IMP1L_MOUSE
ID IMP1L_MOUSE Reviewed; 166 AA.
AC Q9CQU8; Q3THN4;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Mitochondrial inner membrane protease subunit 1;
DE EC=3.4.21.-;
DE AltName: Full=IMP1-like protein;
GN Name=Immp1l;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J;
RC TISSUE=Cerebellum, Egg, Olfactory bulb, Testis, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129, and C57BL/6J; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of 2 subunits, IMMPL1 and IMMPL2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S26 family. IMP1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AK005356; BAB23971.1; -; mRNA.
DR EMBL; AK009570; BAB26367.1; -; mRNA.
DR EMBL; AK010075; BAB26684.1; -; mRNA.
DR EMBL; AK011278; BAB27512.1; -; mRNA.
DR EMBL; AK011382; BAB27582.1; -; mRNA.
DR EMBL; AK011420; BAB27608.1; -; mRNA.
DR EMBL; AK011466; BAB27637.1; -; mRNA.
DR EMBL; AK011618; BAB27737.1; -; mRNA.
DR EMBL; AK011872; BAB27891.1; -; mRNA.
DR EMBL; AK012181; BAB28082.1; -; mRNA.
DR EMBL; AK015978; BAB30062.1; -; mRNA.
DR EMBL; AK078300; BAC37210.1; -; mRNA.
DR EMBL; AK135670; BAE22608.1; -; mRNA.
DR EMBL; AK168202; BAE40162.1; -; mRNA.
DR EMBL; BC008259; AAH08259.1; -; mRNA.
DR EMBL; BC081433; AAH81433.1; -; mRNA.
DR CCDS; CCDS38192.1; -.
DR RefSeq; NP_082536.1; NM_028260.2.
DR AlphaFoldDB; Q9CQU8; -.
DR SMR; Q9CQU8; -.
DR STRING; 10090.ENSMUSP00000049044; -.
DR PhosphoSitePlus; Q9CQU8; -.
DR EPD; Q9CQU8; -.
DR MaxQB; Q9CQU8; -.
DR PaxDb; Q9CQU8; -.
DR PeptideAtlas; Q9CQU8; -.
DR PRIDE; Q9CQU8; -.
DR ProteomicsDB; 269478; -.
DR Antibodypedia; 49000; 85 antibodies from 25 providers.
DR DNASU; 66541; -.
DR Ensembl; ENSMUST00000037499; ENSMUSP00000049044; ENSMUSG00000042670.
DR GeneID; 66541; -.
DR KEGG; mmu:66541; -.
DR UCSC; uc008lle.1; mouse.
DR CTD; 196294; -.
DR MGI; MGI:1913791; Immp1l.
DR VEuPathDB; HostDB:ENSMUSG00000042670; -.
DR eggNOG; KOG0171; Eukaryota.
DR GeneTree; ENSGT00550000075025; -.
DR HOGENOM; CLU_028723_4_3_1; -.
DR InParanoid; Q9CQU8; -.
DR OMA; CKGPSME; -.
DR OrthoDB; 1211147at2759; -.
DR PhylomeDB; Q9CQU8; -.
DR TreeFam; TF315083; -.
DR BioGRID-ORCS; 66541; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Immp1l; mouse.
DR PRO; PR:Q9CQU8; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9CQU8; protein.
DR Bgee; ENSMUSG00000042670; Expressed in animal zygote and 63 other tissues.
DR Genevisible; Q9CQU8; MM.
DR GO; GO:0042720; C:mitochondrial inner membrane peptidase complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IBA:GO_Central.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR CDD; cd06530; S26_SPase_I; 1.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR InterPro; IPR019533; Peptidase_S26.
DR Pfam; PF10502; Peptidase_S26; 2.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; SSF51306; 1.
DR TIGRFAMs; TIGR02227; sigpep_I_bact; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Membrane; Mitochondrion; Mitochondrion inner membrane; Protease;
KW Reference proteome.
FT CHAIN 1..166
FT /note="Mitochondrial inner membrane protease subunit 1"
FT /id="PRO_0000259574"
FT ACT_SITE 40
FT /evidence="ECO:0000250"
FT ACT_SITE 83
FT /evidence="ECO:0000250"
FT CONFLICT 94
FT /note="L -> F (in Ref. 1; BAE40162)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="D -> A (in Ref. 1; BAE40162)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 166 AA; 18502 MW; 5627EE1F1BD80E3D CRC64;
MLRGVLGKAF RLAGYTIQYG CIAHCAFEYV GGVVMCSGPS MEPTIQNSDI VFAENLSRHF
YGIQRGDIVI AKSPSDPKSN ICKRVIGLEG DKILSTSPSD VFKSRSYVPT GHVWLEGDNL
QNSTDSRYYG PIPYGLIRGR IFFKIWPFSD FGFLRDSPNG QRFSDD
