ID   NEUL_BOVIN              Reviewed;         704 AA.
AC   A2VDQ5;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2007) 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; BC133350; AAI33351.1; -; mRNA.
DR   RefSeq; NP_001029161.2; NM_001033989.2.
DR   AlphaFoldDB; A2VDQ5; -.
DR   SMR; A2VDQ5; -.
DR   STRING; 9913.ENSBTAP00000022482; -.
DR   MEROPS; M03.002; -.
DR   PaxDb; A2VDQ5; -.
DR   PRIDE; A2VDQ5; -.
DR   GeneID; 538650; -.
DR   KEGG; bta:538650; -.
DR   CTD; 57486; -.
DR   eggNOG; KOG2089; Eukaryota.
DR   InParanoid; A2VDQ5; -.
DR   OrthoDB; 642479at2759; -.
DR   BRENDA; 3.4.24.16; 908.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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_0000319047"
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;  80728 MW;  F53622A4F7116FC8 CRC64;
     MIVQCLLAVR GLHRVGGSRI LFRMTLGREE MSPLQAMSSY MAAGRNVLRW DLSPEQIKTR
     TEELISQTKQ VYDAIGMRDI KEVTYENCLQ ALADIEVKYI VERTMLDFPQ HVSSDKEVRA
     ASTEADKRLS RFDIEMSMRQ DIFLRIVHLK ETCDLEKIKP EARRYLEKSV KMGKRNGLHL
     PEQVQNEIKA MKKRMSELCI DFNKNLNEDD TFLVFSKAEL GALPDDFINS LEKTDGDKYK
     ITLKYPHYFP VMKKCCVPET RRKMEMAFNT RCKEENTVIL QQLLPLRAEV ARLLGYSTHA
     DFVLEMNTAK STRHVTAFLD DLSQKLKPLG EAEREFILNL KKKECKERGF EYDGKINAWD
     LHYYMTQTEE LKYSVDQETL KEYFPIEVVT EGLLNIYQEL LGLSFEQVTD AHVWNKSVTL
     YTVKDKATGE VLGQFYLDLY PREGKYNHAA CFGLQPGCLL PDGSRMMSVA ALVVNFSQPL
     AGRPSLLRHD EVRTYFHEFG HVMHQICAQT DFARFSGTNV ETDFVEVPSQ MLENWVWDAD
     SLRRLSKHYR HGSPITDDLL EKLVASRLVN TGLLTLRQIV LSKVDQSLHT NTALDAASEY
     AKYCTEILGV AATPGTNMPA TFGHLAGGYD GQYYGYLWSE VFSMDMFYSC FKKEGIMNPE
     VGMKYRNLIL KPGGSLDGMD MLQNFLTREP NQKAFLMSRG LPAP