MPPA_CAEEL
ID MPPA_CAEEL Reviewed; 514 AA.
AC Q95XN2; W6RR41;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Mitochondrial-processing peptidase subunit alpha {ECO:0000303|PubMed:16788047};
DE AltName: Full=Alpha-MPP {ECO:0000303|PubMed:16788047};
DE AltName: Full=Inactive zinc metalloprotease mppa-1 {ECO:0000305};
DE Flags: Precursor;
GN Name=mppa-1 {ECO:0000303|PubMed:16788047,
GN ECO:0000312|WormBase:Y71G12B.24a};
GN ORFNames=Y71G12B.24 {ECO:0000312|EMBL:CCD67978.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, LACK OF PROTEASE ACTIVITY, IDENTIFICATION IN COMPLEX WITH MPPB-1,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=16788047; DOI=10.1093/jb/mvj114;
RA Nomura H., Athauda S.B., Wada H., Maruyama Y., Takahashi K., Inoue H.;
RT "Identification and reverse genetic analysis of mitochondrial processing
RT peptidase and the core protein of the cytochrome bc1 complex of
RT Caenorhabditis elegans, a model parasitic nematode.";
RL J. Biochem. 139:967-979(2006).
CC -!- FUNCTION: Substrate recognition and binding subunit of the essential
CC mitochondrial processing protease (MPP), which cleaves the
CC mitochondrial sequence off newly imported precursors proteins.
CC {ECO:0000305|PubMed:16788047}.
CC -!- SUBUNIT: Heterodimer of mppa-1 (alpha) and mppb-1 (beta) subunits,
CC forming the mitochondrial processing protease (MPP) in which mppa-1 is
CC involved in substrate recognition and binding and mppb-1 is the
CC catalytic subunit. {ECO:0000305|PubMed:16788047}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P20069}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:Y71G12B.24a};
CC IsoId=Q95XN2-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:Y71G12B.24b};
CC IsoId=Q95XN2-2; Sequence=VSP_060435;
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes 63 percent
CC embryonic lethality (PubMed:16788047). Embryonic lethality is further
CC increased in simultaneous RNAi-mediated knockdown of mppa-1 and mppb-1
CC or ucr-1 and mppa-1 (PubMed:16788047). {ECO:0000269|PubMed:16788047}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
CC -!- CAUTION: Although it belongs to the peptidase M16 family, lacks the
CC zinc-binding sites and appears to lack catalytic activity in vitro.
CC {ECO:0000269|PubMed:16788047}.
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DR EMBL; BX284601; CCD67978.2; -; Genomic_DNA.
DR EMBL; BX284601; CDM63585.1; -; Genomic_DNA.
DR RefSeq; NP_001293445.1; NM_001306516.1.
DR RefSeq; NP_490888.2; NM_058487.6. [Q95XN2-1]
DR AlphaFoldDB; Q95XN2; -.
DR SMR; Q95XN2; -.
DR STRING; 6239.Y71G12B.24; -.
DR EPD; Q95XN2; -.
DR PaxDb; Q95XN2; -.
DR PeptideAtlas; Q95XN2; -.
DR EnsemblMetazoa; Y71G12B.24a.1; Y71G12B.24a.1; WBGene00022159. [Q95XN2-1]
DR EnsemblMetazoa; Y71G12B.24b.1; Y71G12B.24b.1; WBGene00022159. [Q95XN2-2]
DR GeneID; 171737; -.
DR KEGG; cel:CELE_Y71G12B.24; -.
DR UCSC; Y71G12B.24; c. elegans. [Q95XN2-1]
DR CTD; 171737; -.
DR WormBase; Y71G12B.24a; CE48095; WBGene00022159; mppa-1. [Q95XN2-1]
DR WormBase; Y71G12B.24b; CE49612; WBGene00022159; mppa-1. [Q95XN2-2]
DR eggNOG; KOG2067; Eukaryota.
DR GeneTree; ENSGT00940000156724; -.
DR HOGENOM; CLU_009902_5_2_1; -.
DR InParanoid; Q95XN2; -.
DR OMA; LKYHHSP; -.
DR OrthoDB; 631107at2759; -.
DR Reactome; R-CEL-8949664; Processing of SMDT1.
DR PRO; PR:Q95XN2; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00022159; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0017087; C:mitochondrial processing peptidase complex; IDA:WormBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IDA:WormBase.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR037715; PMPCA.
DR PANTHER; PTHR11851:SF192; PTHR11851:SF192; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; SSF63411; 2.
PE 3: Inferred from homology;
KW Alternative splicing; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..55
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 56..514
FT /note="Mitochondrial-processing peptidase subunit alpha"
FT /id="PRO_0000448710"
FT VAR_SEQ 1..352
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060435"
SQ SEQUENCE 514 AA; 57494 MW; 0A7FD7C89FDB0498 CRC64;
MLLRKSIPYI KICRDISASV RNNKEIAQKL PLSVPLPMEN NSKSIEKGCP PMGRNSRVTR
LPNGLKVCTE DTYGDFVTVG VAIESGCRYE NGFPFGISRI VEKLAYNSSE SFSSRDEVFA
KLEENSGIVD CQSTRDTMMY AASCHRDGVD SVIHVLSDTI WKPIFDEQSL EQAKLTVSYE
NQDLPNRIEA IEILLTDWIH QAAFQNNTIG YPKFGNNSMD KIRVSDVYGF LSRAHTPQRM
VVGGVGVGHD EFVSIISRHF DLNKSTWTTQ PTVLPAKIPE IDESRAQYTG GELRLDTDLT
KLTIGKPYPL LSHVVLGLEG CSYKDEDFVA FCVLQSLLGG GGAFSAGGPG KGMYARMYTE
LMNRHHWIYS AIAHNHSYSD SGVFTVTASS PPENINDALI LLVHQILQLQ QGVEPTELAR
ARTQLRSHLM MNLEVRPVLF EDMVRQVLGH GDRKQPEEYA EKIEKVTNSD IIRVTERLLA
SKPSLVGYGD IKKLKDLRSL DQAVAKRDLK YLFN
