ID   NEUL_PONAB              Reviewed;         704 AA.
AC   Q5R9V6;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Neurolysin, mitochondrial;
DE            EC=3.4.24.16 {ECO:0000250|UniProtKB:P42676};
DE   AltName: Full=Microsomal endopeptidase;
DE            Short=MEP;
DE   AltName: Full=Mitochondrial oligopeptidase M;
DE   AltName: Full=Neurotensin endopeptidase;
DE   Flags: Precursor;
GN   Name=NLN;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hydrolyzes oligopeptides such as neurotensin, bradykinin and
CC       dynorphin A. Acts as a regulator of cannabinoid signaling pathway by
CC       mediating degradation of hemopressin, an antagonist peptide of the
CC       cannabinoid receptor CNR1. {ECO:0000250|UniProtKB:P42676}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage in neurotensin: 10-Pro-|-Tyr-11.;
CC         EC=3.4.24.16; Evidence={ECO:0000250|UniProtKB:P42676};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P52888};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P52888};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC       {ECO:0000250|UniProtKB:P42676}. Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P42676}.
CC   -!- SIMILARITY: Belongs to the peptidase M3 family. {ECO:0000305}.
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DR   EMBL; CR859276; CAH91454.1; -; mRNA.
DR   RefSeq; NP_001127421.1; NM_001133949.2.
DR   AlphaFoldDB; Q5R9V6; -.
DR   SMR; Q5R9V6; -.
DR   STRING; 9601.ENSPPYP00000017333; -.
DR   MEROPS; M03.002; -.
DR   GeneID; 100174491; -.
DR   KEGG; pon:100174491; -.
DR   CTD; 57486; -.
DR   eggNOG; KOG2089; Eukaryota.
DR   InParanoid; Q5R9V6; -.
DR   OrthoDB; 642479at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
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   Gene3D; 1.10.1370.10; -; 1.
DR   Gene3D; 1.20.1050.40; -; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR024080; Neurolysin/TOP_N.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR11804; PTHR11804; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease;
KW   Mitochondrion; Protease; Reference proteome; Transit peptide; Zinc.
FT   TRANSIT         1..37
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:P42676"
FT   CHAIN           38..704
FT                   /note="Neurolysin, mitochondrial"
FT                   /id="PRO_0000319048"
FT   ACT_SITE        498
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         497
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         501
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         504
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   MOD_RES         664
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BYT8"
SQ   SEQUENCE   704 AA;  80798 MW;  CDE234F0F169D7C8 CRC64;
     MIARCLLAVR SLRRVGGSRI LLRMTLGREV MSPLQAMSSY TVTGRNVLRW DLSPEQIKTR
     TEELIVQTKQ VYDAVGMLGI EEVTYENCLQ ALADIEVKYI VERTMLDFPQ HVSSDKEVRA
     ASTEADKRLS RFDIEMSMRG DIFERIVRLQ ETCDLGKIKP EARRYLEKSI KMGKRNGLHL
     PEQVQNEIKS MKKRMSELCI DFNKNLNEDD TFLVFSKAEL GALPDDFIDS LEKIDDDKYK
     ITLKYPHYFP VMKKCCIPET RRRMEMAFNT RCKEENTIIL QQLLPLRAKV AKLLGYSTHA
     DFVLEMNTAK STSRVTAFLD DLSQKLKPLG EAEREFILNL KKKECEDRGF EYDGKINAWD
     LYYYMTQTEE LKYSIDQEFL KEYFPIEVVT EGLLNTYQEL LGLSFEQVTD AHVWNKNVTL
     YTVKDKATGE VLGQFYLDLY PRDRKYNHAA CFGLQPGCLL PDGSRMMAVA ALVVNFSQPV
     AGRPSLLRHD EVRTYFHEFG HVMHQICAQT DFARFSGTNV ETDFVEVPSQ MLENWVWDVD
     SLRRLSKHYK DGSPISDDLL EKLVASRLIN TGLLTLRQIV LSKVDQSLHT NTSLDAASEY
     AKYCSEILGV AATPGTNMPA TFGHLAGGYD GQYYGYLWSE VFSMDMFYSC FKKEGIMNPE
     VGMKYRNLIL KPGGSLDGMD MLHNFLKREP NQKAFLMSRG LHAS