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P42676 (NEUL_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

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

General annotation (Comments)

Function

Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A.

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Mitochondrion intermembrane space. Cytoplasm.

Sequence similarities

Belongs to the peptidase M3 family.

Ontologies

Keywords
   Cellular componentCytoplasm
Mitochondrion
   DomainTransit peptide
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   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 Ref.3
Chain38 – 704667Neurolysin, mitochondrial
PRO_0000028578

Sites

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

Amino acid modifications

Modified residue321Phosphoserine By similarity
Modified residue6641N6-acetyllysine By similarity

Experimental info

Sequence conflict1281K → R in AAH72687. Ref.2

Secondary structure

1 ............................................................................................. 704
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P42676 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: E33F7967A79343D1

FASTA70480,254
        10         20         30         40         50         60 
MITLCLSTLR GLHRAGGSRL QLTMTLGKEL ASPLQAMSSY TAAGRNVLRW DLSPEQIKTR 

        70         80         90        100        110        120 
TEQLIAQTKQ VYDTVGTIAL KEVTYENCLQ VLADIEVTYI VERTMLDFPQ HVSSDREVRA 

       130        140        150        160        170        180 
ASTEADKKLS RFDIEMSMRE DVFQRIVHLQ ETCDLEKIKP EARRYLEKSI KMGKRNGLHL 

       190        200        210        220        230        240 
SEHIRNEIKS MKKRMSELCI DFNKNLNEDD TSLVFSKAEL GALPDDFIDS LEKTDEDKYK 

       250        260        270        280        290        300 
VTLKYPHYFP VMKKCCVPET RRKMEMAFHT RCKQENTAIL QQLLPLRAQV AKLLGYNTHA 

       310        320        330        340        350        360 
DFVLELNTAK STSRVAAFLD DLSQKLKPLG EAEREFILSL KKKECEERGF EYDGKINAWD 

       370        380        390        400        410        420 
LHYYMTQTEE LKYSVDQESL KEYFPIEVVT EGLLSIYQEL LGLSFEQVPD AHVWNKSVSL 

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

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

       550        560        570        580        590        600 
SLRKLSKHYK DGHPITDELL EKLVASRLVN TGLLTLRQIV LSKVDQSLHT NATLDAASEY 

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

       670        680        690        700 
VGMKYRNLIL KPGGSLDGMD MLQNFLQREP NQKAFLMSRG LNGS

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of rat brain endopeptidase 3.4.24.16."
Dauch P., Vincent J.-P., Checler F.
J. Biol. Chem. 270:27266-27271(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Brain.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[3]"Characterization of a mitochondrial metallopeptidase reveals neurolysin as a homologue of thimet oligopeptidase."
Serizawa A., Dando P.M., Barrett A.J.
J. Biol. Chem. 270:2092-2098(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 38-57, CHARACTERIZATION.
Tissue: Liver.
[4]"Structure of neurolysin reveals a deep channel that limits substrate access."
Brown C.K., Madauss K., Lian W., Beck M.R., Tolbert W.D., Rodgers D.W.
Proc. Natl. Acad. Sci. U.S.A. 98:3127-3132(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X87157 mRNA. Translation: CAA60630.1.
BC072687 mRNA. Translation: AAH72687.1.
IPIIPI00230882.
RefSeqNP_446422.2. NM_053970.2.
UniGeneRn.11029.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1I1IX-ray2.30P24-704[»]
2O3EX-ray2.20A24-701[»]
ProteinModelPortalP42676.
SMRP42676. Positions 37-701.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000059652.

Protein family/group databases

MEROPSM03.002.

PTM databases

PhosphoSiteP42676.

Proteomic databases

PaxDbP42676.
PRIDEP42676.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000066925; ENSRNOP00000059652; ENSRNOG00000011561.
GeneID117041.
KEGGrno:117041.
UCSCRGD:621518. rat.

Organism-specific databases

CTD57486.
RGD621518. Nln.

Phylogenomic databases

eggNOGCOG0339.
GeneTreeENSGT00550000074738.
HOGENOMHOG000245985.
HOVERGENHBG000238.
InParanoidQ6GQQ4.
KOK01393.
OrthoDBEOG4CG07P.

Gene expression databases

ArrayExpressP42676.
GenevestigatorP42676.
GermOnlineENSRNOG00000011561. Rattus norvegicus.

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

EvolutionaryTraceP42676.
NextBio619847.
PMAP-CutDBP42676.

Entry information

Entry nameNEUL_RAT
AccessionPrimary (citable) accession number: P42676
Secondary accession number(s): Q6GQQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 3, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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