ID Q3UGW4_MOUSE Unreviewed; 269 AA. AC Q3UGW4; DT 11-OCT-2005, integrated into UniProtKB/TrEMBL. DT 11-OCT-2005, sequence version 1. DT 05-OCT-2010, entry version 42. DE RecName: Full=ATP-dependent Clp protease proteolytic subunit; 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 [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(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 STRING; Q3UGW4; -. DR Ensembl; ENSMUST00000002735; ENSMUSP00000002735; ENSMUSG00000002660. DR NMPDR; fig|10090.3.peg.3201; -. DR MGI; MGI:1858213; Clpp. DR HOVERGEN; HBG001689; -. DR InParanoid; Q3UGW4; -. DR PhylomeDB; Q3UGW4; -. DR ArrayExpress; Q3UGW4; -. DR Bgee; Q3UGW4; -. DR Genevestigator; Q3UGW4; -. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005515; F:protein binding; IPI:MGI. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR InterPro; IPR001907; Pept_S14_ClpP. DR InterPro; IPR018215; Pept_S14_ClpP_AS. DR PANTHER; PTHR10381; Pept_S14_ClpP; 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 //