
CC (PubMed:11923310, PubMed:15522782). Cleaves PINK1 in the mitochondrion
CC (PubMed:22354088). {ECO:0000269|PubMed:11923310,
CC ECO:0000269|PubMed:15522782, ECO:0000269|PubMed:22354088}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins to small peptides in the presence of
CC ATP and magnesium. alpha-casein is the usual test substrate. In the
CC absence of ATP, only oligopeptides shorter than five residues are
CC hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-
CC Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also
CC occurs).; EC=3.4.21.92; Evidence={ECO:0000269|PubMed:11923310,
CC ECO:0000269|PubMed:15522782, ECO:0000269|PubMed:22354088};
CC -!- SUBUNIT: Fourteen CLPP subunits assemble into 2 heptameric rings which
CC stack back to back to give a disk-like structure with a central cavity.
CC Component of the Clp complex formed by the assembly of two CLPP
CC heptameric rings with two CLPX hexameric rings, giving rise to a
CC symmetrical structure with two central CLPP rings flanked by a CLPX
CC ring at either end of the complex. {ECO:0000269|PubMed:10525407,
CC ECO:0000269|PubMed:11923310, ECO:0000269|PubMed:15522782,
CC ECO:0000269|PubMed:16115876}.
CC -!- INTERACTION:
CC Q16740; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-1056029, EBI-11096309;
CC Q16740; P05067: APP; NbExp=3; IntAct=EBI-1056029, EBI-77613;
CC Q16740; P54252: ATXN3; NbExp=3; IntAct=EBI-1056029, EBI-946046;
CC Q16740; Q9NWQ9: C14orf119; NbExp=3; IntAct=EBI-1056029, EBI-725606;
CC Q16740; P50570-2: DNM2; NbExp=3; IntAct=EBI-1056029, EBI-10968534;
CC Q16740; Q86UW9: DTX2; NbExp=5; IntAct=EBI-1056029, EBI-740376;
CC Q16740; Q12805: EFEMP1; NbExp=3; IntAct=EBI-1056029, EBI-536772;
CC Q16740; O95967: EFEMP2; NbExp=3; IntAct=EBI-1056029, EBI-743414;
CC Q16740; Q8TB36: GDAP1; NbExp=3; IntAct=EBI-1056029, EBI-11110431;
CC Q16740; P28799: GRN; NbExp=3; IntAct=EBI-1056029, EBI-747754;
CC Q16740; P42858: HTT; NbExp=6; IntAct=EBI-1056029, EBI-466029;
CC Q16740; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-1056029, EBI-1055254;
CC Q16740; P61970: NUTF2; NbExp=3; IntAct=EBI-1056029, EBI-591778;
CC Q16740; Q7Z4N8: P4HA3; NbExp=3; IntAct=EBI-1056029, EBI-10181968;
CC Q16740; Q9NRQ2: PLSCR4; NbExp=3; IntAct=EBI-1056029, EBI-769257;
CC Q16740; P67775: PPP2CA; NbExp=3; IntAct=EBI-1056029, EBI-712311;
CC Q16740; P20618: PSMB1; NbExp=3; IntAct=EBI-1056029, EBI-372273;
CC Q16740; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-1056029, EBI-740343;
CC Q16740; P37840: SNCA; NbExp=3; IntAct=EBI-1056029, EBI-985879;
CC Q16740; Q13148: TARDBP; NbExp=3; IntAct=EBI-1056029, EBI-372899;
CC Q16740; Q9Y5L0: TNPO3; NbExp=3; IntAct=EBI-1056029, EBI-1042571;
CC Q16740; O76024: WFS1; NbExp=3; IntAct=EBI-1056029, EBI-720609;
CC PRO_0000005516; O76031: CLPX; NbExp=2; IntAct=EBI-25815820, EBI-1052667;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:10525407, ECO:0000269|PubMed:22354088}.
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level). Predominantly
CC expressed in skeletal muscle. Intermediate levels in heart, liver and
CC pancreas. Low in brain, placenta, lung and kidney.
CC {ECO:0000269|PubMed:10525407, ECO:0000269|PubMed:8543061}.
CC -!- DISEASE: Perrault syndrome 3 (PRLTS3) [MIM:614129]: A sex-influenced
CC disorder characterized by sensorineural deafness in both males and
CC females, and ovarian dysgenesis in females. Affected females have
CC primary amenorrhea, streak gonads, and infertility, whereas affected
CC males show normal pubertal development and are fertile. A spectrum of
CC additional clinical features, including cerebellar ataxia, learning
CC disability, and peripheral neuropathy, have been described in some
CC PRLTS3 affected individuals. {ECO:0000269|PubMed:23541340,
CC ECO:0000269|PubMed:25956234}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000305}.
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DR EMBL; Z50853; CAA90705.1; -; mRNA.
DR EMBL; AK311973; BAG34912.1; -; mRNA.
DR EMBL; BC002956; AAH02956.1; -; mRNA.
DR CCDS; CCDS12162.1; -.
DR PIR; S68421; S68421.
DR RefSeq; NP_006003.1; NM_006012.2.
DR PDB; 1TG6; X-ray; 2.10 A; A/B/C/D/E/F/G=1-277.
DR PDB; 6BBA; X-ray; 2.80 A; A/B/C/D/E/F/G=58-277.
DR PDB; 6DL7; X-ray; 2.00 A; A/B/C/D/E/F/G=58-277.
DR PDB; 6H23; X-ray; 3.09 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=57-277.
DR PDBsum; 1TG6; -.
DR PDBsum; 6BBA; -.
DR PDBsum; 6DL7; -.
DR PDBsum; 6H23; -.
DR AlphaFoldDB; Q16740; -.
DR SMR; Q16740; -.
DR BioGRID; 113835; 345.
DR ComplexPortal; CPX-6177; Mitochondrial endopeptidase ClpXP complex.
DR CORUM; Q16740; -.
DR DIP; DIP-50384N; -.
DR IntAct; Q16740; 108.
DR MINT; Q16740; -.
DR STRING; 9606.ENSP00000245816; -.
DR BindingDB; Q16740; -.
DR ChEMBL; CHEMBL4523305; -.
DR DrugBank; DB04464; N-Formylmethionine.
DR MEROPS; S14.003; -.
DR iPTMnet; Q16740; -.
DR MetOSite; Q16740; -.
DR PhosphoSitePlus; Q16740; -.
DR BioMuta; CLPP; -.
DR DMDM; 3023512; -.
DR EPD; Q16740; -.
DR jPOST; Q16740; -.
DR MassIVE; Q16740; -.
DR MaxQB; Q16740; -.
DR PaxDb; Q16740; -.
DR PeptideAtlas; Q16740; -.
DR PRIDE; Q16740; -.
DR ProteomicsDB; 61051; -.
DR TopDownProteomics; Q16740; -.
DR Antibodypedia; 1703; 367 antibodies from 35 providers.
DR DNASU; 8192; -.
DR Ensembl; ENST00000245816.11; ENSP00000245816.3; ENSG00000125656.11.
DR GeneID; 8192; -.
DR KEGG; hsa:8192; -.
DR MANE-Select; ENST00000245816.11; ENSP00000245816.3; NM_006012.4; NP_006003.1.
DR UCSC; uc002mem.2; human.
DR CTD; 8192; -.
DR DisGeNET; 8192; -.
DR GeneCards; CLPP; -.
DR GeneReviews; CLPP; -.
DR HGNC; HGNC:2084; CLPP.
DR HPA; ENSG00000125656; Low tissue specificity.
DR MalaCards; CLPP; -.
DR MIM; 601119; gene.
DR MIM; 614129; phenotype.
DR neXtProt; NX_Q16740; -.
DR OpenTargets; ENSG00000125656; -.
DR Orphanet; 2855; Perrault syndrome.
DR PharmGKB; PA26610; -.
DR VEuPathDB; HostDB:ENSG00000125656; -.
DR eggNOG; KOG0840; Eukaryota.
DR GeneTree; ENSGT00390000005830; -.
DR InParanoid; Q16740; -.
DR OMA; RDYWMKA; -.
DR OrthoDB; 1274502at2759; -.
DR PhylomeDB; Q16740; -.
DR TreeFam; TF105002; -.
DR BRENDA; 3.4.21.92; 2681.
DR PathwayCommons; Q16740; -.
DR SignaLink; Q16740; -.
DR BioGRID-ORCS; 8192; 38 hits in 1076 CRISPR screens.
DR ChiTaRS; CLPP; human.
DR EvolutionaryTrace; Q16740; -.
DR GeneWiki; CLPP; -.
DR GenomeRNAi; 8192; -.
DR Pharos; Q16740; Tchem.
DR PRO; PR:Q16740; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q16740; protein.
DR Bgee; ENSG00000125656; Expressed in hindlimb stylopod muscle and 204 other tissues.
DR ExpressionAtlas; Q16740; baseline and differential.
DR Genevisible; Q16740; HS.
DR GO; GO:0009368; C:endopeptidase Clp complex; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IBA:GO_Central.
DR GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0008233; F:peptidase activity; TAS:ProtInc.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0033619; P:membrane protein proteolysis; IDA:UniProtKB.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IDA:ComplexPortal.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IDA:UniProtKB.
DR CDD; cd07017; S14_ClpP_2; 1.
DR HAMAP; MF_00444; ClpP; 1.
DR InterPro; IPR001907; ClpP.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR023562; ClpP/TepA.
DR InterPro; IPR033135; ClpP_His_AS.
DR InterPro; IPR018215; ClpP_Ser_AS.
DR PANTHER; PTHR10381; PTHR10381; 1.
DR Pfam; PF00574; CLP_protease; 1.
DR PRINTS; PR00127; CLPPROTEASEP.
DR SUPFAM; SSF52096; SSF52096; 1.
DR PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
DR PROSITE; PS00381; CLP_PROTEASE_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Deafness; Direct protein sequencing;
KW Disease variant; Hydrolase; Mitochondrion; Protease; Reference proteome;
KW Serine protease; Transit peptide.
FT TRANSIT 1..56
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:19892738,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 57..277
FT /note="ATP-dependent Clp protease proteolytic subunit,
FT mitochondrial"
FT /id="PRO_0000005516"
FT REGION 246..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 153
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:11923310"
FT ACT_SITE 178
FT /evidence="ECO:0000250"
FT MOD_RES 200
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O88696"
FT MOD_RES 211
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 145
FT /note="T -> P (in PRLTS3; dbSNP:rs398123033)"
FT /evidence="ECO:0000269|PubMed:23541340"
FT /id="VAR_070092"
FT VARIANT 147
FT /note="C -> S (in PRLTS3; dbSNP:rs398123034)"
FT /evidence="ECO:0000269|PubMed:23541340"
FT /id="VAR_070093"
FT VARIANT 229
FT /note="Y -> D (in PRLTS3)"
FT /evidence="ECO:0000269|PubMed:25956234"
FT /id="VAR_074160"
FT MUTAGEN 58..61
FT /note="Missing: Abolishes protease activity."
FT /evidence="ECO:0000269|PubMed:15522782"
FT MUTAGEN 153
FT /note="S->A,C: Abolishes protease activity."
FT /evidence="ECO:0000269|PubMed:11923310"
FT CONFLICT 111
FT /note="N -> S (in Ref. 2; BAG34912)"
FT /evidence="ECO:0000305"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:6BBA"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:6BBA"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:6BBA"
FT HELIX 75..81
FT /evidence="ECO:0007829|PDB:6DL7"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:6DL7"
FT HELIX 93..109
FT /evidence="ECO:0007829|PDB:6DL7"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:6DL7"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:6DL7"
FT HELIX 126..138
FT /evidence="ECO:0007829|PDB:6DL7"
FT STRAND 143..152
FT /evidence="ECO:0007829|PDB:6DL7"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:6DL7"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:6DL7"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:6DL7"
FT HELIX 195..213
FT /evidence="ECO:0007829|PDB:6DL7"
FT HELIX 217..225
FT /evidence="ECO:0007829|PDB:6DL7"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:1TG6"
FT HELIX 232..238
FT /evidence="ECO:0007829|PDB:6DL7"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:6DL7"
SQ SEQUENCE 277 AA; 30180 MW; B03AAC5D50F7880E CRC64;
MWPGILVGGA RVASCRYPAL GPRLAAHFPA QRPPQRTLQN GLALQRCLHA TATRALPLIP
IVVEQTGRGE RAYDIYSRLL RERIVCVMGP IDDSVASLVI AQLLFLQSES NKKPIHMYIN
SPGGVVTAGL AIYDTMQYIL NPICTWCVGQ AASMGSLLLA AGTPGMRHSL PNSRIMIHQP
SGGARGQATD IAIQAEEIMK LKKQLYNIYA KHTKQSLQVI ESAMERDRYM SPMEAQEFGI
LDKVLVHPPQ DGEDEPTLVQ KEPVEAAPAA EPVPAST
