ID NEUL_RABIT Reviewed; 704 AA.
AC P42675;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-APR-2013, entry version 86.
DE RecName: Full=Neurolysin, mitochondrial;
DE EC=3.4.24.16;
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=8509389;
RA Kawabata S., Nakagawa K., Muta T., Iwanaga S., Davie E.W.;
RT "Rabbit liver microsomal endopeptidase with substrate specificity for
RT processing proproteins is structurally related to rat testes
RT metalloendopeptidase 24.15.";
RL J. Biol. Chem. 268:12498-12503(1993).
CC -!- FUNCTION: Hydrolyzes oligopeptides such as neurotensin, bradykinin
CC and dynorphin A (By similarity).
CC -!- CATALYTIC ACTIVITY: Preferential cleavage in neurotensin: 10-
CC Pro-|-Tyr-11.
CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). Cytoplasm (By
CC similarity).
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
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DR EMBL; D13310; BAA02570.1; -; mRNA.
DR PIR; A45985; A45985.
DR ProteinModelPortal; P42675; -.
DR SMR; P42675; 37-701.
DR STRING; 9986.ENSOCUP00000008123; -.
DR MEROPS; M03.002; -.
DR PRIDE; P42675; -.
DR eggNOG; COG0339; -.
DR HOGENOM; HOG000245985; -.
DR HOVERGEN; HBG000238; -.
DR OrthoDB; EOG4CG07P; -.
DR GO; GO:0005739; C:mitochondrion; 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; -; 2.
DR Gene3D; 1.20.1050.40; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR024080; Neurolysin/TOP_N.
DR InterPro; IPR001567; Pept_M3A_M3B.
DR Pfam; PF01432; Peptidase_M3; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Hydrolase; Metal-binding; Metalloprotease; Mitochondrion;
KW Phosphoprotein; Protease; Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1 37 Mitochondrion (By similarity).
FT CHAIN 38 704 Neurolysin, mitochondrial.
FT /FTId=PRO_0000028577.
FT ACT_SITE 498 498 By similarity.
FT METAL 497 497 Zinc; catalytic (By similarity).
FT METAL 501 501 Zinc; catalytic (By similarity).
FT METAL 504 504 Zinc; catalytic (By similarity).
FT MOD_RES 32 32 Phosphoserine (By similarity).
FT MOD_RES 664 664 N6-acetyllysine (By similarity).
SQ SEQUENCE 704 AA; 80689 MW; A1B7E4DE38E8088C CRC64;
MIARCFSAVR GLHRVGGSRI LFKMTLGREV MSPLQAVSSY TAAGRNVLRW DLSPEQIKTR
TEELIAQTKQ VYDSVGMLDI KDVTYENCLQ ALADVEVKYI VERTMLDFPQ HVSTDREVRA
ASTEADKRLS RFDIEMSMRE DIFQRIVHLQ ETCDLEKIKP EARRYLEKSV KMGRRNGLHL
PEEVQNEIKS MKKRMSELCI DFNKNLNEDD TFLVFSKAEL GALPDDFIDS LEKMDDDKYK
ITLKYPHYFP VMKKCCIPET RRRMEMAFNT RCKEENTVIL QQLLPLRAQV AKLLGYSTHA
DFVLEMNTAK STSRVTAFLD DLSQKLKPLG EAEREFILSL KKKECEEKGF EYDGKINAWD
LHYYMTQTEE LKYSIDQEFI KEYFPIEVVT EGLLNIYQEL LGLSFEQVAD AHVWNPSVTL
YTVKDKATGE VLGQFYLDLY PREGKYNHAA CFGLQPGCLL PDGSRMLSVA ALVVNFSQPV
AGRPSLLRHD EVRTYFHEFG HVMHQICAQT DFARFSGTNV ETDFVEVPSQ MLENWVWDID
SLRRLSKHYK DGNPIADDLL EKLVASRLVN TGLLTLRQIV LSKVDQSLHT NSSLDAASEY
ARYCTDILGV AATPGTNMPA TFGHLAGGYD GQYYGYLWSE VFSMDMFYSC FKKEGIMNPE
VGMKYRNLIL RPGGSLDGMD MLQNFLQREP NQKAFLMSRG LQAP
//
