MMP2 matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase) [Homo sapiens] - Gene

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Summary

Official Symbol: MMP2provided by HGNC
Official Full Name: matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase)provided by HGNC
Primary source: HGNC:7166
See related: Ensembl:ENSG00000087245; HPRD:00386; MIM:120360; Vega:OTTHUMG00000133202
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: CLG4; MONA; CLG4A; TBE-1; MMP-II
Summary: Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. This gene encodes an enzyme which degrades type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response. Mutations in this gene have been associated with Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

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Genomic context

Location :: 16q13-q21

Sequence :: Chromosome: 16; NC_000016.9 (55513081..55540586)

See MMP2 in Epigenomics, MapViewer

Chromosome 16 - NC_000016.9 Genomic Context describing neighboring genes

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Genomic regions, transcripts, and products

Genomic Sequence

Go to nucleotideGraphics FASTA GenBank

Go to reference sequence details

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Bibliography

GeneRIFs: Gene References Into Functions What's a GeneRIF?

Pregnant women with pre-eclampsia had higher plasma MMP-2 and TIMP-2 concentrations than healthy pregnant women. MMP-2 genotypes and haplotypes were associated with significant alterations in plasma MMP-2 and TIMP-2 concentrations in preeclampsia.
Title: Association between matrix metalloproteinase (MMP)-2 polymorphisms and MMP-2 levels in hypertensive disorders of pregnancy.
study identified urotensin-II and NOX4 as new activators of FoxO3a, and MMP2 as a novel target gene of FoxO3a, and showed that activation of FoxO3a by this pathway promotes vascular growth
Title: NOX4 mediates activation of FoxO3a and matrix metalloproteinase-2 expression by urotensin-II.
Two strongly linked snps in MMP9 showed significant associations with subarachnoid hemorrhage in men
Title: No evidence for an association between genetic variation at the MMP2 and MMP9 loci and aneurysmal subarachnoid haemorrhage.
activated platelets may be a major source of MMP-1 and to a minor extent MMP-2, in peripheral blood.
Title: Release of matrix metalloproteinases-1 and -2, but not -9, from activated platelets measured by enzyme-linked immunosorbent assay.
Zoledronic acid can inhibit the in vitro proliferation and invasion of HNE1 cell through suppressing the secretion of VEGF and suppressing MMP2 and MMP9 activity.
Title: [Inhibitory effects of zoledronic acid on cell proliferation and invasion in human nasopharyngeal carcinoma cell line HNE1].
Report activity of MMP2/9 and TIMP-1 in electromagnetic field-exposed THP-1 cells.
Title: Activity of matrix metallo proteinases (MMPs) and the tissue inhibitor of MMP (TIMP)-1 in electromagnetic field-exposed THP-1 cells.
analysis of secretory dynamics of MMP-2 and the specific sites for polarized distribution of MMP-2 on the cell surface
Title: Video-rate bioluminescence imaging of matrix metalloproteinase-2 secreted from a migrating cell.
Expressions of LOX and MMP-2 in gastric cancer tissues are significantly higher than that in pericancerous tissues, and are also higher in gastric cancer with lymph node metastasis.
Title: [Expression of LOX and MMP-2 in gastric cancer tissue and the effects of LOX and MMP-2 on tumor invasion and metastasis].
A significant inverse relationship between miR-29a and total MMP-2 was identified in the thoracic aortic aneurysm specimens.
Title: Selective microRNA suppression in human thoracic aneurysms: relationship of miR-29a to aortic size and proteolytic induction.
The role of MMP-2 expression in the prognosis of invasive ductal carcinoma of the breast is rather limited.
Title: Matrix metalloproteinase-2 (MMP-2) and MMP-9 expression in invasive ductal carcinoma of the breast.

Submit: New GeneRIF Correction See all (770)

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Phenotypes

Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

HIV-1 protein interactions

Protein	Gene	Interaction	Pubs
Envelope surface glycoprotein gp120	env	HIV-1 gp120 interaction with human mannose receptor (hMR) results in increased production of matrix metalloproteinase-2 (MMP-2) in astrocytes	PubMed
Envelope transmembrane glycoprotein gp41	env	Treatment of human glial and neuronal cells with an HIV-1 gp41 peptide (amino acids 583-599) markedly increases the activity of matrix metalloproteinase 2 (MMP-2)	PubMed
Tat	tat	HIV-1 Tat and methamphetamine enhance the release of MMP-1, MMP-2, and uPA from human brain cells	PubMed
	tat	HIV-1 Tat and bFGF synergize to upregulate MMP-2 (type-IV collagenase) secretion and activation in endothelial cells and also synergize in inducing angiogenic Kaposi's sarcoma-like lesions in mice as a result of enhanced MMP-2 expression	PubMed
	tat	HIV-1 Tat from AIDS patients with HIV-associated dementia upregulates MMP-2 and MMP-7 release and activation, leading to neurotoxicity	PubMed

Go to the HIV-1, Human Protein Interaction Database

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Products	Interactant	Other Gene	Source	Pubs	Description
P08253	P01023	A2M	HPRD	PubMed
P08253	P16112	ACAN	HPRD	PubMed
P08253	P56817	BACE1	HPRD	PubMed
P08253	Q96GW7	BCAN	HPRD	PubMed
P08253	P80098	CCL7	HPRD	PubMed
P08253	O95832	CLDN1	HPRD	PubMed
P08253	P39060	COL18A1	HPRD	PubMed
P08253	P02452	COL1A1	HPRD	PubMed
P08253	P12111	COL6A3	HPRD	PubMed
P08253	Q02388	COL7A1	HPRD	PubMed
P08253	P48061	CXCL12	HPRD	PubMed
P08253	P07585	DCN	HPRD	PubMed
P08253	P29323	EPHB2	HPRD	PubMed
P08253	P11362	FGFR1	HPRD	PubMed
P08253	P10915	HAPLN1	HPRD	PubMed
P08253	P07900	HSP90AA1	HPRD	PubMed
P08253	P17936	IGFBP3	HPRD	PubMed
P08253	P01584	IL1B	HPRD	PubMed
P08253	P06756	ITGAV	HPRD	PubMed
P08253	Q15726	KISS1	HPRD	PubMed
P08253	P80188	LCN2	HPRD	PubMed
P08253	P17931	LGALS3	HPRD	PubMed
P08253	P50281	MMP14	HPRD	PubMed
P08253	Q9ULZ9	MMP17	HPRD	PubMed
P08253	Q9NPA2	MMP25	HPRD	PubMed
P08253	P20742	PZP	HPRD	PubMed
P08253	Q08629	SPOCK1	HPRD	PubMed
P08253	P01137	TGFB1	HPRD	PubMed
P08253	P07996	THBS1	HPRD	PubMed
P08253	P35442	THBS2	HPRD	PubMed
P08253	P01033	TIMP1	HPRD	PubMed
P08253	P16035	TIMP2	HPRD	PubMed
P08253	P35625	TIMP3	HPRD	PubMed
P08253	Q99727	TIMP4	HPRD	PubMed
BioGRID:110457	BioGRID:106524	A2M	BioGRID	PubMed	Reconstituted Complex
BioGRID:110457	BioGRID:121964	BCAN	BioGRID	PubMed	Biochemical Activity
BioGRID:110457	BioGRID:112257	CCL7	BioGRID	PubMed	Affinity Capture-Western; Biochemical Activity; Reconstituted Complex; Two-hybrid
BioGRID:110457	BioGRID:107674	COL1A1	BioGRID	PubMed	Reconstituted Complex
BioGRID:110457	BioGRID:110126	LCN2	BioGRID	PubMed	Affinity Capture-Western
BioGRID:110457	BioGRID:125385	OSBPL10	BioGRID	PubMed	Affinity Capture-MS
BioGRID:110457	BioGRID:111796	PZP	BioGRID	PubMed	Reconstituted Complex
BioGRID:110457	BioGRID:112898	TGFB1	BioGRID	PubMed	Biochemical Activity
BioGRID:110457	BioGRID:112915	THBS1	BioGRID	PubMed	Affinity Capture-Western; Two-hybrid
BioGRID:110457	BioGRID:112916	THBS2	BioGRID	PubMed	Affinity Capture-Western; Two-hybrid
BioGRID:110457	BioGRID:112933	TIMP2	BioGRID	PubMed	Co-crystal Structure; Reconstituted Complex; Two-hybrid
BioGRID:110457	BioGRID:112934	TIMP3	BioGRID	PubMed	Reconstituted Complex
BioGRID:110457	BioGRID:112935	TIMP4	BioGRID	PubMed	Reconstituted Complex
BioGRID:110457	BioGRID:128522	USP12	BioGRID	PubMed	Affinity Capture-MS

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

Process	Evidence Code	Pubs
angiogenesis	IEA Inferred from Electronic Annotation more info
blood vessel maturation	IEA Inferred from Electronic Annotation more info
bone trabecula formation	IEA Inferred from Electronic Annotation more info
cellular response to amino acid stimulus	IEA Inferred from Electronic Annotation more info
collagen catabolic process	IEA Inferred from Electronic Annotation more info
face morphogenesis	IEA Inferred from Electronic Annotation more info
intramembranous ossification	IEA Inferred from Electronic Annotation more info
metabolic process	IEA Inferred from Electronic Annotation more info
proteolysis	IEA Inferred from Electronic Annotation more info
response to hypoxia	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
extracellular region	TAS Traceable Author Statement more info
extracellular space	IDA Inferred from Direct Assay more info
nucleus	IEA Inferred from Electronic Annotation more info
plasma membrane	IEA Inferred from Electronic Annotation more info
proteinaceous extracellular matrix	IEA Inferred from Electronic Annotation more info
sarcomere	IEA Inferred from Electronic Annotation more info

General protein information

Preferred Names: 72 kDa type IV collagenase

Names: 72 kDa type IV collagenase; MMP-2; gelatinase A; 72 kDa gelatinase; collagenase type IV-A; neutrophil gelatinase; matrix metalloproteinase-2; matrix metalloproteinase-II

NP_001121363.1

EC 3.4.24.24

NP_004521.1

EC 3.4.24.24

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NCBI Reference Sequences (RefSeq)

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.

Genomic

NG_008989.1 RefSeqGene

Range

5001..32506

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001127891.1 → NP_001121363.1 72 kDa type IV collagenase isoform b

Status: REVIEWED

Description

Transcript Variant: This variant (2) differs in the 5' UTR and coding sequence compared to variant 1. The resulting isoform (b) has a shorter and distinct N-terminus compared to isoform a.

Source sequence(s)

AC007336, AK310314, AK312711, AL046162, CA446916, DB059054, J03210

Consensus CDS

CCDS45487.1

UniProtKB/TrEMBL

E9PE45

UniProtKB/Swiss-Prot

P08253

Related

ENSP00000394237, OTTHUMP00000254842, ENST00000437642, OTTHUMT00000433261

Conserved Domains (5) summary

cd00062
Location:293 – 340
Blast Score: 202

FN2; Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and ...

cd00094
Location:417 – 610
Blast Score: 545

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:68 – 166
Blast Score: 391

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 ...

cl00064
Location:331 – 396
Blast Score: 245

ZnMc; Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which ...

cl15437
Location:2 – 47
Blast Score: 106

PG_binding_1; Putative peptidoglycan binding domain
NM_004530.4 → NP_004521.1 72 kDa type IV collagenase isoform a preproprotein

Status: REVIEWED

Description

Transcript Variant: This variant (1) represents the longer transcript and encodes the longer isoform (a).

Source sequence(s)

AK310314, AK312711, AL046162, AU279927, CA446916, DB154582, J03210

Consensus CDS

CCDS10752.1

UniProtKB/Swiss-Prot

P08253

Related

ENSP00000219070, OTTHUMP00000164261, ENST00000219070, OTTHUMT00000256913

Conserved Domains (5) summary

cd00062
Location:343 – 390
Blast Score: 205

FN2; Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and ...

cd00094
Location:467 – 660
Blast Score: 549

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:118 – 216
Blast Score: 392

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 ...

cl00064
Location:381 – 446
Blast Score: 246

ZnMc; Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which ...

cl15437
Location:48 – 97
Blast Score: 106

PG_binding_1; Putative peptidoglycan binding domain

RefSeqs of Annotated Genomes: Build 37.3

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

Reference GRCh37.p5 Primary Assembly

Genomic

NC_000016.9 Reference GRCh37.p5 Primary Assembly

Range

55513081..55540586

Download

GenBank, FASTA, Sequence Viewer (Graphics)

Alternate HuRef

Genomic

AC_000148.1 Alternate HuRef

Range

41400533..41427983

Download

GenBank, FASTA, Sequence Viewer (Graphics)

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Related Sequences

Nucleotide		Protein
Heading	Accession and Version	Protein
genomic	AC007336.6 (94628..122143)	None
genomic	AJ298926.1	None
genomic	AY738117.1	AAU10089.1
genomic	CH471092.1	EAW82824.1
		EAW82825.1
		EAW82826.1
		EAW82827.1
		EAW82828.1
genomic	FB571114.1	CAR95108.1
genomic	FB668245.1	CAS92766.1
genomic	M33789.1	AAA52027.1
genomic	M55582.1	AAA52028.1
genomic	M55583.1	AAA52028.1
genomic	M55584.1	AAA52028.1
genomic	M55585.1	AAA52028.1
genomic	M55586.1	AAA52028.1
genomic	M55587.1	AAA52028.1
genomic	M55588.1	AAA52028.1
genomic	M55589.1	AAA52028.1
genomic	M55590.1	AAA52028.1
genomic	M55591.1	AAA52028.1
genomic	M55592.1	AAA52028.1
genomic	M55593.1	AAA52028.1
genomic	M58552.1	AAA52028.1
genomic	U96098.1	None
mRNA	AK301536.1	BAG63035.1
mRNA	AK310314.1	None
mRNA	AK312711.1	BAG35588.1
mRNA	AL046162.1	None
mRNA	AL542407.3	None
mRNA	AL832088.1	None
mRNA	AU279927.1	None
mRNA	BC002576.2	AAH02576.1
mRNA	BQ004983.1	None
mRNA	CA446916.1	None
mRNA	DA993141.1	None
mRNA	DB059054.1	None
mRNA	DB154582.1	None
mRNA	DQ385623.1	ABD38929.1
mRNA	J03210.1	AAA35701.1
mRNA	X58968.1	None
other-genetic	DQ891952.2	ABM82878.1
other-genetic	DQ895138.2	ABM86064.1