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Database: UniProt
Entry: Q5RF14
LinkDB: Q5RF14
Original site: Q5RF14 
ID   MIPEP_PONAB             Reviewed;         713 AA.
AC   Q5RF14;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   16-OCT-2013, entry version 54.
DE   RecName: Full=Mitochondrial intermediate peptidase;
DE            Short=MIP;
DE            EC=3.4.24.59;
DE   Flags: Precursor;
GN   Name=MIPEP;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cleaves proteins, imported into the mitochondrion, to
CC       their mature size (By similarity).
CC   -!- CATALYTIC ACTIVITY: Release of an N-terminal octapeptide as second
CC       stage of processing of some proteins imported into the
CC       mitochondrion.
CC   -!- COFACTOR: Binds 1 zinc ion (By similarity).
CC   -!- ENZYME 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).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
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DR   EMBL; CR857347; CAH89643.1; -; mRNA.
DR   RefSeq; NP_001124737.1; NM_001131265.1.
DR   ProteinModelPortal; Q5RF14; -.
DR   MEROPS; M03.A05; -.
DR   GeneID; 100171586; -.
DR   KEGG; pon:100171586; -.
DR   CTD; 4285; -.
DR   HOGENOM; HOG000230535; -.
DR   HOVERGEN; HBG008215; -.
DR   InParanoid; Q5RF14; -.
DR   KO; K01410; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1370.10; -; 2.
DR   Gene3D; 1.20.1050.40; -; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR024080; Neurolysin/TOP_N.
DR   InterPro; IPR001567; Pept_M3A_M3B.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Calcium; Cobalt; Complete proteome; Hydrolase; Iron;
KW   Magnesium; Manganese; Metal-binding; Metalloprotease; Mitochondrion;
KW   Protease; Reference proteome; Transit peptide; Zinc.
FT   TRANSIT       1     35       Mitochondrion (By similarity).
FT   CHAIN        36    713       Mitochondrial intermediate peptidase.
FT                                /FTId=PRO_0000319049.
FT   ACT_SITE    496    496       By similarity.
FT   METAL       495    495       Zinc; catalytic (By similarity).
FT   METAL       499    499       Zinc; catalytic (By similarity).
FT   METAL       502    502       Zinc; catalytic (By similarity).
FT   MOD_RES     126    126       N6-acetyllysine (By similarity).
SQ   SEQUENCE   713 AA;  80478 MW;  32FB7C32F5BD1FF9 CRC64;
     MLCVGRLGGL GARAAALPPR RAGRGILEAG IRARRVSTSW SPVGAAFNVK PQGSRLDLFG
     ERRGLFGVPE LSAPEGFHAA QEKALRKAEL LVGRACSTPP GPQTVLIFDE LSDSLCRVAD
     LADFVKIAHP EPAFREAAEE ACRSIGTMVE KLNTNVDLYQ SLRKLLADKK LVDSLDPETR
     RVAELFMFDF EISGIHLDKE KRKRAVDLNV KILDLSSTFL MGANFPNKIE KHLLPEHIRR
     NFTSAGDHII IDGLHAESPD DLVREAAYKI FLYPNAGQLK CLEELLSSRD LLAKLVGYST
     FSHRALQGTI AKNPETVMQF LEKLSDKLSE RTLKDFEMIR GMKMKLNPQN SEVMPWDPPY
     YSGVIRAERY NIEPSLYCPF FSLGACMEGL NILLNRLLGI SLYAEQPAKG EVWSEDVRKL
     AVVHESEGLL GYIYCDFFQR ADKPHQDCHF TIRGGRLKED GDYQLPVVVL MLNLPRSSRS
     SPTLLTPGMM ENLFHEMGHA MHSMLGRTRY QHVTGTRCPT DFAEVPSILM EYFANDYRVV
     NQFARHYQTG QPLPKNMVSR LCESKKVCAA ADMQLQVFYA TLDQIYHGKH PLRNSTTDIL
     KETQEKFYGL PYVPDTAWQL RFSHLVGYGA KYYSYLMSRA VASMVWKECF LQDPFNRAAG
     ERYRREMLAH GGGREPMLMV EGMLQKCPSV DDFVSALVSD LDLDFETFLM DSE
//
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