MMP3 matrix metallopeptidase 3 [Sus scrofa (pig)] - Gene

Summary

Gene symbol: MMP3
Gene description: matrix metallopeptidase 3
See related: Ensembl:ENSSSCG00000059078
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Sus scrofa
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus
Also known as: MMP-3; MMP10
Expression: Low expression observed in reference dataset See more
Orthologs: human all
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Genomic context

Location:: chromosome: 9

Exon count:: 10

Annotation release	Status	Assembly	Chr	Location
106	current	Sscrofa11.1 (GCF_000003025.6)	9	NC_010451.4 (33446969..33453995, complement)
105	previous assembly	Sscrofa10.2 (GCF_000003025.5)	9	NC_010451.3 (37394116..37401146, complement)

Chromosome 9 - NC_010451.4 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

The present study was aimed to determine the association between metalloproteinase 3 (MMP3), transforming growth factor beta 1 (TGFbeta1) and collagen type X alpha I (COL10A1) gene polymorphisms with traits related to leg weakness in pigs.
Title: Association and expression study of MMP3, TGFβ1 and COL10A1 as candidate genes for leg weakness-related traits in pigs.
the identification of MMP1 and MMP10 genes in swine is reported.
Title: Molecular characterization, mapping, and haplotype analysis of porcine matrix metalloproteinase genes MMP1 and MMP10.
Results indicate that leukemia inhibitory factor (LIF) and Oncostatin M increase the expression of MMP-1, MMP-3, and TIMP-1 several fold, and that their expression is reduced to basal levels in the presence of the LIF antagonist MH35-BD.
Title: Role of a LIF antagonist in LIF and OSM induced MMP-1, MMP-3, and TIMP-1 expression by primary articular chondrocytes.
contribution of MMPs to the inflammatory breakdown of the blood-CSF barrier in vitro
Title: MMPs contribute to TNF-alpha-induced alteration of the blood-cerebrospinal fluid barrier in vitro.

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General gene information

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Gene Ontology Provided by RefSeq

Function	Evidence Code	Pubs
enables metalloendopeptidase activity	IEA Inferred from Electronic Annotation more info	PubMed
enables zinc ion binding	IEA Inferred from Electronic Annotation more info	PubMed

Process	Evidence Code	Pubs
involved_in collagen catabolic process	IEA Inferred from Electronic Annotation more info	PubMed
involved_in extracellular matrix organization	IEA Inferred from Electronic Annotation more info	PubMed
involved_in proteolysis	IEA Inferred from Electronic Annotation more info	PubMed

Component	Evidence Code	Pubs
located_in extracellular matrix	IEA Inferred from Electronic Annotation more info	PubMed

General protein information

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Preferred Names: stromelysin-1

Names: matrix metallopeptidase 3 (stromelysin 1, progelatinase); matrix metalloproteinase-3; stromelysin

NP_001159780.1

EC 3.4.24.17

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)

NM_001166308.1 → NP_001159780.1 stromelysin-1 precursor

See identical proteins and their annotated locations for NP_001159780.1

Status: PROVISIONAL

Source sequence(s)

EU722907

UniProtKB/TrEMBL

A0A4X1TR59, C9VZX5, F1SV58

Related

ENSSSCP00000015910.2, ENSSSCT00000016349.4

Conserved Domains (4) summary

cd00094
Location:287 → 477

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:108 → 264

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:108 → 264

Peptidase_M10; Matrixin

pfam01471
Location:34 → 87

PG_binding_1; Putative peptidoglycan binding domain