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mmp13a matrix metallopeptidase 13a [ Danio rerio (zebrafish) ]

Gene ID: 387293, updated on 16-Oct-2021

Summary

Official Symbol
mmp13aprovided by ZNC
Official Full Name
matrix metallopeptidase 13aprovided by ZNC
Primary source
ZFIN:ZDB-GENE-031202-2
See related
Ensembl:ENSDARG00000012395
Gene type
protein coding
RefSeq status
VALIDATED
Organism
Danio rerio
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; Danionidae; Danioninae; Danio
Also known as
mmp13; cb1034
Orthologs
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Genomic context

See mmp13a in Genome Data Viewer
Location:
chromosome: 10
Exon count:
13
Annotation release Status Assembly Chr Location
106 current GRCz11 (GCF_000002035.6) 10 NC_007121.7 (38593657..38619868)
105 previous assembly GRCz10 (GCF_000002035.5) 10 NC_007121.6 (38649900..38676124)
103 previous assembly Zv9 (GCF_000002035.4) 10 NC_007121.5 (39959929..39968812)

Chromosome 10 - NC_007121.7Genomic Context describing neighboring genes Neighboring gene alkaline ceramidase 3 Neighboring gene matrix metalloproteinase-18-like Neighboring gene uncharacterized LOC103911776 Neighboring gene matrix metallopeptidase 30

Genomic regions, transcripts, and products

Expression

  • Project title: Sequencing the Zebrafish transcriptome from a range of tissues and developmental stages
  • Description: Sequencing the Zebrafish transcriptome from a range of tissues and developmental stages
  • BioProject: PRJEB1986
  • Analysis date: Fri Dec 8 19:48:10 2017

Bibliography

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

General gene information

Markers

Homology

Gene Ontology Provided by ZFIN

Function Evidence Code Pubs
enables hydrolase activity IEA
Inferred from Electronic Annotation
more info
 
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
 
enables metalloendopeptidase activity IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
enables metalloendopeptidase activity IEA
Inferred from Electronic Annotation
more info
 
enables metallopeptidase activity IEA
Inferred from Electronic Annotation
more info
 
enables peptidase activity IEA
Inferred from Electronic Annotation
more info
 
enables zinc ion binding IEA
Inferred from Electronic Annotation
more info
 
Process Evidence Code Pubs
involved_in collagen catabolic process IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
involved_in extracellular matrix organization IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
acts_upstream_of_or_within macrophage chemotaxis IMP
Inferred from Mutant Phenotype
more info
PubMed 
acts_upstream_of_or_within proteolysis IEA
Inferred from Electronic Annotation
more info
 
Component Evidence Code Pubs
located_in extracellular matrix IEA
Inferred from Electronic Annotation
more info
 

General protein information

Preferred Names
collagenase 3a; matrix metalloproteinase 13a
Names
MMPLg
MMPLh
matrix metallopeptidase 13a (collagenase 3)
matrix metalloproteinase 13
NP_001277408.1
XP_009303831.1

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_001290479.1NP_001277408.1  collagenase 3a precursor

    Status: VALIDATED

    Source sequence(s)
    LO018336
    UniProtKB/TrEMBL
    F1QCX8
    Conserved Domains (4) summary
    cd00094
    Location:286475
    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:112268
    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:112268
    Peptidase_M10; Matrixin
    pfam01471
    Location:2891
    PG_binding_1; Putative peptidoglycan binding domain

RefSeqs of Annotated Genomes: Danio rerio Annotation Release 106 details...Open this link in a new tab

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

Reference GRCz11 Primary Assembly

Genomic

  1. NC_007121.7 Reference GRCz11 Primary Assembly

    Range
    38593657..38619868
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_009305556.3XP_009303831.1  matrix metalloproteinase 13a isoform X1

    UniProtKB/TrEMBL
    F1R3P5
    Related
    ENSDARP00000012407.7, ENSDART00000011573.9
    Conserved Domains (4) summary
    cd00094
    Location:286475
    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:112268
    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:112268
    Peptidase_M10; Matrixin
    pfam01471
    Location:2891
    PG_binding_1; Putative peptidoglycan binding domain

Suppressed Reference Sequence(s)

The following Reference Sequences have been suppressed. Explain

  1. NM_201503.1: Suppressed sequence

    Description
    NM_201503.1: This RefSeq was permanently suppressed because currently there is insufficient support for the transcript and the protein.
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