ID A0A8I5ZQ98_RAT Unreviewed; 452 AA. AC A0A8I5ZQ98; DT 25-MAY-2022, integrated into UniProtKB/TrEMBL. DT 25-MAY-2022, sequence version 1. DT 14-DEC-2022, entry version 4. DE RecName: Full=Mitochondrial-processing peptidase subunit beta {ECO:0000256|ARBA:ARBA00020510}; DE EC=3.4.24.64 {ECO:0000256|ARBA:ARBA00012299}; DE AltName: Full=Beta-MPP {ECO:0000256|ARBA:ARBA00031018}; GN Name=Pmpcb {ECO:0000313|Ensembl:ENSRNOP00000080244.1, GN ECO:0000313|RGD:621297}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000080244.1, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000080244.1, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000080244.1, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|Ensembl:ENSRNOP00000080244.1} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000080244.1}; RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of N-terminal transit peptides from precursor proteins CC imported into the mitochondrion, typically with Arg in position P2.; CC EC=3.4.24.64; Evidence={ECO:0000256|ARBA:ARBA00001098}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947}; CC -!- SUBUNIT: Heterodimer of PMPCA (alpha) and PMPCB (beta) subunits, CC forming the mitochondrial processing protease (MPP) in which PMPCA is CC involved in substrate recognition and binding and PMPCB is the CC catalytic subunit. {ECO:0000256|ARBA:ARBA00011587}. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix CC {ECO:0000256|ARBA:ARBA00004305}. CC -!- SIMILARITY: Belongs to the peptidase M16 family. CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}. 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 Ensembl; ENSRNOT00000099923.1; ENSRNOP00000080244.1; ENSRNOG00000012693.6. DR RGD; 621297; Pmpcb. DR GeneTree; ENSGT00940000156608; -. DR Proteomes; UP000002494; Chromosome 4. DR GO; GO:0017087; C:mitochondrial processing peptidase complex; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IEA:InterPro. DR InterPro; IPR011249; Metalloenz_LuxS/M16. DR InterPro; IPR037718; MPP_beat. DR InterPro; IPR011765; Pept_M16_N. DR InterPro; IPR001431; Pept_M16_Zn_BS. DR InterPro; IPR007863; Peptidase_M16_C. DR PANTHER; PTHR11851:SF103; MITOCHONDRIAL-PROCESSING PEPTIDASE SUBUNIT BETA; 1. DR Pfam; PF00675; Peptidase_M16; 1. DR Pfam; PF05193; Peptidase_M16_C; 1. DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2. DR PROSITE; PS00143; INSULINASE; 1. PE 1: Evidence at protein level; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128}; KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A8I5ZQ98}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}. FT DOMAIN 43..177 FT /note="Peptidase_M16" FT /evidence="ECO:0000259|Pfam:PF00675" FT DOMAIN 183..367 FT /note="Peptidase_M16_C" FT /evidence="ECO:0000259|Pfam:PF05193" SQ SEQUENCE 452 AA; 50400 MW; 0956F2D949DFEF5D CRC64; MVVSCRTWCW EQLRSSVRTA DALSCGALSP DAGNLPNSLG FMQVGLWIDA GSRYENEKNN GTAHFLEHMA FKGTKKRSQL DLELEIENMG AHLNAYTSRE QTVYYAKAFS KDLPRAVEIL ADIIQNSTLG EAEIERERGV ILREMQEVET NLQEVVFDYL HATAYQNTAL GRTILGPTEN IKSISRKDLV DYITTHYKGP RIVLAAAGGV CHNELLELAK FHFGDSLCAH KGDVPALPPC KFTGSEIRVR DDKMPLAHLA VAIEAVGWTH PDTICLMVAN TLIGNWDRSF GGGMNLSSKL AQLTCHGNLC HSFQSFNTSY TDTGLWGLYM VCEQATVADM LHAVQKEWMR LCTAVSESEV ARAKNLLKTN MLLQLDGSTP ICEDIGRQML CYNRRIPIPE LEARIDAVDA EMVREVCTKY IYGKSPAIAA LGPIERLPDF NQICSNMRWT RD //