IMP2L_HUMAN
ID IMP2L_HUMAN Reviewed; 175 AA.
AC Q96T52; Q75MF1; Q75MN9; Q75MP0; Q75MS5; Q75MS8; Q96HJ2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Mitochondrial inner membrane protease subunit 2;
DE EC=3.4.21.-;
DE AltName: Full=IMP2-like protein;
GN Name=IMMP2L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), POSSIBLE INVOLVEMENT IN GTS, AND
RP TISSUE SPECIFICITY.
RX PubMed=11254443; DOI=10.1086/319523;
RA Petek E., Windpassinger C., Vincent J.B., Cheung J., Boright A.P.,
RA Scherer S.W., Kroisel P.M., Wagner K.;
RT "Disruption of a novel gene (IMMP2L) by a breakpoint in 7q31 associated
RT with Tourette syndrome.";
RL Am. J. Hum. Genet. 68:848-858(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15814844; DOI=10.1091/mbc.e04-12-1086;
RA Burri L., Strahm Y., Hawkins C.J., Gentle I.E., Puryer M.A., Verhagen A.,
RA Callus B., Vaux D., Lithgow T.;
RT "Mature DIABLO/Smac is produced by the IMP protease complex on the
RT mitochondrial inner membrane.";
RL Mol. Biol. Cell 16:2926-2933(2005).
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:0000269|PubMed:15814844}.
CC -!- SUBUNIT: Heterodimer of 2 subunits, IMMPL1 and IMMPL2. {ECO:0000250}.
CC -!- INTERACTION:
CC Q96T52-2; Q99732: LITAF; NbExp=3; IntAct=EBI-25907627, EBI-725647;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:15814844}; Single-pass membrane protein
CC {ECO:0000305|PubMed:15814844}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96T52-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96T52-2; Sequence=VSP_021474, VSP_021475;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested except adult liver
CC and lung. {ECO:0000269|PubMed:11254443}.
CC -!- DISEASE: Gilles de la Tourette syndrome (GTS) [MIM:137580]: Neurologic
CC disorder manifested particularly by motor and vocal tics and associated
CC with behavioral abnormalities. {ECO:0000269|PubMed:11254443}. Note=The
CC disease may be caused by variants affecting the gene represented in
CC this entry.
CC -!- SIMILARITY: Belongs to the peptidase S26 family. IMP2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF359563; AAK52905.1; -; mRNA.
DR EMBL; AC005161; AAS07432.1; -; Genomic_DNA.
DR EMBL; AC005166; AAS02043.1; -; Genomic_DNA.
DR EMBL; AC006392; AAS07496.1; -; Genomic_DNA.
DR EMBL; AC006392; AAS07497.1; -; Genomic_DNA.
DR EMBL; AC073326; AAS07528.1; -; Genomic_DNA.
DR EMBL; BC008497; AAH08497.1; -; mRNA.
DR CCDS; CCDS5753.1; -. [Q96T52-1]
DR CCDS; CCDS87540.1; -. [Q96T52-2]
DR RefSeq; NP_001231535.1; NM_001244606.1. [Q96T52-1]
DR RefSeq; NP_115938.1; NM_032549.3. [Q96T52-1]
DR RefSeq; XP_005250687.1; XM_005250630.3.
DR RefSeq; XP_016868194.1; XM_017012705.1.
DR AlphaFoldDB; Q96T52; -.
DR SMR; Q96T52; -.
DR BioGRID; 123826; 383.
DR ComplexPortal; CPX-6244; Mitochondrial inner membrane peptidase complex.
DR IntAct; Q96T52; 382.
DR MINT; Q96T52; -.
DR STRING; 9606.ENSP00000384966; -.
DR MEROPS; S26.A09; -.
DR iPTMnet; Q96T52; -.
DR PhosphoSitePlus; Q96T52; -.
DR BioMuta; IMMP2L; -.
DR DMDM; 74752143; -.
DR EPD; Q96T52; -.
DR jPOST; Q96T52; -.
DR MassIVE; Q96T52; -.
DR MaxQB; Q96T52; -.
DR PaxDb; Q96T52; -.
DR PeptideAtlas; Q96T52; -.
DR PRIDE; Q96T52; -.
DR ProteomicsDB; 78187; -. [Q96T52-1]
DR ProteomicsDB; 78188; -. [Q96T52-2]
DR Antibodypedia; 17351; 139 antibodies from 28 providers.
DR DNASU; 83943; -.
DR Ensembl; ENST00000331762.7; ENSP00000329553.3; ENSG00000184903.10. [Q96T52-1]
DR Ensembl; ENST00000405709.7; ENSP00000384966.2; ENSG00000184903.10. [Q96T52-1]
DR Ensembl; ENST00000447215.5; ENSP00000388327.1; ENSG00000184903.10. [Q96T52-2]
DR Ensembl; ENST00000452895.5; ENSP00000399353.1; ENSG00000184903.10. [Q96T52-1]
DR GeneID; 83943; -.
DR KEGG; hsa:83943; -.
DR MANE-Select; ENST00000405709.7; ENSP00000384966.2; NM_032549.4; NP_115938.1.
DR UCSC; uc003vfq.3; human. [Q96T52-1]
DR CTD; 83943; -.
DR DisGeNET; 83943; -.
DR GeneCards; IMMP2L; -.
DR HGNC; HGNC:14598; IMMP2L.
DR HPA; ENSG00000184903; Low tissue specificity.
DR MIM; 137580; phenotype.
DR MIM; 605977; gene.
DR neXtProt; NX_Q96T52; -.
DR OpenTargets; ENSG00000184903; -.
DR Orphanet; 856; NON RARE IN EUROPE: Tourette syndrome.
DR PharmGKB; PA134887258; -.
DR VEuPathDB; HostDB:ENSG00000184903; -.
DR eggNOG; KOG1568; Eukaryota.
DR GeneTree; ENSGT00550000075044; -.
DR HOGENOM; CLU_028723_4_1_1; -.
DR InParanoid; Q96T52; -.
DR OMA; IVWPPQR; -.
DR OrthoDB; 1211147at2759; -.
DR PhylomeDB; Q96T52; -.
DR TreeFam; TF315065; -.
DR PathwayCommons; Q96T52; -.
DR SignaLink; Q96T52; -.
DR BioGRID-ORCS; 83943; 11 hits in 1080 CRISPR screens.
DR ChiTaRS; IMMP2L; human.
DR GenomeRNAi; 83943; -.
DR Pharos; Q96T52; Tbio.
DR PRO; PR:Q96T52; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q96T52; protein.
DR Bgee; ENSG00000184903; Expressed in tibialis anterior and 156 other tissues.
DR ExpressionAtlas; Q96T52; baseline and differential.
DR Genevisible; Q96T52; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR GO; GO:0042720; C:mitochondrial inner membrane peptidase complex; ISS:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008015; P:blood circulation; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:Ensembl.
DR GO; GO:0061300; P:cerebellum vasculature development; IEA:Ensembl.
DR GO; GO:0033108; P:mitochondrial respiratory chain complex assembly; IEA:Ensembl.
DR GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
DR GO; GO:0030728; P:ovulation; IEA:Ensembl.
DR GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; ISS:UniProtKB.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:Ensembl.
DR GO; GO:0006465; P:signal peptide processing; IC:ComplexPortal.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0006801; P:superoxide metabolic process; IEA:Ensembl.
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 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Protease; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..175
FT /note="Mitochondrial inner membrane protease subunit 2"
FT /id="PRO_0000259577"
FT TRANSMEM 19..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 43
FT /evidence="ECO:0000250"
FT ACT_SITE 91
FT /evidence="ECO:0000250"
FT VAR_SEQ 103..110
FT /note="TIGHKNRY -> DGRKLKRI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021474"
FT VAR_SEQ 111..175
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021475"
SQ SEQUENCE 175 AA; 19718 MW; F328B36EA1BED29F CRC64;
MAQSQGWVKR YIKAFCKGFF VAVPVAVTFL DRVACVARVE GASMQPSLNP GGSQSSDVVL
LNHWKVRNFE VHRGDIVSLV SPKNPEQKII KRVIALEGDI VRTIGHKNRY VKVPRGHIWV
EGDHHGHSFD SNSFGPVSLG LLHAHATHIL WPPERWQKLE SVLPPERLPV QREEE
