MPPA_MOUSE
ID MPPA_MOUSE Reviewed; 524 AA.
AC Q9DC61; Q3TF19;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Mitochondrial-processing peptidase subunit alpha;
DE AltName: Full=Alpha-MPP;
DE AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000305};
DE AltName: Full=P-55;
DE Flags: Precursor;
GN Name=Pmpca; Synonyms=Inpp5e;
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=Heart, and Lung;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 250-267; 288-298; 362-369 AND 417-425, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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).
RN [5]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-63, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-298, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Substrate recognition and binding subunit of the essential
CC mitochondrial processing protease (MPP), which cleaves the
CC mitochondrial sequence off newly imported precursors proteins.
CC {ECO:0000250|UniProtKB:Q10713}.
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:P11914}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P20069}. Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q10713}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
CC -!- CAUTION: Does not seem to have a protease activity as it lack the zinc-
CC binding site. {ECO:0000305}.
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DR EMBL; AK004549; BAB23363.1; -; mRNA.
DR EMBL; AK147110; BAE27682.1; -; mRNA.
DR EMBL; AK169325; BAE41079.1; -; mRNA.
DR EMBL; AK169342; BAE41094.1; -; mRNA.
DR EMBL; BC010810; AAH10810.1; -; mRNA.
DR CCDS; CCDS15804.1; -.
DR RefSeq; NP_775272.1; NM_173180.3.
DR AlphaFoldDB; Q9DC61; -.
DR SMR; Q9DC61; -.
DR BioGRID; 211772; 4.
DR IntAct; Q9DC61; 2.
DR MINT; Q9DC61; -.
DR STRING; 10090.ENSMUSP00000075762; -.
DR MEROPS; M16.985; -.
DR MEROPS; M16.P01; -.
DR iPTMnet; Q9DC61; -.
DR PhosphoSitePlus; Q9DC61; -.
DR SwissPalm; Q9DC61; -.
DR EPD; Q9DC61; -.
DR jPOST; Q9DC61; -.
DR MaxQB; Q9DC61; -.
DR PaxDb; Q9DC61; -.
DR PeptideAtlas; Q9DC61; -.
DR PRIDE; Q9DC61; -.
DR ProteomicsDB; 290306; -.
DR Antibodypedia; 18730; 130 antibodies from 25 providers.
DR DNASU; 66865; -.
DR Ensembl; ENSMUST00000076431; ENSMUSP00000075762; ENSMUSG00000026926.
DR GeneID; 66865; -.
DR KEGG; mmu:66865; -.
DR UCSC; uc008ive.1; mouse.
DR CTD; 23203; -.
DR MGI; MGI:1918568; Pmpca.
DR VEuPathDB; HostDB:ENSMUSG00000026926; -.
DR eggNOG; KOG2067; Eukaryota.
DR GeneTree; ENSGT00940000156724; -.
DR HOGENOM; CLU_009902_5_2_1; -.
DR InParanoid; Q9DC61; -.
DR OMA; LKYHHSP; -.
DR OrthoDB; 631107at2759; -.
DR PhylomeDB; Q9DC61; -.
DR TreeFam; TF105031; -.
DR Reactome; R-MMU-8949664; Processing of SMDT1.
DR BioGRID-ORCS; 66865; 22 hits in 75 CRISPR screens.
DR ChiTaRS; Pmpca; mouse.
DR PRO; PR:Q9DC61; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9DC61; protein.
DR Bgee; ENSMUSG00000026926; Expressed in yolk sac and 253 other tissues.
DR ExpressionAtlas; Q9DC61; baseline and differential.
DR Genevisible; Q9DC61; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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; ISS:UniProtKB.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR037715; PMPCA.
DR PANTHER; PTHR11851:SF192; PTHR11851:SF192; 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 Acetylation; Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 34..524
FT /note="Mitochondrial-processing peptidase subunit alpha"
FT /id="PRO_0000026768"
FT MOD_RES 63
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 298
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
SQ SEQUENCE 524 AA; 58279 MW; AD15AE6C97E95F9A CRC64;
MATAVWAAAR LLRGSAVLCA RPRFGSPAHR RFSSGATYPN IPLSSPLPGV PKPIFATVDG
QEKFETKVTT LDNGLRVASQ NKFGQFCTVG ILINSGSRYE AKYLSGIAHF LEKLAFSSTA
RFDSKDEILL TLEKHGGICD CQTSRDTTMY AVSADSKGLD TVVDLLADVV LHPRLTDEEI
EMTRMAVQFE LEDLNMRPDP EPLLTEMIHE AAFRENTVGL HRFCPVENIA KIDREVLHSY
LKNYYTPDRM VLAGVGVEHE HLVECARKYL VGAEPAWGAP GTVDVDRSVA QYTGGIIKVE
RDMSNVSLGP TPIPELTHIM VGLESCSFLE DDFIPFAVLN MMMGGGGSFS AGGPGKGMFS
RLYLNVLNRH HWMYNATSYH HSYEDTGLLC IHASADPRQV REMVEIITKE FILMGRTVDL
VELERAKTQL MSMLMMNLES RPVIFEDVGR QVLATHSRKL PHELCTLIRN VKPEDIKRVA
SKMLRGKPAV AALGDLTDLP TYEHIQAALS SRNGHLPRSY RLFR
