ID   MIPEP_MOUSE             Reviewed;         711 AA.
AC   A6H611; Q2YD79; Q3UJJ3; Q80VA3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   24-JAN-2024, entry version 122.
DE   RecName: Full=Mitochondrial intermediate peptidase;
DE            Short=MIP;
DE            EC=3.4.24.59;
DE   Flags: Precursor;
GN   Name=Mipep;
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=DBA/2J;
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=Czech II, and FVB/N; TISSUE=Brain, and Mammary tumor;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Spleen, and
RC   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: Cleaves proteins, imported into the mitochondrion, to their
CC       mature size. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal octapeptide as second stage of
CC         processing of some proteins imported into the mitochondrion.;
CC         EC=3.4.24.59;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activity is divalent cation-dependent. It is
CC       stimulated by manganese, magnesium or calcium ions and reversibly
CC       inhibited by zinc, cobalt and iron (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M3 family. {ECO:0000305}.
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DR   EMBL; AK146428; BAE27162.1; -; mRNA.
DR   EMBL; BC049871; AAH49871.1; -; mRNA.
DR   EMBL; BC110358; AAI10359.1; -; mRNA.
DR   EMBL; BC145711; AAI45712.1; -; mRNA.
DR   CCDS; CCDS49517.1; -.
DR   RefSeq; NP_081712.2; NM_027436.3.
DR   AlphaFoldDB; A6H611; -.
DR   SMR; A6H611; -.
DR   BioGRID; 214082; 6.
DR   STRING; 10090.ENSMUSP00000069840; -.
DR   iPTMnet; A6H611; -.
DR   PhosphoSitePlus; A6H611; -.
DR   SwissPalm; A6H611; -.
DR   EPD; A6H611; -.
DR   MaxQB; A6H611; -.
DR   PaxDb; 10090-ENSMUSP00000069840; -.
DR   PeptideAtlas; A6H611; -.
DR   ProteomicsDB; 290253; -.
DR   Pumba; A6H611; -.
DR   Antibodypedia; 22428; 455 antibodies from 28 providers.
DR   DNASU; 70478; -.
DR   Ensembl; ENSMUST00000063562.9; ENSMUSP00000069840.8; ENSMUSG00000021993.11.
DR   Ensembl; ENSMUST00000224635.2; ENSMUSP00000153502.2; ENSMUSG00000021993.11.
DR   GeneID; 70478; -.
DR   KEGG; mmu:70478; -.
DR   AGR; MGI:1917728; -.
DR   CTD; 4285; -.
DR   MGI; MGI:1917728; Mipep.
DR   VEuPathDB; HostDB:ENSMUSG00000021993; -.
DR   eggNOG; KOG2090; Eukaryota.
DR   GeneTree; ENSGT00950000183171; -.
DR   HOGENOM; CLU_001805_0_2_1; -.
DR   InParanoid; A6H611; -.
DR   OMA; ALMFEYM; -.
DR   OrthoDB; 735202at2759; -.
DR   PhylomeDB; A6H611; -.
DR   TreeFam; TF105715; -.
DR   BioGRID-ORCS; 70478; 19 hits in 79 CRISPR screens.
DR   ChiTaRS; Mipep; mouse.
DR   PRO; PR:A6H611; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; A6H611; Protein.
DR   Bgee; ENSMUSG00000021993; Expressed in seminiferous tubule of testis and 231 other cell types or tissues.
DR   ExpressionAtlas; A6H611; baseline and differential.
DR   GO; GO:0005759; C:mitochondrial matrix; 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; IBA:GO_Central.
DR   GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR   GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IBA:GO_Central.
DR   CDD; cd06457; M3A_MIP; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR   InterPro; IPR033851; M3A_MIP.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR11804:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 1.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
DR   Genevisible; A6H611; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Calcium; Cobalt; Hydrolase; Iron; Magnesium; Manganese;
KW   Metal-binding; Metalloprotease; Mitochondrion; Protease;
KW   Reference proteome; Transit peptide; Zinc.
FT   TRANSIT         1..33
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           34..711
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000319045"
FT   ACT_SITE        494
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         493
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         497
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         500
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   MOD_RES         124
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99797"
FT   CONFLICT        61
FT                   /note="R -> RVP (in Ref. 1; BAE27162)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        286
FT                   /note="S -> N (in Ref. 1; BAE27162)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        419
FT                   /note="A -> T (in Ref. 1; BAE27162)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        508
FT                   /note="Y -> H (in Ref. 2; AAI10359)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        595
FT                   /note="T -> A (in Ref. 1; BAE27162)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   711 AA;  80852 MW;  C22E9FFFB86A7ECB CRC64;
     MLLAAGARYA RRLCGRGAAA ALQGRTGRSC ARDVSTSWSP VGAAFNVKPQ SHLWNLLGER
     RGLFGVPELS TPEGFQVAQE EALKKTEWLV ERACSTPPGP QTVLIFDELS DCLCRVADLA
     DFVKIGHPDP AFREAAQEAC RSIGTMVEKL NTNVELYQSL QRLLGDKKLM ESLDAETRRV
     AELFMFDFEI SGIHLDEEKR RRAVDLNVKI LDLSNAFLMR TNFPNKIRKS LLPEHIQHHF
     ARDGSHLIID GLHAEASDDL VREAAYKIFL YPNADQLKCL EELLSSRDLL AKLVGYSTFS
     HRALQGTIAQ TPETVMQFLE KLSEKLSERT RKDFKMMQGM KTKLNPQNSK LMPWDPPYYS
     GVIRAERYNI EPSLYCPFLS LGACMEGLNV LFNKLLGITL YAEQTFKGEV WCNDIRKLAV
     VHESEGLLGY IYCDFFQRAN KPQQDCHFTI RGGRLKEDGS YQLPVVVLML NLPHASRDFP
     TLLTPGMMEN LFHEMGHAMH SMLGRTRYQH VTGTRCPTDF AEVPSILMEY FSNDYRVVSQ
     FAKHYQTGQP LPKAMVSRLC ESKKVCTAAE MQLQVFYAAL DQIYHGQHPL KKSTTDILME
     TQEQFYGLPY VPDTAWQLRF SHLVGYGAKY YSYLMSRAVA SMIWKECFLQ DPFNRAAGER
     YRREMLAHGG GKEPMLMIQG MLQKCPSIDD FVDALVSDMN LDFETFFLDS K
//