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P42675

- NEUL_RABIT

UniProt

P42675 - NEUL_RABIT

Protein

Neurolysin, mitochondrial

Gene

NLN

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    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; 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

    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

    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.

    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: October 1, 2014
    This is version 90 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