ID Q2PFU2_MACFA Unreviewed; 514 AA.
AC Q2PFU2; A0A2K5UXB0;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Neurolysin, mitochondrial {ECO:0000256|ARBA:ARBA00039454};
DE EC=3.4.24.16 {ECO:0000256|ARBA:ARBA00039068};
DE AltName: Full=Microsomal endopeptidase {ECO:0000256|ARBA:ARBA00041940};
DE AltName: Full=Mitochondrial oligopeptidase M {ECO:0000256|ARBA:ARBA00042607};
DE AltName: Full=Neurotensin endopeptidase {ECO:0000256|ARBA:ARBA00041659};
GN Name=NLN {ECO:0000313|Ensembl:ENSMFAP00000017108.2};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|EMBL:BAE73028.1};
RN [1] {ECO:0000313|EMBL:BAE73028.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain parietal lobe {ECO:0000313|EMBL:BAE73028.1};
RA Kobayashi M., Tanuma R., Hirata M., Osada N., Kusuda J., Sugano S.,
RA Hashimoto K.;
RT "Analysis of gene expression in cynomolgus monkey tissues by macaque cDNA
RT oligo-chips.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000017108.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSMFAP00000017108.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage in neurotensin: 10-Pro-|-Tyr-11.;
CC EC=3.4.24.16; Evidence={ECO:0000256|ARBA:ARBA00035987};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000256|ARBA:ARBA00004569}.
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR EMBL; AB220495; BAE73028.1; -; mRNA.
DR MEROPS; M03.002; -.
DR Ensembl; ENSMFAT00000067648.2; ENSMFAP00000017108.2; ENSMFAG00000031704.2.
DR VEuPathDB; HostDB:ENSMFAG00000031704; -.
DR GeneTree; ENSGT00950000183171; -.
DR OMA; RSGAWCS; -.
DR OrthoDB; 735202at2759; -.
DR Proteomes; UP000233100; Chromosome 6.
DR Bgee; ENSMFAG00000031704; Expressed in skeletal muscle tissue and 13 other cell types or tissues.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06455; M3A_TOP; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804:SF44; NEUROLYSIN, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 61..510
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 514 AA; 58813 MW; 857C60D130D3A8A9 CRC64;
MKKRMSELCI DFNKNLNEDD TFLVFSKAEL GALPDDFIDS LEKTDDDKYK ITLKYPHYFP
VMKKCCIPET RRRMEMAFNT RCKEENTIIL QQLLPLRAKV AKLLGYSTHA DFVLEMNTAK
STSRVTAFLD DLSQKLKPLG EAEREFILNL KKKECEDRGF EYDGKINAWD LYYYMTQTEE
LKYSIDQEFL KEYFPIEVVT EGLLNTYQEL LGLSFEQVTD AHVWNKSVTL YTVKDKATGE
VLGQFYLDLY PREGKYNHAA CFGLQPGCLL PDGSRMMAVA ALVVNFSQPV AGRPSLLRHD
EVRTYFHEFG HVMHQICAQT DFARFSGTNV ETDFVEVPSQ MLENWVWDID SLRRLSKHYK
DGSPISDDLL EKLVASRLVN TGLLTLRQIV LSKVDQSLHT NTSLDAASEY AKYCSEILGV
AATPGTNMPA TFGHLAGGYD GQYYGYLWSE VFSIDMFYSC FKKEGIMNPE VGMKYRNLIL
KPGGSLDGMD MLHNFLKREP NQKAFLMSRG LHAS
//
