P09237 (MMP7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Matrilysin
EC=3.4.24.23

Alternative name(s):
Matrin
Matrix metalloproteinase-7
Short name=MMP-7
Pump-1 protease
Uterine metalloproteinase

Gene names

Name:	MMP7
Synonyms:	MPSL1, PUMP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	267 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase. Ref.7
Catalytic activity	Cleavage of 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in B chain of insulin. No action on collagen types I, II, IV, V. Cleaves gelatin chain alpha-2(I) > alpha-1(I).
Cofactor	Binds 2 calcium ions per subunit. Binds 2 zinc ions per subunit.
Subcellular location	Secreted › extracellular space › extracellular matrix Probable.
Domain	The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Sequence similarities	Belongs to the peptidase M10A family.

Ontologies

Keywords
Biological process	Collagen degradation
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	Calcium Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	antibacterial peptide secretion Inferred from electronic annotation. Source: Compara collagen catabolic process Traceable author statement. Source: Reactome defense response to Gram-negative bacterium Inferred from electronic annotation. Source: Compara defense response to Gram-positive bacterium Inferred from electronic annotation. Source: Compara extracellular matrix disassembly Traceable author statement. Source: Reactome proteolysis Traceable author statement Ref.2. Source: ProtInc regulation of cell proliferation Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular space Traceable author statement Ref.2. Source: ProtInc proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metalloendopeptidase activity Traceable author statement Ref.2. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Ref.6

Propeptide

18 – 94

77

Activation peptide

PRO_0000028738

Chain

95 – 267

173

Matrilysin

PRO_0000028739

Regions

Motif

85 – 92

8

Cysteine switch By similarity

Sites

Active site

215

1

Metal binding

87

1

Zinc 2; in inhibited form By similarity

Metal binding

153

1

Calcium 1

Metal binding

163

1

Zinc 1

Metal binding

165

1

Zinc 1

Metal binding

170

1

Calcium 2

Metal binding

171

1

Calcium 2; via carbonyl oxygen

Metal binding

173

1

Calcium 2; via carbonyl oxygen

Metal binding

175

1

Calcium 2; via carbonyl oxygen

Metal binding

178

1

Zinc 1

Metal binding

185

1

Calcium 1; via carbonyl oxygen

Metal binding

187

1

Calcium 1; via carbonyl oxygen

Metal binding

189

1

Calcium 1

Metal binding

191

1

Zinc 1

Metal binding

193

1

Calcium 2

Metal binding

196

1

Calcium 2

Metal binding

214

1

Zinc 2; catalytic

Metal binding

218

1

Zinc 2; catalytic

Metal binding

224

1

Zinc 2; catalytic

Natural variations

Natural variant

77

1

R → H. Ref.4
Corresponds to variant rs10502001 [ dbSNP | Ensembl ].

VAR_006729

Natural variant

137

1

G → D. Ref.4
Corresponds to variant rs17884789 [ dbSNP | Ensembl ].

VAR_021027

Natural variant

241

1

P → L. Ref.4
Corresponds to variant rs17886506 [ dbSNP | Ensembl ].

VAR_021028

Secondary structure

1

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267

Helix Strand Turn

Details...

Beta strand

106 – 113

8

Beta strand

118 – 120

3

Helix

122 – 137

16

Beta strand

143 – 146

4

Beta strand

148 – 150

3

Beta strand

153 – 159

7

Beta strand

164 – 166

3

Beta strand

171 – 174

4

Beta strand

177 – 179

3

Beta strand

182 – 184

3

Turn

185 – 188

4

Beta strand

190 – 193

4

Beta strand

198 – 207

10

Helix

208 – 219

12

Beta strand

233 – 236

4

Beta strand

241 – 243

3

Helix

248 – 257

10

Sequences

	Sequence		Length	Mass (Da)
	P09237 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: F6BD1FC0ADA23603	FASTA	267	29,677
	10 20 30 40 50 60 MRLTVLCAVC LLPGSLALPL PQEAGGMSEL QWEQAQDYLK RFYLYDSETK NANSLEAKLK 70 80 90 100 110 120 EMQKFFGLPI TGMLNSRVIE IMQKPRCGVP DVAEYSLFPN SPKWTSKVVT YRIVSYTRDL 130 140 150 160 170 180 PHITVDRLVS KALNMWGKEI PLHFRKVVWG TADIMIGFAR GAHGDSYPFD GPGNTLAHAF 190 200 210 220 230 240 APGTGLGGDA HFDEDERWTD GSSLGINFLY AATHELGHSL GMGHSSDPNA VMYPTYGNGD 250 260 PQNFKLSQDD IKGIQKLYGK RSNSRKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The collagenase gene family in humans consists of at least four members." Muller D., Quantin B., Gesnel M.-C., Millon-Collard R., Abecassis J., Breathnach R. Biochem. J. 253:187-192(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Molecular characterization of a low-molecular-mass matrix metalloproteinase secreted by glomerular mesangial cells as PUMP-1." Marti H.P., McNeil L., Thomas G., Davies M., Lovett D.H. Biochem. J. 285:899-905(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[3]	"Structure and expression of the human gene for the matrix metalloproteinase matrilysin." Gaire M., Magbanua Z., McDonnell S., McNeil L.B., Lovett D.H., Matrisian L.M. J. Biol. Chem. 269:2032-2040(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Placenta.
[4]	NIEHS SNPs program Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-77; ASP-137 AND LEU-241.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon.
[6]	"Purification and characterization of extracellular matrix-degrading metalloproteinase, matrin (pump-1), secreted from human rectal carcinoma cell line." Miyazaki K., Hattori Y., Umenishi F., Yasumitsu H., Umeda M. Cancer Res. 50:7758-7764(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-42.
[7]	"Pump-1 cDNA codes for a protein with characteristics similar to those of classical collagenase family members." Quantin B., Murphy G., Breathnach R. Biochemistry 28:5327-5334(1989) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Matrilysin-inhibitor complexes: common themes among metalloproteases." Browner M.F., Smith W.W., Castelhano A.L. Biochemistry 34:6602-6610(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X07819 mRNA. Translation: CAA30678.1.
Z11887 mRNA. Translation: CAA77942.1.
L22524 , L22519, L22520, L22521, L22522, L22523 Genomic DNA. Translation: AAC37543.1.
AY795972 Genomic DNA. Translation: AAV40839.1.
BC003635 mRNA. Translation: AAH03635.1.

IPI

IPI00013400.

PIR

KCHUM. B28816.

RefSeq

NP_002414.1. NM_002423.3.

UniGene

Hs.2256.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MMP	X-ray	2.30	A/B	95-264	[»]
1MMQ	X-ray	1.90	A	95-264	[»]
1MMR	X-ray	2.40	A	95-264	[»]
2DDY	NMR	-	A	95-267	[»]
2Y6C	X-ray	1.70	A	95-258	[»]
2Y6D	X-ray	1.60	A	95-267	[»]

ProteinModelPortal

P09237.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-7709639.

STRING

9606.ENSP00000260227.

Protein family/group databases

MEROPS

M10.008.

PTM databases

PhosphoSite

P09237.

Polymorphism databases

DMDM

116861.

Proteomic databases

PaxDb

P09237.

PRIDE

P09237.

Protocols and materials databases

DNASU

4316.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000260227; ENSP00000260227; ENSG00000137673.

GeneID

4316.

KEGG

hsa:4316.

UCSC

uc001phb.3. human.

Organism-specific databases

CTD

4316.

GeneCards

GC11M102425.

HGNC

HGNC:7174. MMP7.

HPA

CAB025869.

MIM

178990. gene.

neXtProt

NX_P09237.

PharmGKB

PA30887.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG312228.

HOGENOM

HOG000239471.

HOVERGEN

HBG052484.

InParanoid

P09237.

KO

K01397.

OMA

YGNGDPQ.

OrthoDB

EOG4H464B.

PhylomeDB

P09237.

Enzyme and pathway databases

BRENDA

3.4.24.23. 2681.

Pathway_Interaction_DB

p75ntrpathway. p75(NTR)-mediated signaling.

Reactome

REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpress

P09237.

Bgee

P09237.

CleanEx

HS_MMP7.

Genevestigator

P09237.

GermOnline

ENSG00000137673. Homo sapiens.

Family and domain databases

Gene3D

3.40.390.10. 1 hit.

InterPro

IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]

Pfam

PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]

PRINTS

PR00138. MATRIXIN.

SMART

SM00235. ZnMc. 1 hit.
[Graphical view]

SUPFAM

SSF47090. PGBD_like. 1 hit.

PROSITE

PS00546. CYSTEINE_SWITCH. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P09237.

ChEMBL

CHEMBL4073.

EvolutionaryTrace

P09237.

GenomeRNAi

4316.

NextBio

16981.

PMAP-CutDB

P09237.

SOURCE

Search...

Entry information

Entry name

MMP7_HUMAN

Accession

Primary (citable) accession number: P09237
Secondary accession number(s): Q9BTK9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	May 29, 2013
This is version 146 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.