[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1093/nar/15.3.1139; PubMed=3547333 [NCBI, ExPASy, EBI, Israel, Japan] Breathnach R., Matrisian L.M., Gesnel M.-C., Staub A., Leroy P.; "Sequences coding for part of oncogene-induced transin are highly conserved in a related rat gene."; Nucleic Acids Res. 15:1139-1151(1987).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=1370458 [NCBI, ExPASy, EBI, Israel, Japan] Chan J.C., Scanlon M., Zhang H.Z., Jia L.B., Yu D., Hung M.C., French M., Eastman E.M.; "Molecular cloning and characterization of v-mos-activated transformation-associated proteins."; J. Biol. Chem. 267:1099-1103(1992).

Comments

FUNCTION: Can degrade fibronectin, gelatins of type I, III, IV, and V; weakly collagens III, IV, and V. Activates procollagenase.
CATALYTIC ACTIVITY: Similar to stromelysin 1, but action on collagen types III, IV and V is weak.
COFACTOR: Binds 2 zinc ions per subunit (By similarity).
COFACTOR: Calcium (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.
SIMILARITY: Belongs to the peptidase M10A family [view classification].
SIMILARITY: Contains 4 hemopexin-like domains.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X05083; CAA28739.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M65253; AAA42202.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

B26403; KCRTS2.

NP_598198.1; -.

3D structure databases

HSSP

P08254; 1HY7. [HSSP ENTRY / PDB]

ModBase

P07152.

Protein family/group databases

MEROPS

M10.011; -.

Organism-specific databases

RGD

620192; Mmp10.

Gene expression databases

ArrayExpress

P07152; -.

GermOnline

ENSRNOG00000032832; Rattus norvegicus.

Ontologies

GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030574;	Biological process: collagen catabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000585; Hemopexin.
IPR001818; Pept_M10A_M12B.
IPR016293; Pept_M10A_matrix.
IPR006025; Pept_M_Zn_BS.
IPR006026; Peptidase_M.
IPR002477; Peptidoglycan-bd-like.
Graphical view of domain structure.

Gene3D

G3DSA:2.110.10.10; Hemopexin; 1.

Pfam

PF00045; Hemopexin; 4.
PF00413; Peptidase_M10; 1.
PF01471; PG_binding_1; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001191; Peptidase_M10A_matrix; 1.

PRINTS

PR00138; MATRIXIN.

SMART

SM00120; HX; 4.
SM00235; ZnMc; 1.
SMART graphical view of domain structure.

PROSITE

PS00546; CYSTEINE_SWITCH; 1.
PS00024; HEMOPEXIN; 1.
PS00142; ZINC_PROTEASE; 1.

Genome annotation databases

Ensembl

ENSRNOG00000032832; Rattus norvegicus. [Contig view]

GeneID

117061; -.

KEGG

rno:117061; -.

Phylogenomic databases

HOVERGEN

P07152; -.

Other

NextBio

619922; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Calcium; Collagen degradation; Extracellular matrix; Hydrolase; Metal-binding; Metalloprotease; Protease; Repeat; Secreted; Signal; Zinc; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 17`	`17`	`Probable.`
`PROPEP`	`18 99`	`82`	`Activation peptide (By similarity).`	`PRO_0000028768`
`CHAIN`	`100 476`	`377`	`Stromelysin-2.`	`PRO_0000028769`
`DOMAIN`	`295 337`	`43`	`Hemopexin-like 1.`
`DOMAIN`	`339 382`	`44`	`Hemopexin-like 2.`
`DOMAIN`	`387 434`	`48`	`Hemopexin-like 3.`
`DOMAIN`	`436 476`	`41`	`Hemopexin-like 4.`
`MOTIF`	`90 97`	`8`	`Cysteine switch (By similarity).`
`ACT_SITE`	`219 219`		`By similarity.`
`METAL`	`92 92`		`Zinc; in inhibited form (By similarity).`
`METAL`	`218 218`		`Zinc; catalytic (By similarity).`
`METAL`	`222 222`		`Zinc; catalytic (By similarity).`
`METAL`	`228 228`		`Zinc; catalytic (By similarity).`
`DISULFID`	`289 476`		`By similarity.`

Sequence information

Length: 476 AA [This is the length of the unprocessed precursor]

Molecular weight: 54222 Da [This is the MW of the unprocessed precursor]

CRC64: B556B6FB1D8BA7EE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEPLAILVLL CFPICSAYPL HGAVRQDHST MDLAQQYLEK YYNFRKNEKQ FFKRKDSSPV 

        70         80         90        100        110        120 
VKKIEEMQKF LGLEMTGKLD SNTVEMMHKP RCGVPDVGGF STFPGSPKWR KNHISYRIVN 

       130        140        150        160        170        180 
YTLDLPRESV DSAIERALKV WEEVTPLTFS RISEGEADIM ISFAVGEHGD FYPFDGVGQS 

       190        200        210        220        230        240 
LAHAYPPGPG FYGDAHFDDD EKWSLGPSGT NLFLVAAHEL GHSLGLFHSN NKESLMYPVY 

       250        260        270        280        290        300 
RFSTSQANIR LSQDDIEGIQ SLYGARPSSD ATVVPVPSVS PKPETPVKCD PALSFDAVTM 

       310        320        330        340        350        360 
LRGEFLFFKD RHFWRRTQWN PEPEFHLISA FWPSLPSGLD AAYEANNKDR VLIFKGSQFW 

       370        380        390        400        410        420 
AVRGNEVQAG YPKRIHTLGF PPTVKKIDAA VFEKEKKKTY FFVGDKYWRF DETRQLMDKG 

       430        440        450        460        470 
FPRLITDDFP GIEPQVDAVL HAFGFFYFFC GSSQFEFDPN ARTVTHTLKS NSWLLC

P07152 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools