ID A0A212CXX6_CEREH Unreviewed; 525 AA.
AC A0A212CXX6;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Mitochondrial-processing peptidase subunit alpha {ECO:0000256|ARBA:ARBA00016741};
DE AltName: Full=Alpha-MPP {ECO:0000256|ARBA:ARBA00030006};
DE AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000256|ARBA:ARBA00032315};
GN ORFNames=Celaphus_00005085 {ECO:0000313|EMBL:OWK10806.1};
OS Cervus elaphus hippelaphus (European red deer).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC Cervinae; Cervus.
OX NCBI_TaxID=46360 {ECO:0000313|EMBL:OWK10806.1, ECO:0000313|Proteomes:UP000242450};
RN [1] {ECO:0000313|Proteomes:UP000242450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=29294181;
RA Bana N.A., Nyiri A., Nagy J., Frank K., Nagy T., Steger V., Schiller M.,
RA Lakatos P., Sugar L., Horn P., Barta E., Orosz L.;
RT "The red deer Cervus elaphus genome CerEla1.0: sequencing, annotating,
RT genes, and chromosomes.";
RL Mol. Genet. Genomics 293:665-684(2018).
CC -!- FUNCTION: Substrate recognition and binding subunit of the essential
CC mitochondrial processing protease (MPP), which cleaves the
CC mitochondrial sequence off newly imported precursors proteins.
CC {ECO:0000256|ARBA:ARBA00002123}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|RuleBase:RU004447}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWK10806.1}.
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DR EMBL; MKHE01000011; OWK10806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212CXX6; -.
DR Proteomes; UP000242450; Chromosome 11.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR PANTHER; PTHR11851:SF49; MITOCHONDRIAL-PROCESSING PEPTIDASE SUBUNIT ALPHA; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000242450}.
FT DOMAIN 77..226
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 232..431
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 525 AA; 58223 MW; E1DAE3FCC12D486F CRC64;
MAAMVLAATR LLRGSGSWGR SRLRFGDPAY RRFSSGGAYP NIPLSSPLPG VPKPVFATVD
GQEKFETKVT TLDNGLRVAS QNKFGQFCTV GILINSGSRY EAKYLSGIAH FLEKLAFSST
DQFDSKDEIL LTLEKHGGIC DCQTSRDTTM YAVSADSKGL DTVVGLLADV VLHPRLTDEE
IEMTRMAVQF ELEDLNMRPD PEPLLTEMIH EAAYRENTVG LHRFCPVENI GKIDRDVLHS
YLRNYYTPDR MVLAGVGVEH AQLVECARKY LLGTGPAWGT GAAVHVDRSV AQYTGGIVKL
ERDMSNVSLG PTPFPELTHI MIGLESCSFL EGDFIPFAVL NMMMGGGGSF SAGGPGKGMF
TRLYLNVLNR HHWMYNATSY HHSYEDTGLL CIHASADPRQ VREMVEIITR EFVLMAGTVD
VVELERAKTQ LMSMLMMNLE ARPVIFEDVG RQVLATRSRK LPHELCALIR DVKPEDIKRV
ASKMLRGKPA VAALGDLSEL PAYEHVQTAL ASRDGRLPRT YRLFR
//
