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Protein

ATP-dependent Clp protease proteolytic subunit, mitochondrial

Gene

Clpp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Protease component of the Clp complex that cleaves peptides and various proteins in an ATP-dependent process. Has low peptidase activity in the absence of CLPX. The Clp complex can degrade CSN1S1, CSN2 and CSN3, as well as synthetic peptides (in vitro) and may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates (By similarity).By similarity

Catalytic activityi

Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei149 – 1491NucleophileBy similarity
Active sitei174 – 1741By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BRENDAi3.4.21.92. 3474.

Protein family/group databases

MEROPSiS14.003.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent Clp protease proteolytic subunit, mitochondrial (EC:3.4.21.92)
Alternative name(s):
Endopeptidase Clp
Gene namesi
Name:Clpp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1858213. Clpp.

Subcellular locationi

GO - Cellular componenti

  • endopeptidase Clp complex Source: UniProtKB
  • mitochondrial matrix Source: UniProtKB
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Disruption phenotypei

Homozygous pups are born at about 60 % of the expected Mendelian rate, indicating decreased intrauterine survival. Mutant mice are smaller in size than wild-type littermates, show decreased motor activity, are completely deaf after 12 months and their lifespan is decreased relative to that of wild-type littermates. Both female and male mutant mice are completely infertile due to defects in germ cell development.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5252MitochondrionBy similarityAdd
BLAST
Chaini53 – 272220ATP-dependent Clp protease proteolytic subunit, mitochondrialPRO_0000005517Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei196 – 1961N6-succinyllysineCombined sources
Modified residuei207 – 2071N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiO88696.
MaxQBiO88696.
PaxDbiO88696.
PRIDEiO88696.

2D gel databases

REPRODUCTION-2DPAGEIPI00133270.
O88696.

PTM databases

iPTMnetiO88696.
PhosphoSiteiO88696.

Expressioni

Tissue specificityi

Detected in liver (at protein level). High levels found in heart, liver and skeletal muscle.2 Publications

Gene expression databases

BgeeiO88696.
GenevisibleiO88696. MM.

Interactioni

Subunit structurei

Fourteen CLPP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity. Component of the Clp complex formed by the assembly of two CLPP heptameric rings with two CLPX hexameric rings, giving rise to a symmetrical structure with two central CLPP rings flanked by a CLPX ring at either end of the complex.1 Publication

Protein-protein interaction databases

BioGridi207517. 1 interaction.
IntActiO88696. 3 interactions.
MINTiMINT-1850742.
STRINGi10090.ENSMUSP00000002735.

Structurei

3D structure databases

ProteinModelPortaliO88696.
SMRiO88696. Positions 53-248.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S14 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0840. Eukaryota.
COG0740. LUCA.
GeneTreeiENSGT00390000005830.
HOGENOMiHOG000285833.
HOVERGENiHBG001689.
InParanoidiO88696.
KOiK01358.
OMAiARMNELM.
OrthoDBiEOG77WWD5.
PhylomeDBiO88696.
TreeFamiTF105002.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
HAMAPiMF_00444. ClpP.
InterProiIPR001907. ClpP.
IPR029045. ClpP/crotonase-like_dom.
IPR023562. ClpP/TepA.
IPR033135. ClpP_His_AS.
IPR018215. ClpP_Ser_AS.
[Graphical view]
PANTHERiPTHR10381. PTHR10381. 1 hit.
PfamiPF00574. CLP_protease. 1 hit.
[Graphical view]
PRINTSiPR00127. CLPPROTEASEP.
SUPFAMiSSF52096. SSF52096. 1 hit.
PROSITEiPS00382. CLP_PROTEASE_HIS. 1 hit.
PS00381. CLP_PROTEASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O88696-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWPRVLLGEA RVAVDGCRAL LSRLAVHFSP PWTAVSCSPL RRSLHGTATR
60 70 80 90 100
AFPLIPIVVE QTGRGERAYD IYSRLLRERI VCVMGPIDDS VASLVIAQLL
110 120 130 140 150
FLQSESNKKP IHMYINSPGG VVTAGLAIYD TMQYILNPIC TWCVGQAASM
160 170 180 190 200
GSLLLAAGSP GMRHSLPNSR IMIHQPSGGA RGQATDIAIQ AEEIMKLKKQ
210 220 230 240 250
LYNIYAKHTK QSLQVIESAM ERDRYMSPME AQEFGILDKV LVHPPQDGED
260 270
EPELVQKETA TAPTDPPAPT ST
Length:272
Mass (Da):29,800
Last modified:November 1, 1998 - v1
Checksum:i1F34C21E9C5C04D6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ005253 mRNA. Translation: CAA06443.1.
AJ012249
, AJ012250, AJ012251, AJ012252, AJ012253 Genomic DNA. Translation: CAA09966.1.
AK004024 mRNA. Translation: BAB23132.1.
AK145765 mRNA. Translation: BAE26636.1.
AK168053 mRNA. Translation: BAE40033.1.
BC001998 mRNA. Translation: AAH01998.1.
CCDSiCCDS28920.1.
RefSeqiNP_059089.1. NM_017393.2.
UniGeneiMm.287892.

Genome annotation databases

EnsembliENSMUST00000002735; ENSMUSP00000002735; ENSMUSG00000002660.
GeneIDi53895.
KEGGimmu:53895.
UCSCiuc008ddm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ005253 mRNA. Translation: CAA06443.1.
AJ012249
, AJ012250, AJ012251, AJ012252, AJ012253 Genomic DNA. Translation: CAA09966.1.
AK004024 mRNA. Translation: BAB23132.1.
AK145765 mRNA. Translation: BAE26636.1.
AK168053 mRNA. Translation: BAE40033.1.
BC001998 mRNA. Translation: AAH01998.1.
CCDSiCCDS28920.1.
RefSeqiNP_059089.1. NM_017393.2.
UniGeneiMm.287892.

3D structure databases

ProteinModelPortaliO88696.
SMRiO88696. Positions 53-248.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207517. 1 interaction.
IntActiO88696. 3 interactions.
MINTiMINT-1850742.
STRINGi10090.ENSMUSP00000002735.

Protein family/group databases

MEROPSiS14.003.

PTM databases

iPTMnetiO88696.
PhosphoSiteiO88696.

2D gel databases

REPRODUCTION-2DPAGEIPI00133270.
O88696.

Proteomic databases

EPDiO88696.
MaxQBiO88696.
PaxDbiO88696.
PRIDEiO88696.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000002735; ENSMUSP00000002735; ENSMUSG00000002660.
GeneIDi53895.
KEGGimmu:53895.
UCSCiuc008ddm.2. mouse.

Organism-specific databases

CTDi8192.
MGIiMGI:1858213. Clpp.

Phylogenomic databases

eggNOGiKOG0840. Eukaryota.
COG0740. LUCA.
GeneTreeiENSGT00390000005830.
HOGENOMiHOG000285833.
HOVERGENiHBG001689.
InParanoidiO88696.
KOiK01358.
OMAiARMNELM.
OrthoDBiEOG77WWD5.
PhylomeDBiO88696.
TreeFamiTF105002.

Enzyme and pathway databases

BRENDAi3.4.21.92. 3474.

Miscellaneous databases

PROiO88696.
SOURCEiSearch...

Gene expression databases

BgeeiO88696.
GenevisibleiO88696. MM.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
HAMAPiMF_00444. ClpP.
InterProiIPR001907. ClpP.
IPR029045. ClpP/crotonase-like_dom.
IPR023562. ClpP/TepA.
IPR033135. ClpP_His_AS.
IPR018215. ClpP_Ser_AS.
[Graphical view]
PANTHERiPTHR10381. PTHR10381. 1 hit.
PfamiPF00574. CLP_protease. 1 hit.
[Graphical view]
PRINTSiPR00127. CLPPROTEASEP.
SUPFAMiSSF52096. SSF52096. 1 hit.
PROSITEiPS00382. CLP_PROTEASE_HIS. 1 hit.
PS00381. CLP_PROTEASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: 129/SvJ and BALB/cJ.
    Tissue: Heart.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/cJ and C57BL/6J.
    Tissue: Embryo.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "Substrate recognition and processing by a Walker B mutant of the human mitochondrial AAA+ protein CLPX."
    Lowth B.R., Kirstein-Miles J., Saiyed T., Broetz-Oesterhelt H., Morimoto R.I., Truscott K.N., Dougan D.A.
    J. Struct. Biol. 179:193-201(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH CLPX, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. "Loss of mitochondrial peptidase Clpp leads to infertility, hearing loss plus growth retardation via accumulation of CLPX, mtDNA and inflammatory factors."
    Gispert S., Parganlija D., Klinkenberg M., Drose S., Wittig I., Mittelbronn M., Grzmil P., Koob S., Hamann A., Walter M., Buchel F., Adler T., Hrabe de Angelis M., Busch D.H., Zell A., Reichert A.S., Brandt U., Osiewacz H.D., Jendrach M., Auburger G.
    Hum. Mol. Genet. 22:4871-4887(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-196, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-207, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCLPP_MOUSE
AccessioniPrimary (citable) accession number: O88696
Secondary accession number(s): Q3TI13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: June 8, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.