Reviewed, UniProtKB/Swiss-Prot Q10738 (MMP7_MOUSE)

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
      Short name=Matrin

Gene names

Name:

Mmp7

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	264 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase By similarity. May play a role in tissue reorganization.
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 By similarity. Binds 2 zinc ions per subunit By similarity.
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
Domain	Signal
Ligand	Calcium Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Zymogen
Gene Ontology (GO)
Biological process	collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro regulation of cell proliferation Inferred from genetic interaction. Source: MGI
Cellular component	extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro 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	Potential
	Propeptide	18 – 94	77	Activation peptide By similarity		PRO_0000028740
	Chain	95 – 264	170	Matrilysin		PRO_0000028741
Regions
	Motif	85 – 92	8	Cysteine switch By similarity
Sites
	Active site	215	1	By similarity
	Metal binding	87	1	Zinc 2; in inhibited form By similarity
	Metal binding	153	1	Calcium 1 By similarity
	Metal binding	163	1	Zinc 1 By similarity
	Metal binding	165	1	Zinc 1 By similarity
	Metal binding	170	1	Calcium 2 By similarity
	Metal binding	171	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	173	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	175	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	178	1	Zinc 1 By similarity
	Metal binding	185	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	187	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	189	1	Calcium 1 By similarity
	Metal binding	191	1	Zinc 1 By similarity
	Metal binding	193	1	Calcium 2 By similarity
	Metal binding	196	1	Calcium 2 By similarity
	Metal binding	214	1	Zinc 2; catalytic By similarity
	Metal binding	218	1	Zinc 2; catalytic By similarity
	Metal binding	224	1	Zinc 2; catalytic By similarity
Experimental info
	Sequence conflict	201	1	G → D in AAA99983. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q10738-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: EDA31A5EBAC63342	FASTA	264	29,755
	10 20 30 40 50 60 MQLTLFCFVC LLPGHLALPL SQEAGDVSAH QWEQAQNYLR KFYPHDSKTK KVNSLVDNLK 70 80 90 100 110 120 EMQKFFGLPM TGKLSPYIME IMQKPRCGVP DVAEYSLMPN SPKWHSRIVT YRIVSYTSDL 130 140 150 160 170 180 PRIVVDQIVK KALRMWSMQI PLNFKRVSWG TADIIIGFAR RDHGDSFPFD GPGNTLGHAF 190 200 210 220 230 240 APGPGLGGDA HFDKDEYWTD GEDAGVNFLF AATHEFGHSL GLSHSSVPGT VMYPTYQRDY 250 260 SEDFSLTKDD IAGIQKLYGK RNTL

References

[1]	"The metalloproteinase matrilysin is preferentially expressed by epithelial cells in a tissue-restricted pattern in the mouse." Wilson C.L., Heppner K.J., Rudolph L.A., Matrisian L.M. Mol. Biol. Cell 6:851-869(1995) [PubMed: 7579699] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: ICR. Tissue: Uterus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L36238 , L36243, L36242, L36241, L36240, L36239 Genomic DNA. Translation: AAA99984.1. L36244 mRNA. Translation: AAA99983.1.
IPI	IPI00275232.
UniGene	Mm.4825
3D structure databases
HSSP	HSSP built from PDB template 1MMR based on UniProtKB P09237.
SMR	Q10738. Positions 95-261.
ModBase	Search...
Protein family/group databases
MEROPS	M10.008.
Genome annotation databases
Ensembl	ENSMUSG00000018623. Mus musculus. [Contig view]
Organism-specific databases
MGI	MGI:103189. Mmp7.
Phylogenomic databases
HOVERGEN	Q10738.
Enzyme and pathway databases
BRENDA	3.4.24.23. 244.
Gene expression databases
ArrayExpress	Q10738.
Bgee	Q10738.
CleanEx	MM_MMP7.
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
SOURCE	Search...

Entry information

Entry name

MMP7_MOUSE

Accession

Primary (citable) accession number: Q10738

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)