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    mmp16.L matrix metallopeptidase 16 L homeolog [ Xenopus laevis (African clawed frog) ]

    Gene ID: 443562, updated on 11-Apr-2024

    Summary

    Official Symbol
    mmp16.L
    Official Full Name
    matrix metallopeptidase 16 L homeolog
    Primary source
    Xenbase:XB-GENE-1007182
    Locus tag
    XELAEV_18032164mg
    See related
    EnsemblRapid:ENSXLAG00005031638
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Xenopus laevis
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus
    Also known as
    MMP24; mmp16; mt3-mmp
    NEW
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    Try the new Transcript table

    Genomic context

    Location:
    chromosome: 6L
    Exon count:
    12
    Annotation release Status Assembly Chr Location
    101 current Xenopus_laevis_v10.1 (GCF_017654675.1) 6L NC_054381.1 (135400541..135594846, complement)
    100 previous assembly Xenopus_laevis_v2 (GCF_001663975.1) 6L NC_030734.1 (126235982..126428734, complement)

    Chromosome 6L - NC_054381.1Genomic Context describing neighboring genes Neighboring gene cyclic nucleotide gated channel beta 3 L homeolog Neighboring gene uncharacterized LOC121394895 Neighboring gene paraneoplastic antigen Ma2-like Neighboring gene receptor interacting serine/threonine kinase 2 L homeolog

    Genomic regions, transcripts, and products

    Bibliography

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?

    General gene information

    Gene Ontology Provided by Xenbase

    Function Evidence Code Pubs
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
     
    enables metalloendopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
     
    enables metallopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
     
    enables zinc ion binding IEA
    Inferred from Electronic Annotation
    more info
     
    Process Evidence Code Pubs
    acts_upstream_of_or_within collagen catabolic process IEA
    Inferred from Electronic Annotation
    more info
     
    acts_upstream_of_or_within extracellular matrix organization IEA
    Inferred from Electronic Annotation
    more info
     
    acts_upstream_of_or_within proteolysis IEA
    Inferred from Electronic Annotation
    more info
     
    acts_upstream_of_or_within skeletal system development IEA
    Inferred from Electronic Annotation
    more info
     
    Component Evidence Code Pubs
    located_in extracellular matrix IEA
    Inferred from Electronic Annotation
    more info
     
    located_in extracellular region IEA
    Inferred from Electronic Annotation
    more info
     
    located_in extracellular space IEA
    Inferred from Electronic Annotation
    more info
     
    located_in membrane IEA
    Inferred from Electronic Annotation
    more info
     

    General protein information

    Preferred Names
    matrix metallopeptidase 16 L homeolog
    Names
    Membrane-type 3 matrix metalloproteinase
    matrix metallopeptidase 16 (membrane-inserted)
    matrix metalloproteinase MT3-MMP

    NCBI Reference Sequences (RefSeq)

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    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    mRNA and Protein(s)

    1. NM_001091793.1NP_001085262.1  matrix metallopeptidase 16 L homeolog precursor

      See identical proteins and their annotated locations for NP_001085262.1

      Status: PROVISIONAL

      Source sequence(s)
      AY310397
      UniProtKB/TrEMBL
      B7ZQB2, Q6W5M7
      Related
      ENSXLAP00005095293.1, ENSXLAT00005097024.1
      Conserved Domains (6) summary
      cd00094
      Location:346538
      HX; Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of ...
      cd04278
      Location:130295
      ZnMc_MMP; Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate ...
      pfam00413
      Location:130295
      Peptidase_M10; Matrixin
      pfam01471
      Location:4593
      PG_binding_1; Putative peptidoglycan binding domain
      pfam11857
      Location:543613
      DUF3377; Domain of unknown function (DUF3377)
      pfam12824
      Location:280334
      MRP-L20; Mitochondrial ribosomal protein subunit L20

    RefSeqs of Annotated Genomes: Xenopus laevis Annotation Release 101 details...Open this link in a new tab

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference Xenopus_laevis_v10.1 Primary Assembly

    Genomic

    1. NC_054381.1 Reference Xenopus_laevis_v10.1 Primary Assembly

      Range
      135400541..135594846 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_041565421.1XP_041421355.1  matrix metallopeptidase 16 L homeolog isoform X1

      UniProtKB/TrEMBL
      A0A8J1KVL8, B7ZQB2
      Related
      ENSXLAP00005095410.1, ENSXLAT00005097141.1
      Conserved Domains (3) summary
      PHA03247
      Location:277357
      PHA03247; large tegument protein UL36; Provisional
      cd00094
      Location:346538
      HX; Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of ...
      cd04278
      Location:130295
      ZnMc_MMP; Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate ...
    2. XM_041565423.1XP_041421357.1  matrix metallopeptidase 16 L homeolog isoform X3

      UniProtKB/TrEMBL
      A0A8J1KVM6, B7ZQB2
      Related
      ENSXLAP00005095355.1, ENSXLAT00005097086.1
      Conserved Domains (3) summary
      PHA03247
      Location:272352
      PHA03247; large tegument protein UL36; Provisional
      cd00094
      Location:341533
      HX; Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of ...
      cd04278
      Location:125290
      ZnMc_MMP; Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate ...
    3. XM_041565422.1XP_041421356.1  matrix metallopeptidase 16 L homeolog isoform X2

      UniProtKB/TrEMBL
      A0A8J1KVM5, B7ZQB2
      Conserved Domains (3) summary
      PHA03247
      Location:272352
      PHA03247; large tegument protein UL36; Provisional
      cd00094
      Location:341533
      HX; Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of ...
      cd04278
      Location:125290
      ZnMc_MMP; Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate ...