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Q91YP2

- NEUL_MOUSE

UniProt

Q91YP2 - NEUL_MOUSE

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Protein
Neurolysin, mitochondrial
Gene
Nln
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript 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
  3. peptide binding Source: MGI
Complete GO annotation...

GO - Biological processi

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:1923055. Nln.

    Subcellular locationi

    Mitochondrion intermembrane space By similarity. Cytoplasm By similarity

    GO - Cellular componenti

    1. mitochondrial intermembrane space Source: UniProtKB-SubCell
    2. mitochondrion Source: MGI
    3. plasma membrane Source: MGI
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3737Mitochondrion
    Add
    BLAST
    Chaini38 – 704667Neurolysin, mitochondrial
    PRO_0000319046Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ91YP2.
    PaxDbiQ91YP2.
    PRIDEiQ91YP2.

    PTM databases

    PhosphoSiteiQ91YP2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ91YP2.
    BgeeiQ91YP2.
    CleanExiMM_NLN.
    GenevestigatoriQ91YP2.

    Interactioni

    Protein-protein interaction databases

    IntActiQ91YP2. 1 interaction.
    MINTiMINT-4122037.

    Structurei

    3D structure databases

    ProteinModelPortaliQ91YP2.
    SMRiQ91YP2. Positions 37-701.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M3 family.

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0339.
    GeneTreeiENSGT00550000074738.
    HOGENOMiHOG000245985.
    HOVERGENiHBG000238.
    KOiK01393.
    OMAiYENCLQV.
    OrthoDBiEOG7SR4KW.
    PhylomeDBiQ91YP2.
    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.

    Q91YP2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MITLCLSALR GLHRAGGSRI RLRMTLGREA ASPLQAMSSY TAAGRNVLRW    50
    DLSPEQIRTR TEELIAQTKQ VYDTVGTINL EDVTYENCLQ VLADIEVKYI 100
    VERTMLDFPQ HVSSDREVRA ASTEADKRLS RFDIEMSMRE DVFQRIVHLQ 150
    ETCDLEKIKP EARRYLEKSI KMGKRNGLHL PEHVKNEIKS MKKRMSELCI 200
    DFNKNLNEDD TSLVFSKAEL GALPDDFIDS LEKTDEDKYK VTLKYPHYFP 250
    VMKKCCVPET RRKMEMAFHT RCKEENTIIL QQLLPLRAQV AKLLGYNTHA 300
    DFVLELNTAK STSHVATFLD DLSQKLKPLG EAEREFILSL KKKECEERGF 350
    AYDGKINAWD LHYYMTQTEE LKYSVDQESL KEYFPIEVVT EGLLSIYQEL 400
    LGLSFEQVAD AHVWNKSVSL YTVKDKATGE VLGQFYLDLY PREGKYNHAA 450
    CFGLQPGCLL PDGSRMMSVA ALVVNFSQPI AGRPSLLRHD EVRTYFHEFG 500
    HVMHQICAQT DFARFSGTNV ETDFVEVPSQ MLENWVWDID SLRKLSKHYR 550
    DGHPITDELL EKLVASRLVN TGLLTLRQIV LSKVDQSLHT NASLDAASEY 600
    AKYCTEILGV AATPGTNMPA TFGHLAGGYD GQYYGYLWSE VFSMDMFHSC 650
    FRKEGIMNPE VGMKYRNLIL KPGGSLDGMD MLQNFLQREP NQKAFLMSRG 700
    LNAS 704
    Length:704
    Mass (Da):80,429
    Last modified:December 1, 2001 - v1
    Checksum:iE4F342E346AB0E07
    GO

    Sequence conflict

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti44 – 441G → V in BAE27114. 1 Publication
    Sequence conflicti329 – 3313LGE → HAS in AAH25520. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK079090 mRNA. Translation: BAC37533.1.
    AK146364 mRNA. Translation: BAE27114.1.
    BC016224 mRNA. Translation: AAH16224.1.
    BC025520 mRNA. Translation: AAH25520.1.
    CCDSiCCDS36772.1.
    RefSeqiNP_083723.1. NM_029447.2.
    UniGeneiMm.127692.

    Genome annotation databases

    EnsembliENSMUST00000109315; ENSMUSP00000104938; ENSMUSG00000021710.
    GeneIDi75805.
    KEGGimmu:75805.
    UCSCiuc007rsp.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK079090 mRNA. Translation: BAC37533.1 .
    AK146364 mRNA. Translation: BAE27114.1 .
    BC016224 mRNA. Translation: AAH16224.1 .
    BC025520 mRNA. Translation: AAH25520.1 .
    CCDSi CCDS36772.1.
    RefSeqi NP_083723.1. NM_029447.2.
    UniGenei Mm.127692.

    3D structure databases

    ProteinModelPortali Q91YP2.
    SMRi Q91YP2. Positions 37-701.
    ModBasei Search...

    Protein-protein interaction databases

    IntActi Q91YP2. 1 interaction.
    MINTi MINT-4122037.

    Protein family/group databases

    MEROPSi M03.002.

    PTM databases

    PhosphoSitei Q91YP2.

    Proteomic databases

    MaxQBi Q91YP2.
    PaxDbi Q91YP2.
    PRIDEi Q91YP2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000109315 ; ENSMUSP00000104938 ; ENSMUSG00000021710 .
    GeneIDi 75805.
    KEGGi mmu:75805.
    UCSCi uc007rsp.1. mouse.

    Organism-specific databases

    CTDi 57486.
    MGIi MGI:1923055. Nln.

    Phylogenomic databases

    eggNOGi COG0339.
    GeneTreei ENSGT00550000074738.
    HOGENOMi HOG000245985.
    HOVERGENi HBG000238.
    KOi K01393.
    OMAi YENCLQV.
    OrthoDBi EOG7SR4KW.
    PhylomeDBi Q91YP2.
    TreeFami TF300459.

    Miscellaneous databases

    NextBioi 344006.
    PROi Q91YP2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q91YP2.
    Bgeei Q91YP2.
    CleanExi MM_NLN.
    Genevestigatori Q91YP2.

    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 transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: BALB/c and C57BL/6J.
      Tissue: Diencephalon.
    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].
      Strain: FVB/N.
      Tissue: Mammary tumor.

    Entry informationi

    Entry nameiNEUL_MOUSE
    AccessioniPrimary (citable) accession number: Q91YP2
    Secondary accession number(s): Q3UJP1, Q8R3F4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: December 1, 2001
    Last modified: July 9, 2014
    This is version 96 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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