OMA1_CANAL
ID OMA1_CANAL Reviewed; 336 AA.
AC Q5A663;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, 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:0000303|PubMed:27325672};
GN OrderedLocusNames=CAALFM_C404550CA; ORFNames=orf19.3827;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27325672; DOI=10.1128/mcb.00156-16;
RA Bohovych I., Kastora S., Christianson S., Topil D., Kim H., Fangman T.,
RA Zhou Y.J., Barrientos A., Lee J., Brown A.J., Khalimonchuk O.;
RT "Oma1 links mitochondrial protein quality control and TOR signaling to
RT modulate physiological plasticity and cellular stress responses.";
RL Mol. Cell. Biol. 36:2300-2312(2016).
CC -!- FUNCTION: Protease that is part of the quality control system in the
CC inner membrane of mitochondria (By similarity). Cleaves and thereby
CC promotes the turnover of mistranslated or misfolded membrane protein
CC (By similarity). Required for TOR signaling (PubMed:27325672).
CC {ECO:0000250|UniProtKB:P36163, ECO:0000269|PubMed:27325672}.
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:0000250|UniProtKB:P36163}.
CC -!- DISRUPTION PHENOTYPE: Cells are resistant to rapamycin and display
CC reduced TOR signaling. {ECO:0000269|PubMed:27325672}.
CC -!- SIMILARITY: Belongs to the peptidase M48 family. {ECO:0000305}.
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DR EMBL; CP017626; AOW29202.1; -; Genomic_DNA.
DR RefSeq; XP_717231.1; XM_712138.2.
DR AlphaFoldDB; Q5A663; -.
DR SMR; Q5A663; -.
DR STRING; 237561.Q5A663; -.
DR MEROPS; M48.018; -.
DR EnsemblFungi; KHC76546; KHC76546; W5Q_03757.
DR GeneID; 3641106; -.
DR KEGG; cal:CAALFM_C404550CA; -.
DR CGD; CAL0000185639; OMA1.
DR VEuPathDB; FungiDB:C4_04550C_A; -.
DR eggNOG; KOG2661; Eukaryota.
DR HOGENOM; CLU_029002_1_0_1; -.
DR InParanoid; Q5A663; -.
DR OMA; NVCRSED; -.
DR OrthoDB; 960152at2759; -.
DR PHI-base; PHI:7048; -.
DR Proteomes; UP000000559; Chromosome 4.
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; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0035694; P:mitochondrial protein catabolic process; IEA:EnsemblFungi.
DR GO; GO:0034982; P:mitochondrial protein processing; IBA:GO_Central.
DR GO; GO:0033108; P:mitochondrial respiratory chain complex assembly; IEA:EnsemblFungi.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0051775; P:response to redox state; IEA:EnsemblFungi.
DR GO; GO:0031929; P:TOR signaling; IMP:CGD.
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..336
FT /note="Mitochondrial metalloendopeptidase OMA1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000450321"
FT TOPO_DOM 17..154
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 155..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..336
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT ACT_SITE 186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT DISULFID 254..320
FT /evidence="ECO:0000250|UniProtKB:P36163"
SQ SEQUENCE 336 AA; 38971 MW; 9444C2A2A305FB01 CRC64;
MFGSKIFSRL FFKRTYATYK RFDNTTSSSS FTTSYAHLLT NRKTLYIGGG LLGFYVYNLH
DAPYTHRSRF IWVPYWLETK IGDYSYRQIY QQFQSQILPH SNPLYNRVST IMNKLLDVAL
NDNINDDLNA RFLNHLKSLK WEINIIQNDS LPPNAFILPN GKIFIFSSIM PICKNEDGLA
TVLSHELSHQ LAQHSSEQLS KQPIYMVLST ILYTITGVSW FNDLLINGVL TMSASREMES
EADHIGCELL ARACFNPQES INFWHRMSQA EKKAAGIVSQ EGGYLNTWEF FSTHPATSRR
IADIQKWMPQ LLQIRESSGC YEYGRFYNFN KSYFSH
