ID M3YIN5_MUSPF Unreviewed; 202 AA.
AC M3YIN5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Mitochondrial inner membrane protease subunit {ECO:0000256|RuleBase:RU362041};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU362041};
GN Name=IMMP1L {ECO:0000313|Ensembl:ENSMPUP00000011192.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000011192.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000011192.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
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. Known to process the nuclear
CC encoded protein DIABLO. {ECO:0000256|ARBA:ARBA00025546}.
CC -!- SUBUNIT: Heterodimer of 2 subunits, IMMPL1 and IMMPL2.
CC {ECO:0000256|ARBA:ARBA00011805}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273,
CC ECO:0000256|RuleBase:RU362041}.
CC -!- SIMILARITY: Belongs to the peptidase S26 family. IMP1 subfamily.
CC {ECO:0000256|ARBA:ARBA00038445}.
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DR EMBL; AEYP01040227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004755964.1; XM_004755907.2.
DR RefSeq; XP_004755965.1; XM_004755908.2.
DR RefSeq; XP_012913400.1; XM_013057946.1.
DR AlphaFoldDB; M3YIN5; -.
DR STRING; 9669.ENSMPUP00000011192; -.
DR Ensembl; ENSMPUT00000011380.1; ENSMPUP00000011192.1; ENSMPUG00000011284.1.
DR KEGG; mpuf:101691138; -.
DR eggNOG; KOG0171; Eukaryota.
DR GeneTree; ENSGT00550000075025; -.
DR HOGENOM; CLU_028723_4_3_1; -.
DR InParanoid; M3YIN5; -.
DR OMA; CKGPSME; -.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR CDD; cd06530; S26_SPase_I; 1.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR InterPro; IPR019533; Peptidase_S26.
DR NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR PANTHER; PTHR12383:SF16; MITOCHONDRIAL INNER MEMBRANE PROTEASE SUBUNIT 1; 1.
DR PANTHER; PTHR12383; PROTEASE FAMILY S26 MITOCHONDRIAL INNER MEMBRANE PROTEASE-RELATED; 1.
DR Pfam; PF10502; Peptidase_S26; 2.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362041};
KW Membrane {ECO:0000256|RuleBase:RU362041};
KW Mitochondrion {ECO:0000256|RuleBase:RU362041};
KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU362041};
KW Protease {ECO:0000256|RuleBase:RU362041}.
FT DOMAIN 58..130
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 138..182
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 76
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 119
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 202 AA; 22884 MW; D31E4F39A99C35AD CRC64;
MSFMKLKAIS TLLTMINFIN NNNKKSGQWW QSLHRTMLRG VLGKTFRLIG YTIQYGCIAH
CAFEYVGGVL MCSGPSMEPT IQNSDIVFAE NLSRHFYGIQ RGDIVIAKSP SDPKSNICKR
VIGLEGDKIL TNSPSDFFKS HSYVPTGHVW LEGDNLQNST DSRYYGPIPY GLIRGRIFFK
IWPLSDFGFL RDSPNGHRFS DD
//