ID Q3UGW4_MOUSE Unreviewed; 269 AA. AC Q3UGW4; DT 11-OCT-2005, integrated into UniProtKB/TrEMBL. DT 11-OCT-2005, sequence version 1. DT 29-MAY-2013, entry version 61. DE RecName: Full=ATP-dependent Clp protease proteolytic subunit; DE EC=3.4.21.92; DE Flags: Fragment; GN Name=Clpp; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J; RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9; RA Carninci P., Hayashizaki Y.; RT "High-efficiency full-length cDNA cloning."; RL Methods Enzymol. 303:19-44(1999). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J; RX PubMed=11042159; DOI=10.1101/gr.145100; RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.; RT "Normalization and subtraction of cap-trapper-selected cDNAs to RT prepare full-length cDNA libraries for rapid discovery of new genes."; RL Genome Res. 10:1617-1630(2000). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J; RX PubMed=11076861; DOI=10.1101/gr.152600; RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P., RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., RA Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., RA Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., RA Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., RA Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., RA Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.; RT "RIKEN integrated sequence analysis (RISA) system--384-format RT sequencing pipeline with 384 multicapillary sequencer."; RL Genome Res. 10:1757-1771(2000). RN [4] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J; RG The RIKEN Genome Exploration Research Group Phase II Team and the RG FANTOM Consortium; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). RN [5] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J; RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group RG Phase I and II Team; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [6] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J; RA Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., RA Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., RA Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N., RA Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D., RA Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A., RA Muramatsu M., Hayashizaki Y.; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J; RG The FANTOM Consortium, Riken Genome Exploration Research Group and RG Genome Science Group (Genome Network Project Core Group); RT "The Transcriptional Landscape of the Mammalian Genome."; RL Science 309:1559-1563(2005). RN [8] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J; RX PubMed=16141073; DOI=10.1126/science.1112009; RG RIKEN Genome Exploration Research Group and Genome Science Group RG (Genome Network Project Core Group) and the FANTOM Consortium; RT "Antisense Transcription in the Mammalian Transcriptome."; RL Science 309:1564-1566(2005). CC -!- CATALYTIC ACTIVITY: Hydrolysis of proteins to small peptides in CC the presence of ATP and magnesium. Alpha-casein is the usual test CC substrate. In the absence of ATP, only oligopeptides shorter than CC five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; CC and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- CC and -Tyr-|-Trp bonds also occurs). CC -!- SIMILARITY: Belongs to the peptidase S14 family. 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; AK147719; BAE28093.1; -; mRNA. DR IPI; IPI00133270; -. DR UniGene; Mm.287892; -. DR MGI; MGI:1858213; Clpp. DR HOVERGEN; HBG001689; -. DR InParanoid; Q3UGW4; -. DR ArrayExpress; Q3UGW4; -. DR Bgee; Q3UGW4; -. DR Genevestigator; Q3UGW4; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006515; P:misfolded or incompletely synthesized protein catabolic process; ISA:MGI. DR HAMAP; MF_00444; ClpP; 1; -. DR InterPro; IPR001907; ClpP. DR InterPro; IPR023562; ClpP/TepA. DR InterPro; IPR018215; ClpP_AS. DR PANTHER; PTHR10381; PTHR10381; 1. DR Pfam; PF00574; CLP_protease; 1. DR PRINTS; PR00127; CLPPROTEASEP. DR PROSITE; PS00382; CLP_PROTEASE_HIS; 1. DR PROSITE; PS00381; CLP_PROTEASE_SER; 1. PE 2: Evidence at transcript level; KW Hydrolase; Protease; Serine protease. FT NON_TER 1 1 SQ SEQUENCE 269 AA; 29386 MW; A52360678EE1002E CRC64; RVLLGEARVA VDGCRALLSR LAVHFSPPWT AVSCSPLRRS LHGTATRAFP LIPIVVEQTG RGERAYDIYS RLLRERIVCV MGPIDDSVAS LVIAQLLFLQ SESNKKPIHM YINSPGGVVT AGLAIYDTMQ YILNPICTWC VGQAASMGSL LLAAGSPGMR HSLPNSRIMI HQPSGGARGQ ATDIAIQAEE IMKLKKQLYN IYAKHTKQSL QVIESAMERD RYMSPMEAQE FGILDKVLVH PPQDGEDEPE LVQKETATAP TDPPAPTST //