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Protein

Neurolysin, mitochondrial

Gene

NLN

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

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
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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

Subcellular locationi

Mitochondrion By similarity. Cytoplasm By similarity

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3737MitochondrionBy similarityAdd
BLAST
Chaini38 – 704667Neurolysin, mitochondrialPRO_0000028577Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP42675.

Interactioni

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000008123.

Structurei

3D structure databases

ProteinModelPortaliP42675.
SMRiP42675. Positions 37-701.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M3 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0339.
HOGENOMiHOG000245985.
HOVERGENiHBG000238.
InParanoidiP42675.
KOiK01393.

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.

P42675-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIARCFSAVR GLHRVGGSRI LFKMTLGREV MSPLQAVSSY TAAGRNVLRW
60 70 80 90 100
DLSPEQIKTR TEELIAQTKQ VYDSVGMLDI KDVTYENCLQ ALADVEVKYI
110 120 130 140 150
VERTMLDFPQ HVSTDREVRA ASTEADKRLS RFDIEMSMRE DIFQRIVHLQ
160 170 180 190 200
ETCDLEKIKP EARRYLEKSV KMGRRNGLHL PEEVQNEIKS MKKRMSELCI
210 220 230 240 250
DFNKNLNEDD TFLVFSKAEL GALPDDFIDS LEKMDDDKYK ITLKYPHYFP
260 270 280 290 300
VMKKCCIPET RRRMEMAFNT RCKEENTVIL QQLLPLRAQV AKLLGYSTHA
310 320 330 340 350
DFVLEMNTAK STSRVTAFLD DLSQKLKPLG EAEREFILSL KKKECEEKGF
360 370 380 390 400
EYDGKINAWD LHYYMTQTEE LKYSIDQEFI KEYFPIEVVT EGLLNIYQEL
410 420 430 440 450
LGLSFEQVAD AHVWNPSVTL YTVKDKATGE VLGQFYLDLY PREGKYNHAA
460 470 480 490 500
CFGLQPGCLL PDGSRMLSVA ALVVNFSQPV AGRPSLLRHD EVRTYFHEFG
510 520 530 540 550
HVMHQICAQT DFARFSGTNV ETDFVEVPSQ MLENWVWDID SLRRLSKHYK
560 570 580 590 600
DGNPIADDLL EKLVASRLVN TGLLTLRQIV LSKVDQSLHT NSSLDAASEY
610 620 630 640 650
ARYCTDILGV AATPGTNMPA TFGHLAGGYD GQYYGYLWSE VFSMDMFYSC
660 670 680 690 700
FKKEGIMNPE VGMKYRNLIL RPGGSLDGMD MLQNFLQREP NQKAFLMSRG

LQAP
Length:704
Mass (Da):80,689
Last modified:November 1, 1995 - v1
Checksum:iA1B7E4DE38E8088C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13310 mRNA. Translation: BAA02570.1.
PIRiA45985.
RefSeqiXP_008260508.1. XM_008262286.1.

Genome annotation databases

GeneIDi100357326.
KEGGiocu:100357326.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13310 mRNA. Translation: BAA02570.1.
PIRiA45985.
RefSeqiXP_008260508.1. XM_008262286.1.

3D structure databases

ProteinModelPortaliP42675.
SMRiP42675. Positions 37-701.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000008123.

Protein family/group databases

MEROPSiM03.002.

Proteomic databases

PRIDEiP42675.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100357326.
KEGGiocu:100357326.

Organism-specific databases

CTDi57486.

Phylogenomic databases

eggNOGiCOG0339.
HOGENOMiHOG000245985.
HOVERGENiHBG000238.
InParanoidiP42675.
KOiK01393.

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

  1. "Rabbit liver microsomal endopeptidase with substrate specificity for processing proproteins is structurally related to rat testes metalloendopeptidase 24.15."
    Kawabata S., Nakagawa K., Muta T., Iwanaga S., Davie E.W.
    J. Biol. Chem. 268:12498-12503(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Liver.

Entry informationi

Entry nameiNEUL_RABIT
AccessioniPrimary (citable) accession number: P42675
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: March 4, 2015
This is version 95 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.