MPPB_MOUSE
ID MPPB_MOUSE Reviewed; 489 AA.
AC Q9CXT8;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Mitochondrial-processing peptidase subunit beta;
DE EC=3.4.24.64 {ECO:0000250|UniProtKB:Q03346};
DE AltName: Full=Beta-MPP;
DE AltName: Full=P-52;
DE Flags: Precursor;
GN Name=Pmpcb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic head;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalytic subunit of the essential mitochondrial processing
CC protease (MPP), which cleaves the mitochondrial sequence off newly
CC imported precursors proteins (By similarity). Preferentially, cleaves
CC after an arginine at position P2 (By similarity). Required for PINK1
CC turnover by coupling PINK1 mitochondrial import and cleavage, which
CC results in subsequent PINK1 proteolysis (By similarity).
CC {ECO:0000250|UniProtKB:O75439, ECO:0000250|UniProtKB:Q03346}.
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:0000250|UniProtKB:Q03346};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P10507};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P10507};
CC -!- ACTIVITY REGULATION: Binding to PMPCA is required for catalytic
CC activity. {ECO:0000250|UniProtKB:P10507}.
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:0000250|UniProtKB:P10507}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:O75439}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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DR EMBL; AK013995; BAB29105.1; -; mRNA.
DR CCDS; CCDS19106.1; -.
DR RefSeq; NP_082707.1; NM_028431.2.
DR AlphaFoldDB; Q9CXT8; -.
DR SMR; Q9CXT8; -.
DR BioGRID; 215753; 4.
DR STRING; 10090.ENSMUSP00000030882; -.
DR MEROPS; M16.973; -.
DR iPTMnet; Q9CXT8; -.
DR PhosphoSitePlus; Q9CXT8; -.
DR SwissPalm; Q9CXT8; -.
DR REPRODUCTION-2DPAGE; Q9CXT8; -.
DR EPD; Q9CXT8; -.
DR jPOST; Q9CXT8; -.
DR MaxQB; Q9CXT8; -.
DR PaxDb; Q9CXT8; -.
DR PRIDE; Q9CXT8; -.
DR ProteomicsDB; 252609; -.
DR Antibodypedia; 31179; 189 antibodies from 27 providers.
DR DNASU; 73078; -.
DR Ensembl; ENSMUST00000030882; ENSMUSP00000030882; ENSMUSG00000029017.
DR GeneID; 73078; -.
DR KEGG; mmu:73078; -.
DR UCSC; uc008wox.1; mouse.
DR CTD; 9512; -.
DR MGI; MGI:1920328; Pmpcb.
DR VEuPathDB; HostDB:ENSMUSG00000029017; -.
DR eggNOG; KOG0960; Eukaryota.
DR GeneTree; ENSGT00940000156608; -.
DR HOGENOM; CLU_009902_4_0_1; -.
DR InParanoid; Q9CXT8; -.
DR OMA; IDVVCDM; -.
DR OrthoDB; 638125at2759; -.
DR PhylomeDB; Q9CXT8; -.
DR TreeFam; TF105032; -.
DR Reactome; R-MMU-8949664; Processing of SMDT1.
DR BioGRID-ORCS; 73078; 25 hits in 74 CRISPR screens.
DR ChiTaRS; Pmpcb; mouse.
DR PRO; PR:Q9CXT8; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9CXT8; protein.
DR Bgee; ENSMUSG00000029017; Expressed in spermatid and 260 other tissues.
DR ExpressionAtlas; Q9CXT8; baseline and differential.
DR Genevisible; Q9CXT8; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0017087; C:mitochondrial processing peptidase complex; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISO:MGI.
DR GO; GO:0008237; F:metallopeptidase activity; ISO:MGI.
DR GO; GO:0016485; P:protein processing; ISO:MGI.
DR GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; ISO:MGI.
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; PTHR11851:SF103; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; SSF63411; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Protease;
KW Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..45
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:O75439"
FT CHAIN 46..489
FT /note="Mitochondrial-processing peptidase subunit beta"
FT /id="PRO_0000026778"
FT ACT_SITE 104
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT SITE 191
FT /note="Required for the specific determination of the
FT substrate cleavage site"
FT /evidence="ECO:0000250|UniProtKB:Q03346"
FT SITE 195
FT /note="Required for the specific determination of the
FT substrate cleavage site"
FT /evidence="ECO:0000250|UniProtKB:Q03346"
SQ SEQUENCE 489 AA; 54614 MW; 1B594EE0B6FE34A4 CRC64;
MAAAALSRTL LPEARRRLWG FTRRLPLRRA AAQPLYFGGD RLRSTQAAPQ VVLNVPETQV
TCLENGLRVA SENSGLSTCT VGLWIDAGSR YENEKNNGTA HFLEHMAFKG TKKRSQLDLE
LEIENMGAHL NAYTSREQTV YYAKAFSRDL PRAVEILADI IQNSTLGEAE IERERGVILR
EMQEVETNLQ EVVFDYLHAT AYQNTALGRT ILGPTENIKS INRKDLVDYI TTHYKGPRIV
LAAAGGVCHN ELLELAKFHF GDSLCSHKGA IPALPPCKFT GSEIRVRDDK MPLAHLAIAV
EAVGWAHPDT ICLMVANTLI GNWDRSFGGG MNLSSKLAQL TCHGNLCHSF QSFNTSYTDT
GLWGLYMVCE QATVADMLHV VQNEWKRLCT DVTESEVARA KNLLKTNMLL QLDGSTPICE
DIGRQMLCYN RRIPIPELEA RIDAVDAETV RRVCTKYIHD KSPAIAALGP IERLPDFNQI
CSNMRWIRD
