ID A0A674P768_TAKRU Unreviewed; 504 AA.
AC A0A674P768;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 18.
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};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000081503.1, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000081503.1, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000081503.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A674P768; -.
DR Ensembl; ENSTRUT00000083657.1; ENSTRUP00000081503.1; ENSTRUG00000016669.3.
DR GeneTree; ENSGT00940000156724; -.
DR Proteomes; UP000005226; Chromosome 21.
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:UP000005226}.
FT DOMAIN 96..245
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 252..452
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 504 AA; 55254 MW; 75DF41B9FB556D0A CRC64;
IFISSSSSSS SSSSSSSSNS SVCGSSSTSR SLVCAGSSSL SFYHHPAYRK YSSSGGGYPN
ISLSTPLQGL PRPVFASVDG QEKYETKITT LENGLKVASQ NKFGQFCTVG ILVNSGSRHE
AKYPSGIAHF LEKLAFSSTA QYGSKDEILL TLEKHGGICD CQASRDTTMY AVSAEVKGLD
TVVSLLSDAV LQPRLLDEEI EMTRMAVRFE LEDLNMRPDP EPLLTEMIHA AAYRGNTVGL
PRFCPVNNID KIDKGVLHSY LQNYYSPERM VLAGVGIEHE QLVDCARKYL LNVKPVWGTS
SGANVDCSVA QYTGGIVKIE KDMSDVSLGP TPIPELTHIM IGLESCSFLE EDFIPFAVLN
MMMGGGGSFS AGGPGKGMFT RLYLNVLNRH HWMYNATSYH HSYEDSGLLC IHASADPRQV
REMVEIITRE FIQMAGNAGE VVMELERAKT QLKSMLMMNL ESRPVIFEDV GRQVLSTGRR
KLPHELCDLI SESSIYQRLQ KIPL
//
