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P42675

- NEUL_RABIT

UniProt

P42675 - NEUL_RABIT

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Protein

Neurolysin, mitochondrial

Gene
NLN
Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - 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

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
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 – 3737Mitochondrion By similarityAdd
BLAST
Chaini38 – 704667Neurolysin, mitochondrialPRO_0000028577Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP42675.

Interactioni

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000008123.

Structurei

3D structure databases

ProteinModelPortaliP42675.
SMRiP42675. Positions 37-701.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M3 family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0339.
HOGENOMiHOG000245985.
HOVERGENiHBG000238.

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

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MIARCFSAVR GLHRVGGSRI LFKMTLGREV MSPLQAVSSY TAAGRNVLRW    50
DLSPEQIKTR TEELIAQTKQ VYDSVGMLDI KDVTYENCLQ ALADVEVKYI 100
VERTMLDFPQ HVSTDREVRA ASTEADKRLS RFDIEMSMRE DIFQRIVHLQ 150
ETCDLEKIKP EARRYLEKSV KMGRRNGLHL PEEVQNEIKS MKKRMSELCI 200
DFNKNLNEDD TFLVFSKAEL GALPDDFIDS LEKMDDDKYK ITLKYPHYFP 250
VMKKCCIPET RRRMEMAFNT RCKEENTVIL QQLLPLRAQV AKLLGYSTHA 300
DFVLEMNTAK STSRVTAFLD DLSQKLKPLG EAEREFILSL KKKECEEKGF 350
EYDGKINAWD LHYYMTQTEE LKYSIDQEFI KEYFPIEVVT EGLLNIYQEL 400
LGLSFEQVAD AHVWNPSVTL YTVKDKATGE VLGQFYLDLY PREGKYNHAA 450
CFGLQPGCLL PDGSRMLSVA ALVVNFSQPV AGRPSLLRHD EVRTYFHEFG 500
HVMHQICAQT DFARFSGTNV ETDFVEVPSQ MLENWVWDID SLRRLSKHYK 550
DGNPIADDLL EKLVASRLVN TGLLTLRQIV LSKVDQSLHT NSSLDAASEY 600
ARYCTDILGV AATPGTNMPA TFGHLAGGYD GQYYGYLWSE VFSMDMFYSC 650
FKKEGIMNPE VGMKYRNLIL RPGGSLDGMD MLQNFLQREP NQKAFLMSRG 700
LQAP 704
Length:704
Mass (Da):80,689
Last modified:November 1, 1995 - v1
Checksum:iA1B7E4DE38E8088C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D13310 mRNA. Translation: BAA02570.1.
PIRiA45985.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D13310 mRNA. Translation: BAA02570.1 .
PIRi A45985.

3D structure databases

ProteinModelPortali P42675.
SMRi P42675. Positions 37-701.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9986.ENSOCUP00000008123.

Protein family/group databases

MEROPSi M03.002.

Proteomic databases

PRIDEi P42675.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0339.
HOGENOMi HOG000245985.
HOVERGENi HBG000238.

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

  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: May 14, 2014
This is version 89 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

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