Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q499S5 (MMP11_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Stromelysin-3

Short name=SL-3
Short name=ST3
EC=3.4.24.-
Alternative name(s):
Matrix metalloproteinase-11
Short name=MMP-11
Gene names
Name:Mmp11
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length491 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play an important role in the progression of epithelial malignancies By similarity.

Cofactor

Binds 1 calcium ion per subunit.

Binds 2 zinc ions per subunit.

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Tissue specificity

Highly expressed in ovary and uterus. Ref.1

Induction

In skin fibroblasts of superficial dermis upon skin lesion with highest level between days 5-10. Ref.1

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.

Post-translational modification

The precursor is cleaved by a furin endopeptidase. Ref.1

Sequence similarities

Belongs to the peptidase M10A family.

Contains 4 hemopexin repeats.

Sequence caution

The sequence AAC53061.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH99781.2 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Potential
Propeptide36 – 10166Activation peptide By similarity
PRO_0000042649
Chain102 – 491390Stromelysin-3
PRO_0000042650

Regions

Repeat298 – 34245Hemopexin 1
Repeat343 – 38543Hemopexin 2
Repeat387 – 43549Hemopexin 3
Repeat436 – 48348Hemopexin 4
Motif82 – 898Cysteine switch By similarity

Sites

Active site2191 By similarity
Metal binding841Zinc 2; in inhibited form By similarity
Metal binding1681Zinc 1 By similarity
Metal binding1701Zinc 1 By similarity
Metal binding1751Calcium By similarity
Metal binding1761Calcium; via carbonyl oxygen By similarity
Metal binding1781Calcium; via carbonyl oxygen By similarity
Metal binding1801Calcium; via carbonyl oxygen By similarity
Metal binding1831Zinc 1 By similarity
Metal binding1961Zinc 1 By similarity
Metal binding2181Zinc 2; catalytic By similarity
Metal binding2221Zinc 2; catalytic By similarity
Metal binding2281Zinc 2; catalytic By similarity

Amino acid modifications

Disulfide bond297 ↔ 483 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q499S5 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: B0C5B191A623FD41

FASTA49155,511
        10         20         30         40         50         60 
MARAACLLRA ISRALLLPLP LLLLLLLLLP PQLMARARPP ENHRHRPVKR VPQLLPAALP 

        70         80         90        100        110        120 
NSLPSVPASH WVPGPASSSR PLRCGVPDPP DVLNARNRQK RFVLSGGRWE KTDLTYRILR 

       130        140        150        160        170        180 
FPWQLVREQV RQTVAEALRV WSEVTPLTFT EVHEGRADIM IDFTRYWHGD NLPFDGPGGI 

       190        200        210        220        230        240 
LAHAFFPKTH REGDVHFDYD ETWTIGDKGT DLLQVAAHEF GHVLGLQHTT AAKALMSPFY 

       250        260        270        280        290        300 
TFRYPLSLSP DDRRGIQHLY GRPQLTPTSP TPTLSSQAGT DTNEIALQEP EVPPEVCETS 

       310        320        330        340        350        360 
FDAVSTIRGE LFFFKAGFVW RLRSGQLQPG YPALASRHWQ GLPSPVDAAF EDAQGQIWFF 

       370        380        390        400        410        420 
QGAQYWVYDG EKPVLGPAPL SKLGLQGSPV HAALVWGPEK NKIYFFRGGD YWRFHPRTQR 

       430        440        450        460        470        480 
VDNPVPRRTT DWRGVPSEID AAFQDAEGYA YFLRGHLYWK FDPVKVKVLE SFPRPIGPDF 

       490 
FDCAEPANTF R 

« Hide

References

« Hide 'large scale' references
[1]"Rat stromelysin 3: cDNA cloning from healing skin wound, activation by furin and expression in rat tissues."
Okada A., Saez S., Misumi Y., Basset P.
Gene 185:187-193(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION, PROTEOLYTIC PROCESSING.
Strain: Wistar.
[2]"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: Prostate.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U46034 mRNA. Translation: AAC53061.1. Different initiation.
BC099781 mRNA. Translation: AAH99781.2. Different initiation.
RefSeqNP_037112.2. NM_012980.2.
UniGeneRn.11123.

3D structure databases

ProteinModelPortalQ499S5.
SMRQ499S5. Positions 102-264.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247514. 2 interactions.

Protein family/group databases

MEROPSM10.007.

PTM databases

PhosphoSiteQ499S5.

Proteomic databases

PaxDbQ499S5.
PRIDEQ499S5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000031400; ENSRNOP00000035334; ENSRNOG00000028344.
GeneID25481.
KEGGrno:25481.
UCSCRGD:3099. rat.

Organism-specific databases

CTD4320.
RGD3099. Mmp11.

Phylogenomic databases

eggNOGNOG236137.
GeneTreeENSGT00750000117332.
HOGENOMHOG000217927.
HOVERGENHBG052484.
InParanoidQ499S5.
KOK07993.
OMAVDTNEIA.
OrthoDBEOG7XPZ57.
PhylomeDBQ499S5.

Gene expression databases

GenevestigatorQ499S5.

Family and domain databases

Gene3D2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR006026. Peptidase_Metallo.
IPR028705. Stromelysin-3.
[Graphical view]
PANTHERPTHR10201. PTHR10201. 1 hit.
PTHR10201:SF20. PTHR10201:SF20. 1 hit.
PfamPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
[Graphical view]
PIRSFPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSPR00138. MATRIXIN.
SMARTSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF50923. SSF50923. 1 hit.
PROSITEPS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio606819.
PROQ499S5.

Entry information

Entry nameMMP11_RAT
AccessionPrimary (citable) accession number: Q499S5
Secondary accession number(s): P97568
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: September 13, 2005
Last modified: April 16, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries