Q499S5 · MMP11_RAT
- ProteinStromelysin-3
- GeneMmp11
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids491 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May play an important role in the progression of epithelial malignancies.
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Ca2+ ion per subunit.
Note: Binds 2 Zn2+ ions per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 84 | Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form | ||||
Sequence: C | ||||||
Binding site | 168 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 170 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 175 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 176 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 178 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 180 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 183 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 196 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 218 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 219 | |||||
Sequence: E | ||||||
Binding site | 222 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 228 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular matrix | |
Cellular Component | extracellular space | |
Molecular Function | metalloendopeptidase activity | |
Molecular Function | metallopeptidase activity | |
Molecular Function | zinc ion binding | |
Biological Process | basement membrane organization | |
Biological Process | collagen catabolic process | |
Biological Process | collagen fibril organization | |
Biological Process | extracellular matrix organization | |
Biological Process | negative regulation of fat cell differentiation | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameStromelysin-3
- EC number
- Short namesSL-3; ST3
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ499S5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, propeptide, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-35 | |||||
Sequence: MARAACLLRAISRALLLPLPLLLLLLLLLPPQLMA | ||||||
Propeptide | PRO_0000042649 | 36-101 | Activation peptide | |||
Sequence: RARPPENHRHRPVKRVPQLLPAALPNSLPSVPASHWVPGPASSSRPLRCGVPDPPDVLNARNRQKR | ||||||
Chain | PRO_0000042650 | 102-491 | Stromelysin-3 | |||
Sequence: FVLSGGRWEKTDLTYRILRFPWQLVREQVRQTVAEALRVWSEVTPLTFTEVHEGRADIMIDFTRYWHGDNLPFDGPGGILAHAFFPKTHREGDVHFDYDETWTIGDKGTDLLQVAAHEFGHVLGLQHTTAAKALMSPFYTFRYPLSLSPDDRRGIQHLYGRPQLTPTSPTPTLSSQAGTDTNEIALQEPEVPPEVCETSFDAVSTIRGELFFFKAGFVWRLRSGQLQPGYPALASRHWQGLPSPVDAAFEDAQGQIWFFQGAQYWVYDGEKPVLGPAPLSKLGLQGSPVHAALVWGPEKNKIYFFRGGDYWRFHPRTQRVDNPVPRRTTDWRGVPSEIDAAFQDAEGYAYFLRGHLYWKFDPVKVKVLESFPRPIGPDFFDCAEPANTFR | ||||||
Disulfide bond | 297↔483 | |||||
Sequence: CETSFDAVSTIRGELFFFKAGFVWRLRSGQLQPGYPALASRHWQGLPSPVDAAFEDAQGQIWFFQGAQYWVYDGEKPVLGPAPLSKLGLQGSPVHAALVWGPEKNKIYFFRGGDYWRFHPRTQRVDNPVPRRTTDWRGVPSEIDAAFQDAEGYAYFLRGHLYWKFDPVKVKVLESFPRPIGPDFFDC |
Post-translational modification
The precursor is cleaved by a furin endopeptidase.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in ovary and uterus.
Induction
In skin fibroblasts of superficial dermis upon skin lesion with highest level between days 5-10.
Gene expression databases
Structure
Family & Domains
Features
Showing features for motif, region, compositional bias, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 82-89 | Cysteine switch | ||||
Sequence: LRCGVPDP | ||||||
Region | 260-279 | Disordered | ||||
Sequence: YGRPQLTPTSPTPTLSSQAG | ||||||
Compositional bias | 262-279 | Polar residues | ||||
Sequence: RPQLTPTSPTPTLSSQAG | ||||||
Repeat | 298-342 | Hemopexin 1 | ||||
Sequence: ETSFDAVSTIRGELFFFKAGFVWRLRSGQLQPGYPALASRHWQGL | ||||||
Repeat | 343-385 | Hemopexin 2 | ||||
Sequence: PSPVDAAFEDAQGQIWFFQGAQYWVYDGEKPVLGPAPLSKLGL | ||||||
Repeat | 387-435 | Hemopexin 3 | ||||
Sequence: GSPVHAALVWGPEKNKIYFFRGGDYWRFHPRTQRVDNPVPRRTTDWRGV | ||||||
Repeat | 436-483 | Hemopexin 4 | ||||
Sequence: PSEIDAAFQDAEGYAYFLRGHLYWKFDPVKVKVLESFPRPIGPDFFDC |
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.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length491
- Mass (Da)55,511
- Last updated2005-09-13 v1
- ChecksumB0C5B191A623FD41
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8L2R8J4 | A0A8L2R8J4_RAT | Mmp11 | 488 |
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 262-279 | Polar residues | ||||
Sequence: RPQLTPTSPTPTLSSQAG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U46034 EMBL· GenBank· DDBJ | AAC53061.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC099781 EMBL· GenBank· DDBJ | AAH99781.2 EMBL· GenBank· DDBJ | mRNA | Different initiation |