ID   IMP2L_XENLA             Reviewed;         170 AA.
AC   Q5PQ63;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Mitochondrial inner membrane protease subunit 2;
DE            EC=3.4.21.-;
DE   AltName: Full=IMP2-like protein;
GN   Name=immp2l;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the removal of transit peptides required for the
CC       targeting of proteins from the mitochondrial matrix, across the inner
CC       membrane, into the inter-membrane space. {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of 2 subunits, IMMPL1 and IMMPL2. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family. IMP2 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC087345; AAH87345.1; -; mRNA.
DR   RefSeq; NP_001088705.1; NM_001095236.1.
DR   RefSeq; XP_018106654.1; XM_018251165.1.
DR   AlphaFoldDB; Q5PQ63; -.
DR   SMR; Q5PQ63; -.
DR   DNASU; 495969; -.
DR   GeneID; 495969; -.
DR   KEGG; xla:495969; -.
DR   CTD; 495969; -.
DR   Xenbase; XB-GENE-1010852; immp2l.L.
DR   OrthoDB; 1211147at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 495969; Expressed in stomach and 19 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042720; C:mitochondrial inner membrane peptidase complex; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IEA:InterPro.
DR   GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR   CDD; cd06530; S26_SPase_I; 1.
DR   InterPro; IPR037730; IMP2.
DR   InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR   InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR   InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR   InterPro; IPR019533; Peptidase_S26.
DR   PANTHER; PTHR46041; PTHR46041; 1.
DR   Pfam; PF10502; Peptidase_S26; 2.
DR   PRINTS; PR00727; LEADERPTASE.
DR   SUPFAM; SSF51306; SSF51306; 1.
DR   TIGRFAMs; TIGR02227; sigpep_I_bact; 1.
DR   PROSITE; PS00761; SPASE_I_3; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Membrane; Mitochondrion; Mitochondrion inner membrane; Protease;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..170
FT                   /note="Mitochondrial inner membrane protease subunit 2"
FT                   /id="PRO_0000259580"
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        40
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        88
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   170 AA;  19269 MW;  D92E09E30CCFF710 CRC64;
     MAQHGRRYVR AFISGFFVAV PVTVTFLDRV ACIARVEGVS MQPSLNPDAR GESDIVLLNR
     WRARNYDVQR GDIVSLVSPK NPEQKIIKRV IALEGDIVKT LGHKNRYVKV PRGHVWVEGD
     HHGHSFDSNA FGPVSLGLLH SHATHILWPP NRWQKLKPFL PVERESVQND