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 29-MAY-2013, entry version 53.
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; M03.006; -.
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
//
