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

Gene ID: 443562, updated on 4-Nov-2024

Summary

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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 AllianceGenome:Xenbase:XB-GENE-1007182
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
Summary
Predicted to enable metalloendopeptidase activity and zinc ion binding activity. Predicted to act upstream of or within several processes, including collagen catabolic process; extracellular matrix organization; and skeletal system development. Predicted to be located in extracellular matrix; extracellular space; and membrane. Is expressed in musculoskeletal system; nervous system; vestibuloauditory system; and visual system. Orthologous to human MMP16 (matrix metallopeptidase 16). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See mmp16.L in Genome Data Viewer
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

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Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Soluble membrane-type 3 matrix metalloprioteinase causes changes in gene expression and increased gelatinase activity during Xenopus laevis development. Walsh LA, et al. Int J Dev Biol, 2007. PMID 17616928
  2. Cloning and developmental characterization of Xenopus laevis membrane type-3 matrix metalloproteinase (MT3-MMP). Hammoud L, et al. Biochem Cell Biol, 2006 Apr. PMID 16609697
  3. Membrane type-1 matrix metalloproteinases and tissue inhibitor of metalloproteinases-2 RNA levels mimic each other during Xenopus laevis metamorphosis. Walsh LA, et al. PLoS One, 2007 Oct 3. PMID 17912339, Free PMC Article
  4. Genetic and genomic tools for Xenopus research: The NIH Xenopus initiative. Klein SL, et al. Dev Dyn, 2002 Dec. PMID 12454917
  5. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Strausberg RL, et al. Proc Natl Acad Sci U S A, 2002 Dec 24. PMID 12477932, Free PMC Article

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. metamorphic tail and intestine RNA levels of TIMP-2, MT1-MMP and Gel-A, but not MT3-MMP or TIMP-3, are elevated during periods of cell death and proliferation
    Title: Membrane type-1 matrix metalloproteinases and tissue inhibitor of metalloproteinases-2 RNA levels mimic each other during Xenopus laevis metamorphosis.
  2. embryos injected with the soluble form of MT3-MMP exhibited decreased expression of these same marker genes
    Title: Soluble membrane-type 3 matrix metalloprioteinase causes changes in gene expression and increased gelatinase activity during Xenopus laevis development.
  3. MT3-MMP expression is spatially and temporally restricted
    Title: Cloning and developmental characterization of Xenopus laevis membrane type-3 matrix metalloproteinase (MT3-MMP).
Submit: New GeneRIF Correction

General gene information

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Homology

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 space IEA
Inferred from Electronic Annotation
more info
  
located_in membrane IEA
Inferred from Electronic Annotation
more info
  

General protein information

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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_001091793.1 → NP_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:346 → 538
    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:130 → 295
    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:130 → 295
    Peptidase_M10; Matrixin
    pfam01471
    Location:45 → 93
    PG_binding_1; Putative peptidoglycan binding domain
    pfam11857
    Location:543 → 613
    DUF3377; Domain of unknown function (DUF3377)
    pfam12824
    Location:280 → 334
    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_041565421.1 → XP_041421355.1  matrix metallopeptidase 16 L homeolog isoform X1

    UniProtKB/TrEMBL
    A0A8J1KVL8, B7ZQB2
    Related
    ENSXLAP00005095410.1, ENSXLAT00005097141.1
    Conserved Domains (3) summary
    PHA03247
    Location:277 → 357
    PHA03247; large tegument protein UL36; Provisional
    cd00094
    Location:346 → 538
    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:130 → 295
    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_041565423.1 → XP_041421357.1  matrix metallopeptidase 16 L homeolog isoform X3

    UniProtKB/TrEMBL
    A0A8J1KVM6, B7ZQB2
    Related
    ENSXLAP00005095355.1, ENSXLAT00005097086.1
    Conserved Domains (3) summary
    PHA03247
    Location:272 → 352
    PHA03247; large tegument protein UL36; Provisional
    cd00094
    Location:341 → 533
    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:125 → 290
    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_041565422.1 → XP_041421356.1  matrix metallopeptidase 16 L homeolog isoform X2

    UniProtKB/TrEMBL
    A0A8J1KVM5, B7ZQB2
    Conserved Domains (3) summary
    PHA03247
    Location:272 → 352
    PHA03247; large tegument protein UL36; Provisional
    cd00094
    Location:341 → 533
    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:125 → 290
    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 ...
Nucleotide Protein Strain
Heading Accession and Version

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