Reviewed, UniProtKB/Swiss-Prot P09237 (MMP7_HUMAN)

Names and origin

Protein names

Recommended name:
    Matrilysin
    EC=3.4.24.23
Alternative name(s):
    Pump-1 protease
    Uterine metalloproteinase
    Matrix metalloproteinase-7
      Short name=MMP-7
    Matrin

Gene names

Name:	MMP7
Synonyms:	MPSL1, PUMP1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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
Gene Ontology (GO)
Biological process	collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Ref.2 Traceable author statement. Source: ProtInc
Cellular component	extracellular space Ref.2 Traceable author statement. Source: ProtInc proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Ref.2 Traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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: dbSNP rs10502001. Ref.4

VAR_006729

Natural variant

137

1

G → D: dbSNP rs17884789. Ref.4

VAR_021027

Natural variant

241

1

P → L: dbSNP rs17886506. Ref.4

VAR_021028

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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 – 220

13

Beta strand

233 – 236

4

Helix

248 – 258

11

Sequences

	Sequence		Length	Mass (Da)
	P09237-1 [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: 2844164] [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: 1497627] [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: 8294454] [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: 15489334] [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: 2253219] [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: 2550050] [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: 7756291] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

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

IPI

IPI00013400.

PIR

KCHUM. B28816.

RefSeq

NP_002414.1.

UniGene

Hs.2256

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P09237.

Protein family/group databases

MEROPS

M10.008.

Proteomic databases

PRIDE

P09237.

Genome annotation databases

Ensembl

ENST00000260227; ENSP00000260227; ENSG00000137673; Homo sapiens. [Genome view]

GeneID

4316.

KEGG

hsa:4316.

UCSC

uc001phb.1. human.

Organism-specific databases

CTD

4316.

GeneCards

GC11M101896.

H-InvDB

HIX0010065.

HGNC

HGNC:7174. MMP7.

MIM

178990. gene.

PharmGKB

PA30887.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P09237.

HOVERGEN

P09237.

OMA

DERWTDG.

Enzyme and pathway databases

BRENDA

3.4.24.23. 247.

Pathway_Interaction_DB

p75ntrpathway. p75(NTR)-mediated signaling.

Gene expression databases

ArrayExpress

P09237.

Bgee

P09237.

CleanEx

HS_MMP7.

Genevestigator

P09237.

GermOnline

ENSG00000137673. Homo sapiens.

Family and domain databases

InterPro

IPR001818. Pept_M10A_M12B.
IPR006025. Pept_M_Zn_BS.
IPR006026. Peptidase_M.
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]

PROSITE

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

ProtoNet

Search...

Other Resources

BindingDB

P09237.

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:	November 3, 2009
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.