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A2VDQ5 (NEUL_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neurolysin, mitochondrial

EC=3.4.24.16
Alternative name(s):
Microsomal endopeptidase
Short name=MEP
Mitochondrial oligopeptidase M
Neurotensin endopeptidase
Gene names
Name:NLN
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length704 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A By similarity.

Catalytic activity

Preferential cleavage in neurotensin: 10-Pro-|-Tyr-11.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Mitochondrion intermembrane space By similarity. Cytoplasm By similarity.

Sequence similarities

Belongs to the peptidase M3 family.

Ontologies

Keywords
   Cellular componentCytoplasm
Mitochondrion
   DomainTransit peptide
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentmitochondrial intermembrane space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3737Mitochondrion
Chain38 – 704667Neurolysin, mitochondrial
PRO_0000319047

Sites

Active site4981 By similarity
Metal binding4971Zinc; catalytic By similarity
Metal binding5011Zinc; catalytic By similarity
Metal binding5041Zinc; catalytic By similarity

Amino acid modifications

Modified residue6641N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A2VDQ5 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: F53622A4F7116FC8

FASTA70480,728
        10         20         30         40         50         60 
MIVQCLLAVR GLHRVGGSRI LFRMTLGREE MSPLQAMSSY MAAGRNVLRW DLSPEQIKTR 

        70         80         90        100        110        120 
TEELISQTKQ VYDAIGMRDI KEVTYENCLQ ALADIEVKYI VERTMLDFPQ HVSSDKEVRA 

       130        140        150        160        170        180 
ASTEADKRLS RFDIEMSMRQ DIFLRIVHLK ETCDLEKIKP EARRYLEKSV KMGKRNGLHL 

       190        200        210        220        230        240 
PEQVQNEIKA MKKRMSELCI DFNKNLNEDD TFLVFSKAEL GALPDDFINS LEKTDGDKYK 

       250        260        270        280        290        300 
ITLKYPHYFP VMKKCCVPET RRKMEMAFNT RCKEENTVIL QQLLPLRAEV ARLLGYSTHA 

       310        320        330        340        350        360 
DFVLEMNTAK STRHVTAFLD DLSQKLKPLG EAEREFILNL KKKECKERGF EYDGKINAWD 

       370        380        390        400        410        420 
LHYYMTQTEE LKYSVDQETL KEYFPIEVVT EGLLNIYQEL LGLSFEQVTD AHVWNKSVTL 

       430        440        450        460        470        480 
YTVKDKATGE VLGQFYLDLY PREGKYNHAA CFGLQPGCLL PDGSRMMSVA ALVVNFSQPL 

       490        500        510        520        530        540 
AGRPSLLRHD EVRTYFHEFG HVMHQICAQT DFARFSGTNV ETDFVEVPSQ MLENWVWDAD 

       550        560        570        580        590        600 
SLRRLSKHYR HGSPITDDLL EKLVASRLVN TGLLTLRQIV LSKVDQSLHT NTALDAASEY 

       610        620        630        640        650        660 
AKYCTEILGV AATPGTNMPA TFGHLAGGYD GQYYGYLWSE VFSMDMFYSC FKKEGIMNPE 

       670        680        690        700 
VGMKYRNLIL KPGGSLDGMD MLQNFLTREP NQKAFLMSRG LPAP 

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Hypothalamus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC133350 mRNA. Translation: AAI33351.1.
RefSeqNP_001029161.2. NM_001033989.2.
UniGeneBt.40554.

3D structure databases

ProteinModelPortalA2VDQ5.
SMRA2VDQ5. Positions 37-701.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000022482.

Protein family/group databases

MEROPSM03.002.

Proteomic databases

PRIDEA2VDQ5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID538650.
KEGGbta:538650.

Organism-specific databases

CTD57486.

Phylogenomic databases

eggNOGCOG0339.
HOGENOMHOG000245985.
HOVERGENHBG000238.
InParanoidA2VDQ5.
KOK01393.

Family and domain databases

Gene3D1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20877494.

Entry information

Entry nameNEUL_BOVIN
AccessionPrimary (citable) accession number: A2VDQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: March 20, 2007
Last modified: May 14, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries