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P42676

- NEUL_RAT

UniProt

P42676 - NEUL_RAT

Protein

Neurolysin, mitochondrial

Gene

Nln

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (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.

    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
    3. peptide binding Source: Ensembl

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 2

    Organism-specific databases

    RGDi621518. Nln.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial intermembrane space Source: UniProtKB-SubCell
    2. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3737Mitochondrion1 PublicationAdd
    BLAST
    Chaini38 – 704667Neurolysin, mitochondrialPRO_0000028578Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP42676.
    PRIDEiP42676.

    PTM databases

    PhosphoSiteiP42676.

    Miscellaneous databases

    PMAP-CutDBP42676.

    Expressioni

    Gene expression databases

    GenevestigatoriP42676.

    Interactioni

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000059652.

    Structurei

    Secondary structure

    1
    704
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni43 – 453
    Helixi54 – 7522
    Helixi80 – 823
    Turni85 – 884
    Helixi89 – 10719
    Helixi109 – 1124
    Helixi116 – 13722
    Helixi140 – 15213
    Helixi160 – 17516
    Turni176 – 1794
    Helixi182 – 1876
    Helixi189 – 20820
    Beta strandi212 – 2165
    Turni217 – 2226
    Helixi225 – 2295
    Beta strandi231 – 2333
    Beta strandi235 – 24410
    Helixi245 – 25410
    Helixi258 – 26811
    Turni269 – 2724
    Helixi273 – 29321
    Helixi299 – 3046
    Helixi312 – 34736
    Helixi358 – 3603
    Helixi361 – 37212
    Helixi377 – 3804
    Helixi381 – 3833
    Helixi386 – 40116
    Beta strandi403 – 4075
    Beta strandi419 – 4257
    Turni426 – 4283
    Beta strandi431 – 4388
    Beta strandi450 – 4556
    Beta strandi468 – 4736
    Beta strandi481 – 4833
    Helixi489 – 50719
    Beta strandi510 – 5123
    Helixi513 – 5153
    Turni522 – 5265
    Helixi527 – 5337
    Helixi534 – 5374
    Helixi539 – 5457
    Beta strandi549 – 5513
    Helixi557 – 5659
    Turni566 – 5705
    Helixi571 – 58818
    Helixi596 – 60611
    Helixi618 – 6214
    Beta strandi625 – 6284
    Helixi635 – 64915
    Helixi651 – 6544
    Helixi659 – 66911
    Turni670 – 6723
    Helixi673 – 6753
    Helixi678 – 6869
    Helixi693 – 6997

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1I1IX-ray2.30P24-704[»]
    2O3EX-ray2.20A24-701[»]
    4FXYX-ray2.80P/Q24-704[»]
    ProteinModelPortaliP42676.
    SMRiP42676. Positions 37-701.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP42676.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M3 family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0339.
    GeneTreeiENSGT00550000074738.
    HOGENOMiHOG000245985.
    HOVERGENiHBG000238.
    InParanoidiQ6GQQ4.
    KOiK01393.
    OrthoDBiEOG7SR4KW.
    PhylomeDBiP42676.
    TreeFamiTF300459.

    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.

    P42676-1 [UniParc]FASTAAdd to Basket

    « Hide

    MITLCLSTLR GLHRAGGSRL QLTMTLGKEL ASPLQAMSSY TAAGRNVLRW    50
    DLSPEQIKTR TEQLIAQTKQ VYDTVGTIAL KEVTYENCLQ VLADIEVTYI 100
    VERTMLDFPQ HVSSDREVRA ASTEADKKLS RFDIEMSMRE DVFQRIVHLQ 150
    ETCDLEKIKP EARRYLEKSI KMGKRNGLHL SEHIRNEIKS MKKRMSELCI 200
    DFNKNLNEDD TSLVFSKAEL GALPDDFIDS LEKTDEDKYK VTLKYPHYFP 250
    VMKKCCVPET RRKMEMAFHT RCKQENTAIL QQLLPLRAQV AKLLGYNTHA 300
    DFVLELNTAK STSRVAAFLD DLSQKLKPLG EAEREFILSL KKKECEERGF 350
    EYDGKINAWD LHYYMTQTEE LKYSVDQESL KEYFPIEVVT EGLLSIYQEL 400
    LGLSFEQVPD AHVWNKSVSL YTVKDKATGE VLGQFYLDLY PREGKYNHAA 450
    CFGLQPGCLL PDGSRMMSVA ALVVNFSQPV AGRPSLLRHD EVRTYFHEFG 500
    HVMHQICAQT DFARFSGTNV ETDFVEVPSQ MLENWVWDVD SLRKLSKHYK 550
    DGHPITDELL EKLVASRLVN TGLLTLRQIV LSKVDQSLHT NATLDAASEY 600
    AKYCTEILGV AATPGTNMPA TFGHLAGGYD GQYYGYLWSE VFSMDMFHSC 650
    FKKEGIMNPE VGMKYRNLIL KPGGSLDGMD MLQNFLQREP NQKAFLMSRG 700
    LNGS 704
    Length:704
    Mass (Da):80,254
    Last modified:November 1, 1995 - v1
    Checksum:iE33F7967A79343D1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti128 – 1281K → R in AAH72687. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X87157 mRNA. Translation: CAA60630.1.
    BC072687 mRNA. Translation: AAH72687.1.
    RefSeqiNP_446422.2. NM_053970.2.
    UniGeneiRn.11029.

    Genome annotation databases

    EnsembliENSRNOT00000066925; ENSRNOP00000059652; ENSRNOG00000011561.
    GeneIDi117041.
    KEGGirno:117041.
    UCSCiRGD:621518. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X87157 mRNA. Translation: CAA60630.1 .
    BC072687 mRNA. Translation: AAH72687.1 .
    RefSeqi NP_446422.2. NM_053970.2.
    UniGenei Rn.11029.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1I1I X-ray 2.30 P 24-704 [» ]
    2O3E X-ray 2.20 A 24-701 [» ]
    4FXY X-ray 2.80 P/Q 24-704 [» ]
    ProteinModelPortali P42676.
    SMRi P42676. Positions 37-701.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000059652.

    Protein family/group databases

    MEROPSi M03.002.

    PTM databases

    PhosphoSitei P42676.

    Proteomic databases

    PaxDbi P42676.
    PRIDEi P42676.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000066925 ; ENSRNOP00000059652 ; ENSRNOG00000011561 .
    GeneIDi 117041.
    KEGGi rno:117041.
    UCSCi RGD:621518. rat.

    Organism-specific databases

    CTDi 57486.
    RGDi 621518. Nln.

    Phylogenomic databases

    eggNOGi COG0339.
    GeneTreei ENSGT00550000074738.
    HOGENOMi HOG000245985.
    HOVERGENi HBG000238.
    InParanoidi Q6GQQ4.
    KOi K01393.
    OrthoDBi EOG7SR4KW.
    PhylomeDBi P42676.
    TreeFami TF300459.

    Miscellaneous databases

    EvolutionaryTracei P42676.
    NextBioi 619847.
    PMAP-CutDB P42676.
    PROi P42676.

    Gene expression databases

    Genevestigatori P42676.

    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. "Molecular cloning and expression of rat brain endopeptidase 3.4.24.16."
      Dauch P., Vincent J.-P., Checler F.
      J. Biol. Chem. 270:27266-27271(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Brain.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lung.
    3. "Characterization of a mitochondrial metallopeptidase reveals neurolysin as a homologue of thimet oligopeptidase."
      Serizawa A., Dando P.M., Barrett A.J.
      J. Biol. Chem. 270:2092-2098(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 38-57, CHARACTERIZATION.
      Tissue: Liver.
    4. "Structure of neurolysin reveals a deep channel that limits substrate access."
      Brown C.K., Madauss K., Lian W., Beck M.R., Tolbert W.D., Rodgers D.W.
      Proc. Natl. Acad. Sci. U.S.A. 98:3127-3132(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

    Entry informationi

    Entry nameiNEUL_RAT
    AccessioniPrimary (citable) accession number: P42676
    Secondary accession number(s): Q6GQQ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 118 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3