ID   MIPEP_RAT               Reviewed;         710 AA.
AC   Q01992;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Mitochondrial intermediate peptidase;
DE            Short=MIP;
DE            EC=3.4.24.59;
DE   Flags: Precursor;
GN   Name=Mipep; Synonyms=Mip;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=1518864; DOI=10.1073/pnas.89.17.8317;
RA   Isaya G., Kalousek F., Rosenberg L.E.;
RT   "Sequence analysis of rat mitochondrial intermediate peptidase: similarity
RT   to zinc metallopeptidases and to a putative yeast homologue.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:8317-8321(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 34-50 AND 528-542.
RC   TISSUE=Liver;
RX   PubMed=1322290; DOI=10.1002/j.1460-2075.1992.tb05347.x;
RA   Kalousek F., Isaya G., Rosenberg L.E.;
RT   "Rat liver mitochondrial intermediate peptidase (MIP): purification and
RT   initial characterization.";
RL   EMBO J. 11:2803-2809(1992).
CC   -!- FUNCTION: Cleaves proteins, imported into the mitochondrion, to their
CC       mature size.
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.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the peptidase M3 family. {ECO:0000305}.
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DR   EMBL; M96633; AAA41899.1; -; mRNA.
DR   PIR; A46273; A46273.
DR   AlphaFoldDB; Q01992; -.
DR   SMR; Q01992; -.
DR   STRING; 10116.ENSRNOP00000018845; -.
DR   iPTMnet; Q01992; -.
DR   PhosphoSitePlus; Q01992; -.
DR   jPOST; Q01992; -.
DR   PaxDb; Q01992; -.
DR   PRIDE; Q01992; -.
DR   UCSC; RGD:621680; rat.
DR   RGD; 621680; Mipep.
DR   eggNOG; KOG2090; Eukaryota.
DR   InParanoid; Q01992; -.
DR   PRO; PR:Q01992; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IDA:RGD.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004175; F:endopeptidase activity; IDA:RGD.
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; Direct protein sequencing; Hydrolase; Iron;
KW   Magnesium; Manganese; Metal-binding; Metalloprotease; Mitochondrion;
KW   Protease; Reference proteome; Transit peptide; Zinc.
FT   TRANSIT         1..33
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:1322290"
FT   CHAIN           34..710
FT                   /note="Mitochondrial intermediate peptidase"
FT                   /id="PRO_0000028580"
FT   ACT_SITE        493
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         492
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         496
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         499
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"
SQ   SEQUENCE   710 AA;  80674 MW;  4FC2E6743EA43558 CRC64;
     MLLAAGTRYA YRLCGRRAAA ALQGRAGRSC ARSVSTSWSP VGAAFNVKPQ GHLWDLLGER
     RGLFGVPELS TPEGFQVAQE EALRKTEWLV ERACSTPPGP QTVLIFDELS DCLCRVADLA
     DFVKIGHPEQ AFREAAQEAC RSIGTMVEKL NTNVELYQSL QKLLDDKKLM DSLDAETRRV
     AELFMFDFEI SGIHLDEEKR RRAVDLNVKI LDLSSAFLMG TNFPIKIQKH LLPEHIQHHF
     ARDGRHLVID GLHAEASDDL VREAAYKIFL YPNADQLKCL EELLSSRDLL ANLVGYLPFP
     TGPPGTIAQT PETVMQFLEK LSEKLCERTR KDFEMMQGMK TKLNPQNSEL MPWDPPYYSG
     VIRAERYNIE PSLYCPFLSL GACMEGLNVL FNRLLGVTLY AEQPFKGEVW CIDVRKLAVV
     HESEGLLGYI YCDFFQRANK PQQDCHFTIR GGRLKEDGSY QLPVVVLMLN LPHASRDFPT
     LLTPGMMENL FHEMGHAMHS MLGRTRYQHV TGTRCPTDFA EVPSILMEYF SNDYRVVSQF
     AKHYQTGQPL PKAMVSRLCE SKKVCAAAEM QLQVFYAALD QIYHGQHPLK KSTTDILMET
     QEQFYGLPYV PDTAWQLRFS HLVGYGAKYY SYLMSRAVAS MVWKECFLQD PFNRAAGERY
     RREMLAHGGG KEPMLMIQGM LQKCPSIDDF VDALVSDLNL DFETFFMDSK