Reviewed, UniProtKB/Swiss-Prot P55032 (MMP7_FELCA)

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

Organism

Felis catus (Cat) (Felis silvestris catus)

Taxonomic identifier

9685 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Feliformia › Felidae › Felinae › Felis

Protein attributes

Sequence length	262 AA.
Sequence status	Fragment.
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.
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
Cellular component	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 – 12	›12	By similarity
	Propeptide	13 – 89	77	Activation peptide By similarity		PRO_0000028736
	Chain	90 – 262	173	Matrilysin		PRO_0000028737
Regions
	Motif	80 – 87	8	Cysteine switch By similarity
Sites
	Active site	210	1	By similarity
	Metal binding	82	1	Zinc 2; in inhibited form By similarity
	Metal binding	148	1	Calcium 1 By similarity
	Metal binding	158	1	Zinc 1 By similarity
	Metal binding	160	1	Zinc 1 By similarity
	Metal binding	165	1	Calcium 2 By similarity
	Metal binding	166	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	168	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	170	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	173	1	Zinc 1 By similarity
	Metal binding	180	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	182	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	184	1	Calcium 1 By similarity
	Metal binding	186	1	Zinc 1 By similarity
	Metal binding	188	1	Calcium 2 By similarity
	Metal binding	191	1	Calcium 2 By similarity
	Metal binding	209	1	Zinc 2; catalytic By similarity
	Metal binding	213	1	Zinc 2; catalytic By similarity
	Metal binding	219	1	Zinc 2; catalytic By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P55032-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: E4A1FA23320DC732	FASTA	262	29,263
	10 20 30 40 50 60 LCVLCLLPQS PALPLPREAG GHSESQWKQA QEYLKRFYPS DAKSRDADSF GAQLKEMQKF 70 80 90 100 110 120 FRLPVTGMLD SRVIVVMQQP RCGLPDTGED LPSRNRPKWI SKVVTYRIIS YTRDLPRVTV 130 140 150 160 170 180 DHLVAKALNM WSKEIPLSFR RVVLGIPDIV IGFARGAHGD FYPFDGPGGT LAHAYEPGPG 190 200 210 220 230 240 LGGDAHFDED ERWADGRGLG INFLAVATHE LGHSLGLRHS SDPDSVMYPT YGARDSENFK 250 260 LSPGDIREIQ ELYGKRSKSR KK

References

[1]	"Expression and estrogen control of PUMP-1 mRNA in the cat uterus." Scalzo C.M., Verhage H.G., Jaffe R.C. Endocrinol. Jpn. 2:229-235(1994) Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Endometrium.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U04444 mRNA. Translation: AAA18222.1.
3D structure databases
HSSP	HSSP built from PDB template 1MMR based on UniProtKB P09237.
SMR	P55032. Positions 95-255.
ModBase	Search...
Protein-protein interaction databases
STRING	P55032.
Protein family/group databases
MEROPS	M10.008.
Genome annotation databases
Ensembl	ENSFCAT00000015791; ENSFCAP00000014641; ENSFCAG00000015787; Felis catus. [Genome view]
Phylogenomic databases
HOVERGEN	P55032.
Enzyme and pathway databases
BRENDA	3.4.24.23. 273949.
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. False negative. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MMP7_FELCA

Accession

Primary (citable) accession number: P55032

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	October 13, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)