OMA1_MOUSE
ID OMA1_MOUSE Reviewed; 521 AA.
AC Q9D8H7; Q3UWN9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Metalloendopeptidase OMA1, mitochondrial {ECO:0000305};
DE EC=3.4.24.- {ECO:0000269|PubMed:20038678, ECO:0000269|PubMed:24550258, ECO:0000269|PubMed:24719224};
DE AltName: Full=Overlapping with the m-AAA protease 1 homolog {ECO:0000303|PubMed:20038678};
DE Flags: Precursor;
GN Name=Oma1 {ECO:0000303|PubMed:20038678, ECO:0000312|MGI:MGI:1914263};
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Egg, and Small intestine;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, ACTIVE SITE, CATALYTIC ACTIVITY,
RP SUBUNIT, SUBCELLULAR LOCATION, ACTIVITY REGULATION, PROTEOLYTIC CLEAVAGE,
RP DOMAIN, TOPOLOGY, AND MUTAGENESIS OF GLU-324.
RX PubMed=24550258; DOI=10.1002/embj.201386474;
RA Baker M.J., Lampe P.A., Stojanovski D., Korwitz A., Anand R., Tatsuta T.,
RA Langer T.;
RT "Stress-induced OMA1 activation and autocatalytic turnover regulate OPA1-
RT dependent mitochondrial dynamics.";
RL EMBO J. 33:578-593(2014).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20038678; DOI=10.1083/jcb.200906084;
RA Ehses S., Raschke I., Mancuso G., Bernacchia A., Geimer S., Tondera D.,
RA Martinou J.C., Westermann B., Rugarli E.I., Langer T.;
RT "Regulation of OPA1 processing and mitochondrial fusion by m-AAA protease
RT isoenzymes and OMA1.";
RL J. Cell Biol. 187:1023-1036(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
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).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22433842; DOI=10.1038/emboj.2012.70;
RA Quiros P.M., Ramsay A.J., Sala D., Fernandez-Vizarra E., Rodriguez F.,
RA Peinado J.R., Fernandez-Garcia M.S., Vega J.A., Enriquez J.A., Zorzano A.,
RA Lopez-Otin C.;
RT "Loss of mitochondrial protease OMA1 alters processing of the GTPase OPA1
RT and causes obesity and defective thermogenesis in mice.";
RL EMBO J. 31:2117-2133(2012).
RN [8]
RP FUNCTION, ACTIVE SITE, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PROTEOLYTIC
RP CLEAVAGE, AND MUTAGENESIS OF GLU-324.
RX PubMed=24719224; DOI=10.1002/embr.201338240;
RA Zhang K., Li H., Song Z.;
RT "Membrane depolarization activates the mitochondrial protease OMA1 by
RT stimulating self-cleavage.";
RL EMBO Rep. 15:576-585(2014).
RN [9]
RP FUNCTION.
RX PubMed=24616225; DOI=10.1083/jcb.201308006;
RA Anand R., Wai T., Baker M.J., Kladt N., Schauss A.C., Rugarli E.,
RA Langer T.;
RT "The i-AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial
RT fusion and fission.";
RL J. Cell Biol. 204:919-929(2014).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26785494; DOI=10.1126/science.aad0116;
RA Wai T., Garcia-Prieto J., Baker M.J., Merkwirth C., Benit P., Rustin P.,
RA Ruperez F.J., Barbas C., Ibanez B., Langer T.;
RT "Imbalanced OPA1 processing and mitochondrial fragmentation cause heart
RT failure in mice.";
RL Science 350:116-116(2015).
RN [11]
RP FUNCTION.
RX PubMed=26365306; DOI=10.1038/srep13989;
RA Bohovych I., Fernandez M.R., Rahn J.J., Stackley K.D., Bestman J.E.,
RA Anandhan A., Franco R., Claypool S.M., Lewis R.E., Chan S.S.,
RA Khalimonchuk O.;
RT "metalloprotease OMA1 fine-tunes mitochondrial bioenergetic function and
RT respiratory supercomplex stability.";
RL Sci. Rep. 5:13989-13989(2015).
RN [12]
RP FUNCTION.
RX PubMed=26783299; DOI=10.1083/jcb.201507022;
RA Korwitz A., Merkwirth C., Richter-Dennerlein R., Troeder S.E.,
RA Sprenger H.G., Quiros P.M., Lopez-Otin C., Rugarli E.I., Langer T.;
RT "Loss of OMA1 delays neurodegeneration by preventing stress-induced OPA1
RT processing in mitochondria.";
RL J. Cell Biol. 212:157-166(2016).
RN [13]
RP DISRUPTION PHENOTYPE.
RX PubMed=29593106; DOI=10.1126/scitranslmed.aan4935;
RA Acin-Perez R., Lechuga-Vieco A.V., Del Mar Munoz M., Nieto-Arellano R.,
RA Torroja C., Sanchez-Cabo F., Jimenez C., Gonzalez-Guerra A., Carrascoso I.,
RA Beninca C., Quiros P.M., Lopez-Otin C., Castellano J.M., Ruiz-Cabello J.,
RA Jimenez-Borreguero L.J., Enriquez J.A.;
RT "Ablation of the stress protease OMA1 protects against heart failure in
RT mice.";
RL Sci. Transl. Med. 10:0-0(2018).
RN [14]
RP PROTEOLYTIC CLEAVAGE, AND LIPID-BINDING.
RX PubMed=31819158; DOI=10.1038/s41418-019-0469-4;
RA Anderson C.J., Kahl A., Fruitman H., Qian L., Zhou P., Manfredi G.,
RA Iadecola C.;
RT "Prohibitin levels regulate OMA1 activity and turnover in neurons.";
RL Cell Death Differ. 27:1896-1906(2020).
CC -!- FUNCTION: Metalloprotease that is part of the quality control system in
CC the inner membrane of mitochondria (PubMed:20038678, PubMed:22433842,
CC PubMed:24550258, PubMed:24719224, PubMed:24616225, PubMed:26785494).
CC Activated in response to various mitochondrial stress, leading to the
CC proteolytic cleavage of target proteins, such as OPA1, UQCC3 and DELE1
CC (PubMed:20038678, PubMed:22433842, PubMed:24550258, PubMed:24616225,
CC PubMed:26785494). Following stress conditions that induce loss of
CC mitochondrial membrane potential, mediates cleavage of OPA1 at S1
CC position, leading to OPA1 inactivation and negative regulation of
CC mitochondrial fusion (PubMed:20038678, PubMed:22433842,
CC PubMed:24550258, PubMed:24616225, PubMed:26785494, PubMed:26783299).
CC Also acts as a regulator of apoptosis: upon BAK and BAX aggregation,
CC mediates cleavage of OPA1, leading to the remodeling of mitochondrial
CC cristae and allowing the release of cytochrome c from mitochondrial
CC cristae (By similarity). In depolarized mitochondria, may also act as a
CC backup protease for PINK1 by mediating PINK1 cleavage and promoting its
CC subsequent degradation by the proteasome (By similarity). May also
CC cleave UQCC3 in response to mitochondrial depolarization (By
CC similarity). Also acts as an activator of the integrated stress
CC response (ISR): in response to mitochondrial stress, mediates cleavage
CC of DELE1 to generate the processed form of DELE1 (S-DELE1), which
CC translocates to the cytosol and activates EIF2AK1/HRI to trigger the
CC ISR (By similarity). Its role in mitochondrial quality control is
CC essential for regulating lipid metabolism as well as to maintain body
CC temperature and energy expenditure under cold-stress conditions
CC (PubMed:22433842). Binds cardiolipin, possibly regulating its protein
CC turnover (PubMed:31819158). Required for the stability of the
CC respiratory supercomplexes (PubMed:26365306).
CC {ECO:0000250|UniProtKB:Q96E52, ECO:0000269|PubMed:20038678,
CC ECO:0000269|PubMed:22433842, ECO:0000269|PubMed:24550258,
CC ECO:0000269|PubMed:24616225, ECO:0000269|PubMed:24719224,
CC ECO:0000269|PubMed:26365306, ECO:0000269|PubMed:26783299,
CC ECO:0000269|PubMed:26785494, ECO:0000269|PubMed:31819158}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:O75844};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O75844};
CC -!- ACTIVITY REGULATION: Protease activity is activated upon autocatalytic
CC cleavage in response to mitochondrial depolarization.
CC {ECO:0000269|PubMed:24550258, ECO:0000269|PubMed:24719224}.
CC -!- SUBUNIT: Homooligomer. {ECO:0000269|PubMed:24550258}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:24550258, ECO:0000305|PubMed:20038678}; Single-pass
CC membrane protein {ECO:0000305|PubMed:24550258}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D8H7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D8H7-2; Sequence=VSP_027959, VSP_027960;
CC -!- DOMAIN: The stress-sensor region regulates proteolysis and activation.
CC {ECO:0000269|PubMed:24550258}.
CC -!- PTM: Autocatalytically cleaved in response to mitochondrial
CC depolarization both at the N-terminus and C-terminus to generate the
CC short active form (S-OMA1) (PubMed:24550258, PubMed:24719224).
CC Autocatalytic processing at the C-terminus takes place at residues 443-
CC 452 (PubMed:24719224). The S-OMA1 form is unstable (PubMed:24719224).
CC Degradaded by YMEL1 in response to membrane depolarization (By
CC similarity). Protein turnover is regulated by prohibitin (PHB and
CC PHB2), which promotes degradation of OMA1 in a cardiolipin-binding
CC manner (PubMed:31819158). {ECO:0000250|UniProtKB:Q96E52,
CC ECO:0000269|PubMed:24550258, ECO:0000269|PubMed:24719224,
CC ECO:0000269|PubMed:31819158}.
CC -!- PTM: May form a redox-dependent disulfide bond (By similarity). Exists
CC in a semi-oxidized state and is activated by prolonged hypoxia (By
CC similarity). {ECO:0000250|UniProtKB:P36163,
CC ECO:0000250|UniProtKB:Q96E52}.
CC -!- DISRUPTION PHENOTYPE: Mice develop normally with males and females
CC being fertile (PubMed:22433842). They however display transcriptional
CC changes in genes of lipid and glucose metabolic pathways and
CC substantial alterations in circulating blood parameters
CC (PubMed:22433842). Moreover, mice exhibit an increase in body weight
CC due to increased adipose mass, hepatic steatosis, decreased energy
CC expenditure and impaired thermogenenesis (PubMed:22433842). Mice are
CC protected against heart failure by averting cardiomyocyte death in
CC different murine heart failure models (PubMed:29593106). Mice with a
CC double, cardiomyocyte-specific gene disruption of Yme1l and Oma1 have
CC normal cardiac function and do not display myocardial fibrosis,
CC contrary to mice with a single, cardiomyocyte-specific disruption of
CC Yme1l (PubMed:26785494). Likewise, cardiomyocyte mitochondria have
CC normal morphology (PubMed:26785494). Mice with a skeletal muscle Yme1l
CC gene disruption plus a double, cardiomyocyte-specific gene disruption
CC of Yme1l and Oma1 display normal glucose tolerance (PubMed:26785494).
CC {ECO:0000269|PubMed:22433842, ECO:0000269|PubMed:26785494,
CC ECO:0000269|PubMed:29593106}.
CC -!- SIMILARITY: Belongs to the peptidase M48 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK008020; BAB25414.1; -; mRNA.
DR EMBL; AK076209; BAC36255.1; -; mRNA.
DR EMBL; AK136208; BAE22875.1; -; mRNA.
DR EMBL; AL772338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016238; AAH16238.1; -; mRNA.
DR CCDS; CCDS18412.1; -. [Q9D8H7-1]
DR RefSeq; NP_080185.1; NM_025909.3. [Q9D8H7-1]
DR RefSeq; XP_006503362.1; XM_006503299.3. [Q9D8H7-1]
DR RefSeq; XP_006503363.1; XM_006503300.3. [Q9D8H7-1]
DR AlphaFoldDB; Q9D8H7; -.
DR SMR; Q9D8H7; -.
DR STRING; 10090.ENSMUSP00000045269; -.
DR MEROPS; M48.017; -.
DR iPTMnet; Q9D8H7; -.
DR PhosphoSitePlus; Q9D8H7; -.
DR EPD; Q9D8H7; -.
DR MaxQB; Q9D8H7; -.
DR PaxDb; Q9D8H7; -.
DR PeptideAtlas; Q9D8H7; -.
DR PRIDE; Q9D8H7; -.
DR ProteomicsDB; 294198; -. [Q9D8H7-1]
DR ProteomicsDB; 294199; -. [Q9D8H7-2]
DR Antibodypedia; 46900; 96 antibodies from 25 providers.
DR DNASU; 67013; -.
DR Ensembl; ENSMUST00000035780; ENSMUSP00000045269; ENSMUSG00000035069. [Q9D8H7-1]
DR GeneID; 67013; -.
DR KEGG; mmu:67013; -.
DR UCSC; uc008txq.1; mouse. [Q9D8H7-1]
DR CTD; 115209; -.
DR MGI; MGI:1914263; Oma1.
DR VEuPathDB; HostDB:ENSMUSG00000035069; -.
DR eggNOG; KOG2661; Eukaryota.
DR GeneTree; ENSGT00390000007027; -.
DR HOGENOM; CLU_039633_0_0_1; -.
DR InParanoid; Q9D8H7; -.
DR OMA; ILGQWIQ; -.
DR OrthoDB; 960152at2759; -.
DR PhylomeDB; Q9D8H7; -.
DR TreeFam; TF329133; -.
DR Reactome; R-MMU-169911; Regulation of Apoptosis.
DR BioGRID-ORCS; 67013; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Oma1; mouse.
DR PRO; PR:Q9D8H7; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9D8H7; protein.
DR Bgee; ENSMUSG00000035069; Expressed in interventricular septum and 251 other tissues.
DR Genevisible; Q9D8H7; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
DR GO; GO:0042407; P:cristae formation; IGI:MGI.
DR GO; GO:0002024; P:diet induced thermogenesis; IMP:UniProtKB.
DR GO; GO:0097009; P:energy homeostasis; IMP:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; IMP:UniProtKB.
DR GO; GO:0140468; P:HRI-mediated signaling; ISS:UniProtKB.
DR GO; GO:0140467; P:integrated stress response signaling; ISS:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IMP:UniProtKB.
DR GO; GO:0034982; P:mitochondrial protein processing; IDA:UniProtKB.
DR GO; GO:0033108; P:mitochondrial respiratory chain complex assembly; IMP:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IGI:MGI.
DR GO; GO:0010637; P:negative regulation of mitochondrial fusion; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0016540; P:protein autoprocessing; IDA:UniProtKB.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; ISO:MGI.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:1903850; P:regulation of cristae formation; ISS:UniProtKB.
DR GO; GO:0031638; P:zymogen activation; IDA:UniProtKB.
DR InterPro; IPR001915; Peptidase_M48.
DR Pfam; PF01435; Peptidase_M48; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autocatalytic cleavage; Direct protein sequencing;
KW Disulfide bond; Hydrolase; Lipid-binding; Membrane; Metal-binding;
KW Metalloprotease; Mitochondrion; Mitochondrion inner membrane; Protease;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Zinc; Zymogen.
FT TRANSIT 1..79
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT PROPEP 80..139
FT /evidence="ECO:0000305|PubMed:24550258"
FT /id="PRO_0000450315"
FT CHAIN 140..?
FT /note="Metalloendopeptidase OMA1, mitochondrial"
FT /id="PRO_0000302810"
FT PROPEP ?..521
FT /evidence="ECO:0000305|PubMed:24719224"
FT /id="PRO_0000450316"
FT TOPO_DOM 140..191
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:24550258"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..?
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:24550258"
FT REGION 144..163
FT /note="Cardiolipin-binding"
FT /evidence="ECO:0000269|PubMed:31819158"
FT REGION 161..191
FT /note="Stress-sensor region"
FT /evidence="ECO:0000269|PubMed:24550258"
FT ACT_SITE 324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT ECO:0000305|PubMed:24550258, ECO:0000305|PubMed:24719224"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 327
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 388
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT DISULFID 403..461
FT /evidence="ECO:0000250|UniProtKB:P36163"
FT VAR_SEQ 226..231
FT /note="KEHFRL -> ESWAP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027959"
FT VAR_SEQ 232..521
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027960"
FT MUTAGEN 324
FT /note="E->Q: Abolished protease activity and ability to
FT cleave OPA1. Abolished autocatalytic processing."
FT /evidence="ECO:0000269|PubMed:24550258,
FT ECO:0000269|PubMed:24719224"
FT CONFLICT 137
FT /note="R -> M (in Ref. 1; BAE22875)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 521 AA; 58878 MW; 80BCBFA70C9E2D5F CRC64;
MSLLYGLQST RINRFLSGVN NLANRRQWTP PASCPLAPKL RAVNAYWGLN TVSHCHSVTL
LPRNFLFCRT LNHKKSRCLS SAQSKELGVL TYRCTVRGDS VLRQGARKVA GVPALAASCS
PSCPAVIEAR SFRTSARVQA APVPLLLLIL KPVQKLLAII VGRGIRKWWQ ALPPNKKELF
KDSVRKNKWR LLLGLSAFGL LFVVFYFTHL EVSPVTGRSK LLLVGKEHFR LLSDLEYEVW
MEEFKNDLLP ERDPRYLTVK EMVYHLTQCN RDVPGISETN WVVHVVDSPA VNAFVLPNGQ
VFIFTGLLNS VTDVHQLSFL LGHEIAHAVL GHAAEKASLV HLLDFLGMIF LTMIWAICPR
DSLAVLGQWI QSKLQEYMFD RPYSRTLEAE ADKVGLQLAA KACADVRASS VFWQQMEFSE
SLHGYPKLPE WLSTHPSHGN RAEYLDRLIP QALKLREVCN CPPLSGPDPR LLFRLTVKRF
LEDSEKEDLN ITVKKQKTDA LPMQKQEQIP LTYVLEKRTA G
