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Database: UniProt
Entry: G3X795_BOVIN
LinkDB: G3X795_BOVIN
Original site: G3X795_BOVIN 
ID   G3X795_BOVIN            Unreviewed;       704 AA.
AC   G3X795;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 2.
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:ENSBTAP00000022482.6,
GN   ECO:0000313|VGNC:VGNC:97293};
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 {ECO:0000313|Ensembl:ENSBTAP00000022482.6, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000022482.6, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000022482.6,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000022482.6}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000022482.6};
RG   Ensembl;
RL   Submitted (NOV-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   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR   AlphaFoldDB; G3X795; -.
DR   SMR; G3X795; -.
DR   Ensembl; ENSBTAT00000022482.6; ENSBTAP00000022482.6; ENSBTAG00000016903.6.
DR   VEuPathDB; HostDB:ENSBTAG00000016903; -.
DR   VGNC; VGNC:97293; NLN.
DR   GeneTree; ENSGT00950000183171; -.
DR   HOGENOM; CLU_001805_2_1_1; -.
DR   InParanoid; G3X795; -.
DR   OMA; RSGAWCS; -.
DR   TreeFam; TF300459; -.
DR   Reactome; R-BTA-375276; Peptide ligand-binding receptors.
DR   Proteomes; UP000009136; Chromosome 20.
DR   Bgee; ENSBTAG00000016903; Expressed in midbrain and 103 other cell types or tissues.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0042277; F:peptide binding; IEA:Ensembl.
DR   GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   GO; GO:0006111; P:regulation of gluconeogenesis; IEA:Ensembl.
DR   GO; GO:1902809; P:regulation of skeletal muscle fiber differentiation; IEA:Ensembl.
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; IPR024080; Neurolysin/TOP_N.
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   3: Inferred from homology;
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:UP000009136};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          251..700
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   704 AA;  80745 MW;  77DC71F5E5C6DE3F 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 DLSQKLKLLG EAEREFILNL KKKECEERGF 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
//
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