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Q5R9V6

- NEUL_PONAB

UniProt

Q5R9V6 - NEUL_PONAB

Protein

Neurolysin, mitochondrial

Gene

NLN

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      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
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: 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_0000319048Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiQ5R9V6.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5R9V6.
    SMRiQ5R9V6. Positions 37-701.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M3 family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    HOVERGENiHBG000238.
    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.

    Q5R9V6-1 [UniParc]FASTAAdd to Basket

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    MIARCLLAVR SLRRVGGSRI LLRMTLGREV MSPLQAMSSY TVTGRNVLRW    50
    DLSPEQIKTR TEELIVQTKQ VYDAVGMLGI EEVTYENCLQ ALADIEVKYI 100
    VERTMLDFPQ HVSSDKEVRA ASTEADKRLS RFDIEMSMRG DIFERIVRLQ 150
    ETCDLGKIKP EARRYLEKSI KMGKRNGLHL PEQVQNEIKS MKKRMSELCI 200
    DFNKNLNEDD TFLVFSKAEL GALPDDFIDS LEKIDDDKYK ITLKYPHYFP 250
    VMKKCCIPET RRRMEMAFNT RCKEENTIIL QQLLPLRAKV AKLLGYSTHA 300
    DFVLEMNTAK STSRVTAFLD DLSQKLKPLG EAEREFILNL KKKECEDRGF 350
    EYDGKINAWD LYYYMTQTEE LKYSIDQEFL KEYFPIEVVT EGLLNTYQEL 400
    LGLSFEQVTD AHVWNKNVTL YTVKDKATGE VLGQFYLDLY PRDRKYNHAA 450
    CFGLQPGCLL PDGSRMMAVA ALVVNFSQPV AGRPSLLRHD EVRTYFHEFG 500
    HVMHQICAQT DFARFSGTNV ETDFVEVPSQ MLENWVWDVD SLRRLSKHYK 550
    DGSPISDDLL EKLVASRLIN TGLLTLRQIV LSKVDQSLHT NTSLDAASEY 600
    AKYCSEILGV AATPGTNMPA TFGHLAGGYD GQYYGYLWSE VFSMDMFYSC 650
    FKKEGIMNPE VGMKYRNLIL KPGGSLDGMD MLHNFLKREP NQKAFLMSRG 700
    LHAS 704
    Length:704
    Mass (Da):80,798
    Last modified:December 21, 2004 - v1
    Checksum:iCDE234F0F169D7C8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR859276 mRNA. Translation: CAH91454.1.
    RefSeqiNP_001127421.1. NM_001133949.2.
    UniGeneiPab.7982.

    Genome annotation databases

    GeneIDi100174491.
    KEGGipon:100174491.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR859276 mRNA. Translation: CAH91454.1 .
    RefSeqi NP_001127421.1. NM_001133949.2.
    UniGenei Pab.7982.

    3D structure databases

    ProteinModelPortali Q5R9V6.
    SMRi Q5R9V6. Positions 37-701.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M03.002.

    Proteomic databases

    PRIDEi Q5R9V6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100174491.
    KEGGi pon:100174491.

    Organism-specific databases

    CTDi 57486.

    Phylogenomic databases

    HOVERGENi HBG000238.
    KOi K01393.

    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. The German cDNA consortium
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain cortex.

    Entry informationi

    Entry nameiNEUL_PONAB
    AccessioniPrimary (citable) accession number: Q5R9V6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 56 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