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P42676

- NEUL_RAT

UniProt

P42676 - NEUL_RAT

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Protein
Neurolysin, mitochondrial
Gene
Nln
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A.

Catalytic activityi

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

Cofactori

Binds 1 zinc ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi497 – 4971Zinc; catalytic By similarity
Active sitei498 – 4981 By similarity
Metal bindingi501 – 5011Zinc; catalytic By similarity
Metal bindingi504 – 5041Zinc; catalytic By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metalloendopeptidase activity Source: InterPro
  3. peptide binding Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM03.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Neurolysin, mitochondrial (EC:3.4.24.16)
Alternative name(s):
Microsomal endopeptidase
Short name:
MEP
Mitochondrial oligopeptidase M
Neurotensin endopeptidase
Gene namesi
Name:Nln
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 2

Organism-specific databases

RGDi621518. Nln.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial intermembrane space Source: UniProtKB-SubCell
  2. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3737Mitochondrion1 Publication
Add
BLAST
Chaini38 – 704667Neurolysin, mitochondrial
PRO_0000028578Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei664 – 6641N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP42676.
PRIDEiP42676.

PTM databases

PhosphoSiteiP42676.

Miscellaneous databases

PMAP-CutDBP42676.

Expressioni

Gene expression databases

GenevestigatoriP42676.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000059652.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni43 – 453
Helixi54 – 7522
Helixi80 – 823
Turni85 – 884
Helixi89 – 10719
Helixi109 – 1124
Helixi116 – 13722
Helixi140 – 15213
Helixi160 – 17516
Turni176 – 1794
Helixi182 – 1876
Helixi189 – 20820
Beta strandi212 – 2165
Turni217 – 2226
Helixi225 – 2295
Beta strandi231 – 2333
Beta strandi235 – 24410
Helixi245 – 25410
Helixi258 – 26811
Turni269 – 2724
Helixi273 – 29321
Helixi299 – 3046
Helixi312 – 34736
Helixi358 – 3603
Helixi361 – 37212
Helixi377 – 3804
Helixi381 – 3833
Helixi386 – 40116
Beta strandi403 – 4075
Beta strandi419 – 4257
Turni426 – 4283
Beta strandi431 – 4388
Beta strandi450 – 4556
Beta strandi468 – 4736
Beta strandi481 – 4833
Helixi489 – 50719
Beta strandi510 – 5123
Helixi513 – 5153
Turni522 – 5265
Helixi527 – 5337
Helixi534 – 5374
Helixi539 – 5457
Beta strandi549 – 5513
Helixi557 – 5659
Turni566 – 5705
Helixi571 – 58818
Helixi596 – 60611
Helixi618 – 6214
Beta strandi625 – 6284
Helixi635 – 64915
Helixi651 – 6544
Helixi659 – 66911
Turni670 – 6723
Helixi673 – 6753
Helixi678 – 6869
Helixi693 – 6997

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I1IX-ray2.30P24-704[»]
2O3EX-ray2.20A24-701[»]
4FXYX-ray2.80P/Q24-704[»]
ProteinModelPortaliP42676.
SMRiP42676. Positions 37-701.

Miscellaneous databases

EvolutionaryTraceiP42676.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M3 family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0339.
GeneTreeiENSGT00550000074738.
HOGENOMiHOG000245985.
HOVERGENiHBG000238.
InParanoidiQ6GQQ4.
KOiK01393.
OrthoDBiEOG7SR4KW.
PhylomeDBiP42676.
TreeFamiTF300459.

Family and domain databases

Gene3Di1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view]
PfamiPF01432. Peptidase_M3. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P42676-1 [UniParc]FASTAAdd to Basket

« Hide

MITLCLSTLR GLHRAGGSRL QLTMTLGKEL ASPLQAMSSY TAAGRNVLRW    50
DLSPEQIKTR TEQLIAQTKQ VYDTVGTIAL KEVTYENCLQ VLADIEVTYI 100
VERTMLDFPQ HVSSDREVRA ASTEADKKLS RFDIEMSMRE DVFQRIVHLQ 150
ETCDLEKIKP EARRYLEKSI KMGKRNGLHL SEHIRNEIKS MKKRMSELCI 200
DFNKNLNEDD TSLVFSKAEL GALPDDFIDS LEKTDEDKYK VTLKYPHYFP 250
VMKKCCVPET RRKMEMAFHT RCKQENTAIL QQLLPLRAQV AKLLGYNTHA 300
DFVLELNTAK STSRVAAFLD DLSQKLKPLG EAEREFILSL KKKECEERGF 350
EYDGKINAWD LHYYMTQTEE LKYSVDQESL KEYFPIEVVT EGLLSIYQEL 400
LGLSFEQVPD AHVWNKSVSL YTVKDKATGE VLGQFYLDLY PREGKYNHAA 450
CFGLQPGCLL PDGSRMMSVA ALVVNFSQPV AGRPSLLRHD EVRTYFHEFG 500
HVMHQICAQT DFARFSGTNV ETDFVEVPSQ MLENWVWDVD SLRKLSKHYK 550
DGHPITDELL EKLVASRLVN TGLLTLRQIV LSKVDQSLHT NATLDAASEY 600
AKYCTEILGV AATPGTNMPA TFGHLAGGYD GQYYGYLWSE VFSMDMFHSC 650
FKKEGIMNPE VGMKYRNLIL KPGGSLDGMD MLQNFLQREP NQKAFLMSRG 700
LNGS 704
Length:704
Mass (Da):80,254
Last modified:November 1, 1995 - v1
Checksum:iE33F7967A79343D1
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti128 – 1281K → R in AAH72687. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X87157 mRNA. Translation: CAA60630.1.
BC072687 mRNA. Translation: AAH72687.1.
RefSeqiNP_446422.2. NM_053970.2.
UniGeneiRn.11029.

Genome annotation databases

EnsembliENSRNOT00000066925; ENSRNOP00000059652; ENSRNOG00000011561.
GeneIDi117041.
KEGGirno:117041.
UCSCiRGD:621518. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X87157 mRNA. Translation: CAA60630.1 .
BC072687 mRNA. Translation: AAH72687.1 .
RefSeqi NP_446422.2. NM_053970.2.
UniGenei Rn.11029.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1I1I X-ray 2.30 P 24-704 [» ]
2O3E X-ray 2.20 A 24-701 [» ]
4FXY X-ray 2.80 P/Q 24-704 [» ]
ProteinModelPortali P42676.
SMRi P42676. Positions 37-701.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000059652.

Protein family/group databases

MEROPSi M03.002.

PTM databases

PhosphoSitei P42676.

Proteomic databases

PaxDbi P42676.
PRIDEi P42676.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000066925 ; ENSRNOP00000059652 ; ENSRNOG00000011561 .
GeneIDi 117041.
KEGGi rno:117041.
UCSCi RGD:621518. rat.

Organism-specific databases

CTDi 57486.
RGDi 621518. Nln.

Phylogenomic databases

eggNOGi COG0339.
GeneTreei ENSGT00550000074738.
HOGENOMi HOG000245985.
HOVERGENi HBG000238.
InParanoidi Q6GQQ4.
KOi K01393.
OrthoDBi EOG7SR4KW.
PhylomeDBi P42676.
TreeFami TF300459.

Miscellaneous databases

EvolutionaryTracei P42676.
NextBioi 619847.
PMAP-CutDB P42676.
PROi P42676.

Gene expression databases

Genevestigatori P42676.

Family and domain databases

Gene3Di 1.10.1370.10. 2 hits.
1.20.1050.40. 1 hit.
3.40.390.10. 1 hit.
InterProi IPR024079. MetalloPept_cat_dom.
IPR024077. Neurolysin/TOP_dom2.
IPR024080. Neurolysin/TOP_N.
IPR001567. Pept_M3A_M3B.
[Graphical view ]
Pfami PF01432. Peptidase_M3. 1 hit.
[Graphical view ]
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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).

Entry informationi

Entry nameiNEUL_RAT
AccessioniPrimary (citable) accession number: P42676
Secondary accession number(s): Q6GQQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 14, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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