ID A0A3Q3W6D1_MOLML Unreviewed; 527 AA.
AC A0A3Q3W6D1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Metalloendopeptidase OMA1, mitochondrial {ECO:0000256|ARBA:ARBA00040360};
DE AltName: Full=Overlapping with the m-AAA protease 1 homolog {ECO:0000256|ARBA:ARBA00042978};
OS Mola mola (Ocean sunfish) (Tetraodon mola).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Molidae; Mola.
OX NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000004139.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000004139.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBUNIT: Homooligomer. {ECO:0000256|ARBA:ARBA00011182}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004434}.
CC -!- SIMILARITY: Belongs to the peptidase M48 family.
CC {ECO:0000256|ARBA:ARBA00038233}.
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DR AlphaFoldDB; A0A3Q3W6D1; -.
DR STRING; 94237.ENSMMOP00000004139; -.
DR Ensembl; ENSMMOT00000004215.1; ENSMMOP00000004139.1; ENSMMOG00000003303.1.
DR OMA; FDRPYNR; -.
DR Proteomes; UP000261620; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07331; M48C_Oma1_like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR001915; Peptidase_M48.
DR PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR PANTHER; PTHR22726:SF1; METALLOENDOPEPTIDASE OMA1, MITOCHONDRIAL; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000261620};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 158..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 236..421
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 527 AA; 58446 MW; C7592A2B6A5CB70A CRC64;
MVLICFNLFR SRRLFSLPAH LTRDLRVCQQ AGCPLKRPHT VSCQISCQRT ANRVRATPTG
PPLLACSGGR WAYGLKIGPR TGSALHSAPV RTQCPVSGHR FHTSAPARAL PLVYLWLVLK
PLQKLMAIIL GRSLRMWWGT LPANRWQLMR EWVWQRRWRL AGVASVAMVI VFLFLLTHLD
ECPVTGRTRL LVFNRESYME LAVLTSEEWN SVSCMEEFAE LLVPVSDPRH KAVELLVQHL
QLRNKDIPEM SDISWNVHVV ESPTVNAFVI PNGEIFMFTG MLDTVADIHQ LTIILGHEMA
HVLLAHSVEE ASLSHIVDLL SLILLAAIWA VCPRDSLALL GQWVQGKLSQ LMFSRPYSRK
LEVEADQVGM LLAAKACADV RAGPVLWQQM EITDQLSGEL NVPEWLSTHP SHRNRVTQLD
RLVPQALELR ESCGCPALPA TDPRTIFSKS VQVLLDNAQD KGREGQEGSR KVHQTQSLAS
LTAALPAALL DPNAPSNVDR ESKVLPVVSE AAAAAPVPAP PEGEGSQ
//
