ID MPPA_BOVIN Reviewed; 525 AA. AC Q0P5M8; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 19-SEP-2006, sequence version 1. DT 16-JUN-2009, entry version 24. DE RecName: Full=Mitochondrial-processing peptidase subunit alpha; DE EC=3.4.24.64; DE AltName: Full=Alpha-MPP; DE Flags: Precursor; GN Name=PMPCA; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Thalamus; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Cleaves presequences (transit peptides) from CC mitochondrial protein precursors (By similarity). CC -!- CATALYTIC ACTIVITY: Release of N-terminal transit peptides from CC precursor proteins imported into the mitochondrion, typically with CC Arg in position P2. CC -!- SUBUNIT: Heterodimer of alpha and beta subunits (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity). CC -!- SIMILARITY: Belongs to the peptidase M16 family. CC -!- CAUTION: Does not seem to have a protease activity as it lack the CC zinc-binding site. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC119849; AAI19850.1; -; mRNA. DR IPI; IPI00702889; -. DR RefSeq; NP_001070432.1; -. DR UniGene; Bt.1487; -. DR MEROPS; M16.971; -. DR MEROPS; M16.985; -. DR Ensembl; ENSBTAG00000001353; Bos taurus. DR GeneID; 767847; -. DR KEGG; bta:767847; -. DR HOVERGEN; Q0P5M8; -. DR OMA; Q0P5M8; YRGNTVG. DR BRENDA; 3.4.24.64; 251. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR InterPro; IPR011237; Pept_M16_core. DR InterPro; IPR011765; Pept_M16_N. DR InterPro; IPR001431; Pept_M16_Zn_BS. DR InterPro; IPR007863; Peptidase_M16_C. DR Gene3D; G3DSA:3.30.830.10; Pept_M16_core; 2. DR Pfam; PF00675; Peptidase_M16; 1. DR Pfam; PF05193; Peptidase_M16_C; 1. DR PROSITE; PS00143; INSULINASE; 1. PE 2: Evidence at transcript level; KW Hydrolase; Metalloprotease; Mitochondrion; Protease; Transit peptide. FT TRANSIT 1 33 Mitochondrion. FT CHAIN 34 525 Mitochondrial-processing peptidase FT subunit alpha. FT /FTId=PRO_0000283040. SQ SEQUENCE 525 AA; 58135 MW; 9D375E3FA8B7E1C2 CRC64; MAAMVLAATR LLRGSGSWGR SRPRFGDPAY RRFSSGGAYP NIPLSSPLPG VPKPVFATVD GQEKFETKVT TLDNGLRVAS QNKFGQFCTV GILINSGSRY EAKYLSGIAH FLEKLAFSST ERFDSKDEIL LTLEKHGGIC DCQTSRDTTM YAVSADSKGL DTVVGLLADV VLHPRLTDEE IEMARMAVQF ELEDLNMRPD PEPLLTEMVH EAAYRENTVG LHRFCPAENV GKMDRDVLHA YLRNYYTPDR MVLAGVGVEH AQLVECARKY LLGTCPAWGT GAAVHVDRSV AQYTGGIVKL ERDMSNVSLG PTPFPELTHI MIGLESCSFL EGDFIPFAVL NMMMGGGGSF SAGGPGKGMF TRLYLNVLNR HHWMYNATSY HHSYEDTGLL CIHASADPRQ VREMVEIVTR EFVLMAGTVD VVELERAKTQ LTSMLMMNLE ARPVIFEDVG RQVLATRSRK LPHELCALIR DVKPEDIKRV ASKMLRGKPA VAALGDLSEL PAYEHVQAAL ASRDGRLPRV YRLFR //