OMA1_SCHPO
ID OMA1_SCHPO Reviewed; 337 AA.
AC Q9P7G4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Mitochondrial metalloendopeptidase OMA1 {ECO:0000305};
DE EC=3.4.24.- {ECO:0000250|UniProtKB:P36163};
GN Name=oma1 {ECO:0000312|PomBase:SPAP14E8.04}; ORFNames=SPAP14E8.04;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Protease that is part of the quality control system in the
CC inner membrane of mitochondria. Cleaves and thereby promotes the
CC turnover of mistranslated or misfolded membrane protein.
CC {ECO:0000250|UniProtKB:P36163}.
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 induced in response to
CC various mitochondrial stress. {ECO:0000250|UniProtKB:P36163}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P36163}; Single-pass membrane protein
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase M48 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB77005.1; -; Genomic_DNA.
DR RefSeq; NP_593540.1; NM_001018974.2.
DR AlphaFoldDB; Q9P7G4; -.
DR SMR; Q9P7G4; -.
DR BioGRID; 278405; 1.
DR STRING; 4896.SPAP14E8.04.1; -.
DR MaxQB; Q9P7G4; -.
DR PaxDb; Q9P7G4; -.
DR EnsemblFungi; SPAP14E8.04.1; SPAP14E8.04.1:pep; SPAP14E8.04.
DR GeneID; 2541915; -.
DR KEGG; spo:SPAP14E8.04; -.
DR PomBase; SPAP14E8.04; oma1.
DR VEuPathDB; FungiDB:SPAP14E8.04; -.
DR eggNOG; KOG2661; Eukaryota.
DR HOGENOM; CLU_029002_1_0_1; -.
DR InParanoid; Q9P7G4; -.
DR OMA; NVCRSED; -.
DR PhylomeDB; Q9P7G4; -.
DR Reactome; R-SPO-169911; Regulation of Apoptosis.
DR PRO; PR:Q9P7G4; -.
DR Proteomes; UP000002485; Chromosome I.
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; ISS:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISS:PomBase.
DR GO; GO:0034982; P:mitochondrial protein processing; IBA:GO_Central.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; ISS:PomBase.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR InterPro; IPR001915; Peptidase_M48.
DR Pfam; PF01435; Peptidase_M48; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Mitochondrion; Mitochondrion inner membrane; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..337
FT /note="Mitochondrial metalloendopeptidase OMA1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000302811"
FT TOPO_DOM 1..68
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..337
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT ACT_SITE 196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT DISULFID 265..321
FT /evidence="ECO:0000250|UniProtKB:P36163"
SQ SEQUENCE 337 AA; 38610 MW; A31E2DF43172E3C3 CRC64;
MFLNKYISNY SRTRAVSCAP VLSYKKCSYR NFNGLLQARF QSNNLSWSNR NRVVYKSFQP
NPRDKRFQWI FGALIAGGGV YYFTHLEYVP ISNRRRFNDV SLDFEKRMAQ DAYKEVMSEY
GDRMLPSYHP TTLYVSRVLK RIIAVSGMSD LKWELHVIRD PTPNAFVLPG GKVFVFEGIL
PMCKGEDGLA AVLAHETAHQ VARHSAEKIA FTRAVSCIVF LAAASLDLSG QLSHFLLNFG
LLLPFSRKME TEADYIGLML MSQACFDPNA AKTLWERMDA AEGQMGKALA FASTHPSSKK
RIRKIEEWLP EAQVKRETSD CYHETWPMLQ SFKEVHW
