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A2VDQ5

- NEUL_BOVIN

UniProt

A2VDQ5 - NEUL_BOVIN

Protein

Neurolysin, mitochondrial

Gene

NLN

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 54 (01 Oct 2014)
      Sequence version 1 (20 Mar 2007)
      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
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    Mitochondrion intermembrane space By similarity. Cytoplasm By similarity

    GO - Cellular componenti

    1. mitochondrial intermembrane space Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3737MitochondrionAdd
    BLAST
    Chaini38 – 704667Neurolysin, mitochondrialPRO_0000319047Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiA2VDQ5.

    Interactioni

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000022482.

    Structurei

    3D structure databases

    ProteinModelPortaliA2VDQ5.
    SMRiA2VDQ5. 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.
    InParanoidiA2VDQ5.
    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.

    A2VDQ5-1 [UniParc]FASTAAdd to Basket

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    MIVQCLLAVR GLHRVGGSRI LFRMTLGREE MSPLQAMSSY MAAGRNVLRW    50
    DLSPEQIKTR TEELISQTKQ VYDAIGMRDI KEVTYENCLQ ALADIEVKYI 100
    VERTMLDFPQ HVSSDKEVRA ASTEADKRLS RFDIEMSMRQ DIFLRIVHLK 150
    ETCDLEKIKP EARRYLEKSV KMGKRNGLHL PEQVQNEIKA MKKRMSELCI 200
    DFNKNLNEDD TFLVFSKAEL GALPDDFINS LEKTDGDKYK ITLKYPHYFP 250
    VMKKCCVPET RRKMEMAFNT RCKEENTVIL QQLLPLRAEV ARLLGYSTHA 300
    DFVLEMNTAK STRHVTAFLD DLSQKLKPLG EAEREFILNL KKKECKERGF 350
    EYDGKINAWD LHYYMTQTEE LKYSVDQETL KEYFPIEVVT EGLLNIYQEL 400
    LGLSFEQVTD AHVWNKSVTL YTVKDKATGE VLGQFYLDLY PREGKYNHAA 450
    CFGLQPGCLL PDGSRMMSVA ALVVNFSQPL AGRPSLLRHD EVRTYFHEFG 500
    HVMHQICAQT DFARFSGTNV ETDFVEVPSQ MLENWVWDAD SLRRLSKHYR 550
    HGSPITDDLL EKLVASRLVN TGLLTLRQIV LSKVDQSLHT NTALDAASEY 600
    AKYCTEILGV AATPGTNMPA TFGHLAGGYD GQYYGYLWSE VFSMDMFYSC 650
    FKKEGIMNPE VGMKYRNLIL KPGGSLDGMD MLQNFLTREP NQKAFLMSRG 700
    LPAP 704
    Length:704
    Mass (Da):80,728
    Last modified:March 20, 2007 - v1
    Checksum:iF53622A4F7116FC8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC133350 mRNA. Translation: AAI33351.1.
    RefSeqiNP_001029161.2. NM_001033989.2.
    UniGeneiBt.40554.

    Genome annotation databases

    GeneIDi538650.
    KEGGibta:538650.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC133350 mRNA. Translation: AAI33351.1 .
    RefSeqi NP_001029161.2. NM_001033989.2.
    UniGenei Bt.40554.

    3D structure databases

    ProteinModelPortali A2VDQ5.
    SMRi A2VDQ5. Positions 37-701.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000022482.

    Protein family/group databases

    MEROPSi M03.002.

    Proteomic databases

    PRIDEi A2VDQ5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 538650.
    KEGGi bta:538650.

    Organism-specific databases

    CTDi 57486.

    Phylogenomic databases

    eggNOGi COG0339.
    HOGENOMi HOG000245985.
    HOVERGENi HBG000238.
    InParanoidi A2VDQ5.
    KOi K01393.

    Miscellaneous databases

    NextBioi 20877494.

    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. NIH - Mammalian Gene Collection (MGC) project
      Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Hypothalamus.

    Entry informationi

    Entry nameiNEUL_BOVIN
    AccessioniPrimary (citable) accession number: A2VDQ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: March 20, 2007
    Last modified: October 1, 2014
    This is version 54 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, 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