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Protein

Neurolysin, mitochondrial

Gene

Nln

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi497 – 4971Zinc; catalyticPROSITE-ProRule annotation
Active sitei498 – 4981PROSITE-ProRule annotation
Metal bindingi501 – 5011Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi504 – 5041Zinc; catalyticPROSITE-ProRule annotation

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 PublicationAdd
BLAST
Chaini38 – 704667Neurolysin, mitochondrialPRO_0000028578Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei664 – 6641N6-acetyllysineBy 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

1
704
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni43 – 453Combined sources
Helixi54 – 7522Combined sources
Helixi80 – 823Combined sources
Turni85 – 884Combined sources
Helixi89 – 10719Combined sources
Helixi109 – 1124Combined sources
Helixi116 – 13722Combined sources
Helixi140 – 15213Combined sources
Helixi160 – 17516Combined sources
Turni176 – 1794Combined sources
Helixi182 – 1876Combined sources
Helixi189 – 20820Combined sources
Beta strandi212 – 2165Combined sources
Turni217 – 2226Combined sources
Helixi225 – 2295Combined sources
Beta strandi231 – 2333Combined sources
Beta strandi235 – 24410Combined sources
Helixi245 – 25410Combined sources
Helixi258 – 26811Combined sources
Turni269 – 2724Combined sources
Helixi273 – 29321Combined sources
Helixi299 – 3046Combined sources
Helixi312 – 34736Combined sources
Helixi358 – 3603Combined sources
Helixi361 – 37212Combined sources
Helixi377 – 3804Combined sources
Helixi381 – 3833Combined sources
Helixi386 – 40116Combined sources
Beta strandi403 – 4075Combined sources
Beta strandi419 – 4257Combined sources
Turni426 – 4283Combined sources
Beta strandi431 – 4388Combined sources
Beta strandi450 – 4556Combined sources
Beta strandi468 – 4736Combined sources
Beta strandi481 – 4833Combined sources
Helixi489 – 50719Combined sources
Beta strandi510 – 5123Combined sources
Helixi513 – 5153Combined sources
Turni522 – 5265Combined sources
Helixi527 – 5337Combined sources
Helixi534 – 5374Combined sources
Helixi539 – 5457Combined sources
Beta strandi549 – 5513Combined sources
Helixi557 – 5659Combined sources
Turni566 – 5705Combined sources
Helixi571 – 58818Combined sources
Helixi596 – 60611Combined sources
Helixi618 – 6214Combined sources
Beta strandi625 – 6284Combined sources
Helixi635 – 64915Combined sources
Helixi651 – 6544Combined sources
Helixi659 – 66911Combined sources
Turni670 – 6723Combined sources
Helixi673 – 6753Combined sources
Helixi678 – 6869Combined sources
Helixi693 – 6997Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP42676.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M3 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0339.
HOGENOMiHOG000245985.
HOVERGENiHBG000238.
InParanoidiP42676.
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

        10         20         30         40         50
MITLCLSTLR GLHRAGGSRL QLTMTLGKEL ASPLQAMSSY TAAGRNVLRW
60 70 80 90 100
DLSPEQIKTR TEQLIAQTKQ VYDTVGTIAL KEVTYENCLQ VLADIEVTYI
110 120 130 140 150
VERTMLDFPQ HVSSDREVRA ASTEADKKLS RFDIEMSMRE DVFQRIVHLQ
160 170 180 190 200
ETCDLEKIKP EARRYLEKSI KMGKRNGLHL SEHIRNEIKS MKKRMSELCI
210 220 230 240 250
DFNKNLNEDD TSLVFSKAEL GALPDDFIDS LEKTDEDKYK VTLKYPHYFP
260 270 280 290 300
VMKKCCVPET RRKMEMAFHT RCKQENTAIL QQLLPLRAQV AKLLGYNTHA
310 320 330 340 350
DFVLELNTAK STSRVAAFLD DLSQKLKPLG EAEREFILSL KKKECEERGF
360 370 380 390 400
EYDGKINAWD LHYYMTQTEE LKYSVDQESL KEYFPIEVVT EGLLSIYQEL
410 420 430 440 450
LGLSFEQVPD AHVWNKSVSL YTVKDKATGE VLGQFYLDLY PREGKYNHAA
460 470 480 490 500
CFGLQPGCLL PDGSRMMSVA ALVVNFSQPV AGRPSLLRHD EVRTYFHEFG
510 520 530 540 550
HVMHQICAQT DFARFSGTNV ETDFVEVPSQ MLENWVWDVD SLRKLSKHYK
560 570 580 590 600
DGHPITDELL EKLVASRLVN TGLLTLRQIV LSKVDQSLHT NATLDAASEY
610 620 630 640 650
AKYCTEILGV AATPGTNMPA TFGHLAGGYD GQYYGYLWSE VFSMDMFHSC
660 670 680 690 700
FKKEGIMNPE VGMKYRNLIL KPGGSLDGMD MLQNFLQREP NQKAFLMSRG

LNGS
Length:704
Mass (Da):80,254
Last modified:November 1, 1995 - v1
Checksum:iE33F7967A79343D1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti128 – 1281K → R in AAH72687 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87157 mRNA. Translation: CAA60630.1.
BC072687 mRNA. Translation: AAH72687.1.
RefSeqiNP_446422.2. NM_053970.2.
UniGeneiRn.11029.

Genome annotation databases

GeneIDi117041.
KEGGirno:117041.
UCSCiRGD:621518. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87157 mRNA. Translation: CAA60630.1.
BC072687 mRNA. Translation: AAH72687.1.
RefSeqiNP_446422.2. NM_053970.2.
UniGeneiRn.11029.

3D structure databases

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000059652.

Protein family/group databases

MEROPSiM03.002.

PTM databases

PhosphoSiteiP42676.

Proteomic databases

PaxDbiP42676.
PRIDEiP42676.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi117041.
KEGGirno:117041.
UCSCiRGD:621518. rat.

Organism-specific databases

CTDi57486.
RGDi621518. Nln.

Phylogenomic databases

eggNOGiCOG0339.
HOGENOMiHOG000245985.
HOVERGENiHBG000238.
InParanoidiP42676.
KOiK01393.
OrthoDBiEOG7SR4KW.
PhylomeDBiP42676.
TreeFamiTF300459.

Miscellaneous databases

EvolutionaryTraceiP42676.
NextBioi619847.
PMAP-CutDBP42676.
PROiP42676.

Gene expression databases

GenevestigatoriP42676.

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]
ProtoNetiSearch...

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: March 4, 2015
This is version 122 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.