MIPEP_MOUSE
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 03-AUG-2022, entry version 114.
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 EPD; A6H611; -.
DR MaxQB; A6H611; -.
DR PaxDb; A6H611; -.
DR PeptideAtlas; A6H611; -.
DR PRIDE; A6H611; -.
DR ProteomicsDB; 290253; -.
DR Antibodypedia; 22428; 400 antibodies from 28 providers.
DR DNASU; 70478; -.
DR Ensembl; ENSMUST00000063562; ENSMUSP00000069840; ENSMUSG00000021993.
DR Ensembl; ENSMUST00000224635; ENSMUSP00000153502; ENSMUSG00000021993.
DR GeneID; 70478; -.
DR KEGG; mmu:70478; -.
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; VVYCDLF; -.
DR OrthoDB; 642479at2759; -.
DR PhylomeDB; A6H611; -.
DR TreeFam; TF105715; -.
DR BioGRID-ORCS; 70478; 19 hits in 74 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 228 other tissues.
DR ExpressionAtlas; A6H611; baseline and differential.
DR Genevisible; A6H611; MM.
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 GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR Gene3D; 1.10.1370.10; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
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; PTHR11804; 2.
DR Pfam; PF01432; Peptidase_M3; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
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
