ID A0A2K5IIZ0_COLAP Unreviewed; 524 AA.
AC A0A2K5IIZ0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
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 Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000016427.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000016427.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_011796734.1; XM_011941344.1.
DR AlphaFoldDB; A0A2K5IIZ0; -.
DR STRING; 336983.ENSCANP00000016427; -.
DR Ensembl; ENSCANT00000039365.1; ENSCANP00000016427.1; ENSCANG00000031662.1.
DR GeneID; 105511224; -.
DR CTD; 115209; -.
DR OMA; FDRPYNR; -.
DR OrthoDB; 5490879at2759; -.
DR Proteomes; UP000233080; 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:UP000233080};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 195..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 263..451
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 524 AA; 60209 MW; 7A2C305919F28561 CRC64;
MSFICGLQSA ARNHVFFRFN SLSNWRKCNT LASTSQGCHQ VQVNHIVNKY QGLKVNQCDR
WTFLPGNFHF YRTFNSKRTG CLSSTKNKEI WMITSKCTAW NDSFSRQLLI KEVTAVPSLS
VLHPLSPSPV RAIRNFHTSR RFQAAPVPLL LMILKPVQKL FAIIVGRGIR KWWQALPPTK
KELFKQSIRK NKWKLFLGLS SCGLLFVVFY FTHLEVSPIT GRSKLLLLGK EQFRLLSELE
YEAYMEEFKN DMLTEKDARY LAVKEVLCRL IECNKDVPGI SQINWIIHVV DSPIINAFVL
PNGQMFVFSG LLNSVTDIDQ LSFLLGHEIA HAVLGHAAEK AGMVHFLDFL GMIFLTMIWA
ICPRDSLALL GQWIQSKLQE YMFNRPYSRK LEAEADKIGL LLAAKACVDI RASSVFWQQM
EFVDSLHGLP KMPEWSSTHP SHGNRVEHLD RLIPQALKIR EMCNCPPLSK PDPRLLFKLS
MEHFLEESEK EDLNITKKQK MDTLPVQKQE QIPLTYVVEK RTGS
//
