ID F7BVQ5_CALJA Unreviewed; 1038 AA.
AC F7BVQ5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Presequence protease, mitochondrial {ECO:0000256|ARBA:ARBA00020167};
DE AltName: Full=Pitrilysin metalloproteinase 1 {ECO:0000256|ARBA:ARBA00032857};
GN Name=PITRM1 {ECO:0000313|Ensembl:ENSCJAP00000037981.4};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000037981.4, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000037981.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000037981.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBUNIT: Monomer and homodimer; homodimerization is induced by binding
CC of the substrate. {ECO:0000256|ARBA:ARBA00011853}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. PreP subfamily.
CC {ECO:0000256|ARBA:ARBA00007575}.
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DR AlphaFoldDB; F7BVQ5; -.
DR STRING; 9483.ENSCJAP00000037981; -.
DR Ensembl; ENSCJAT00000040122.5; ENSCJAP00000037981.4; ENSCJAG00000020425.5.
DR eggNOG; KOG2019; Eukaryota.
DR GeneTree; ENSGT00390000018381; -.
DR InParanoid; F7BVQ5; -.
DR OMA; NYLYYIR; -.
DR TreeFam; TF300333; -.
DR Proteomes; UP000008225; Chromosome 7.
DR Bgee; ENSCJAG00000020425; Expressed in heart and 6 other cell types or tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:Ensembl.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR013578; Peptidase_M16C_assoc.
DR PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR PANTHER; PTHR43016:SF13; PRESEQUENCE PROTEASE, MITOCHONDRIAL; 1.
DR Pfam; PF08367; M16C_assoc; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SMART; SM01264; M16C_associated; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000008225}.
FT DOMAIN 504..753
FT /note="Peptidase M16C associated"
FT /evidence="ECO:0000259|SMART:SM01264"
FT REGION 804..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1038 AA; 117410 MW; 891277B8E72798C2 CRC64;
MWRCGGRPGL LTLRQLSGGH AYHKAWRWSS TRACERALQY QVGDKIHGFT VNQVTSVPEL
FLTAVKLSHD DTGARYLHLA REDTNNLFSV QFRTTPMDST GVPHILEHTV LCGSQKYPCR
DPFFKMLNRS LSTFMNAFTA SDYTLYPFST QNPKDFQNLL SVYLDATFFP CLRELDFWQE
GWRLEHENPS DPQTPLVFKG VVFNEMKGVF TDNERIFSQH LQNRLLPDHT YSVVSGGDPL
CIPELTWEQL KQFHATHYHP SNARFFTYGN FPLEQHLKQI QEEALSKFQK IEPSTAVPAQ
TPWDKPREFQ ITCGPDSLAT DPSKQRTVSV SFLLPDITDT FEAFTLSLLS SLLISGPNSP
FYKALIESGL GTDFSPDVGY NGYTREAYFS VGLQGIAEKD IETVRSLVDR TIDEVIEKGF
EDERIEALLH KIEIQMKHQS TSFGLTLTSY IASCWNHDGD PVELLKLGNQ LAKFRQCLQE
NPKFLEEKVK QYFKNNQHKL TLSMRPDDKY REKQAQVEAT KLKQKVEALS PRDRQQIYEK
GLELRTRQSK PQDASCLPAL KVSDIEPTIP ATELDVVLTA GDIPVQYCSQ PTNGMVYFRA
FCSLNTLPEE LRPYVPLFCS VLTKLGCGLL DYREQAQQIE LKTGGMSASP HVLPDDSHMD
TYEQVGVLFS SHCLDRNLSD MMHLWSEIFN NPCFEEEEHF KVLVKMTAQE LANGIPDSGH
LYASIRAGRT LTPAGDLREA FSGMDQVRLM KRIAEMTDIK PILRKLPRIK KHLLNGDNMR
CSVNATPQQM AETEKVVENF LRNIGRSKKE RRPVRPHVVE KPAPSSPGGD AHTPNGSQII
RKLVMEPTFK PWQMKTHFLM PFPVNYVGEC IRTVPYTDPD HASLKILACL MTAKFLHTEI
REKGGAYAGG AKLSHNGIFT FYSYRDPNTM ETLQSFGKAV DWAKSGKFTQ QDIDEAKLSA
FSTVDAPVAP SDKGMDHFLS GLSDDMKQAH REQLFAVSRD KLLAVSDRYL GTGKSTHGLA
ILGPENAKIA KDPSWIVS
//