ID M3X386_FELCA Unreviewed; 166 AA.
AC M3X386;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 61.
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:ENSFCAP00000021086.1,
GN ECO:0000313|VGNC:VGNC:62916};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000021086.1, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000021086.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000021086.1,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000021086.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000021086.1,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000021086.1}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000021086.1};
RG Ensembl;
RL Submitted (SEP-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; AANG04004362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003993176.1; XM_003993127.4.
DR RefSeq; XP_006937227.1; XM_006937165.2.
DR RefSeq; XP_006937228.1; XM_006937166.2.
DR RefSeq; XP_006937230.1; XM_006937168.3.
DR RefSeq; XP_006937231.1; XM_006937169.3.
DR RefSeq; XP_006937232.1; XM_006937170.3.
DR RefSeq; XP_011285119.1; XM_011286817.2.
DR RefSeq; XP_019667779.1; XM_019812220.1.
DR RefSeq; XP_019667780.1; XM_019812221.1.
DR AlphaFoldDB; M3X386; -.
DR PaxDb; 9685-ENSFCAP00000021086; -.
DR Ensembl; ENSFCAT00000023795.4; ENSFCAP00000021086.1; ENSFCAG00000028332.4.
DR GeneID; 101086502; -.
DR KEGG; fca:101086502; -.
DR CTD; 196294; -.
DR VGNC; VGNC:62916; IMMP1L.
DR eggNOG; KOG0171; Eukaryota.
DR GeneTree; ENSGT00550000075025; -.
DR HOGENOM; CLU_028723_4_3_1; -.
DR OrthoDB; 447775at2759; -.
DR Proteomes; UP000011712; Chromosome D1.
DR Bgee; ENSFCAG00000028332; Expressed in spleen and 10 other cell types or tissues.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712}.
FT DOMAIN 21..94
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 102..146
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 40
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 83
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 166 AA; 18577 MW; FB331EDF6467C08B CRC64;
MLRGVLGKTF RLVGYTIQYG CIAHCAFEYV GGVVMCSGPS MEPTIQNSDV VFAENLSRHF
YGIQRGDIVI AKSPSDPKSN ICKRVIGLEG DKILTNSPSD FFKSHSYVPT GHVWLEGDNL
QNSTDSRYYG PIPYGLIRGR IFFKIWPLSD FGFLRDSPNG HRFSDD
//