Q90YC2 · MMP21_CYNPY
- ProteinMatrix metalloproteinase-21
- GeneMMP21
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids616 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
May play a role in gastrulation-related cell movement (PubMed:11606053).
Plays a specialized role in the generation of left-right asymmetry during embryogenesis. May act as a negative regulator of the NOTCH-signaling pathway (By similarity).
Plays a specialized role in the generation of left-right asymmetry during embryogenesis. May act as a negative regulator of the NOTCH-signaling pathway (By similarity).
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 141 | Zn2+ (UniProtKB | ChEBI); catalytic; in inhibited form | ||||
Sequence: C | ||||||
Binding site | 329 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 330 | |||||
Sequence: E | ||||||
Binding site | 333 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 339 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular matrix | |
Cellular Component | extracellular space | |
Molecular Function | metalloendopeptidase activity | |
Molecular Function | zinc ion binding | |
Biological Process | collagen catabolic process | |
Biological Process | determination of heart left/right asymmetry | |
Biological Process | determination of left/right symmetry | |
Biological Process | extracellular matrix organization | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameMatrix metalloproteinase-21
- EC number
- Short namesMMP-21
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Caudata > Salamandroidea > Salamandridae > Pleurodelinae > Cynops
Accessions
- Primary accessionQ90YC2
Subcellular Location
PTM/Processing
Features
Showing features for signal, propeptide, glycosylation, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MPTAPALGALLLLLGALTPGHQ | ||||||
Propeptide | PRO_0000028842 | 23-192 | ||||
Sequence: EKLFHSRDHSDLQPSPQHQAELVTDLQSAQQFLSKYGWTEPVKWEGTSSKNAAELPRYGDADLMQEGASISRYGQEFPLEPTQAPAFVEALRKFQTLNGLPATGKLDDSTIAAMNKPRCGVPDNQIGKESAIVKSNSNNVTEKASGKSLNTTTNQNPENGTSTSKIRKKR | ||||||
Glycosylation | 161 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 172 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 181 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Chain | PRO_0000028843 | 193-616 | Matrix metalloproteinase-21 | |||
Sequence: FLQMLAAPVRYKDQANQGSTVRGAFSKKLLKWRLIGEGYSSQLSIDEQRYVFKTAFRMWSEVMPLDFEEDLTSPMSLIDVKLGFGRGRHLGCTRSFDGSGQEFAHAWFLGDIHFDDDEHFTAPSSDSGISLLKVAVHEIGHVLGLSHIYQTGSIMQPNYIPQEAGFELDWTDRKAIQMLYGTCEGSFDAVFDWIWKERNQYGELVLRYNTYFFRNAWYWLYENRKNRTRYGDPVTVSLGWHGIPAEGIDAFVHVWTWTEDATYFFKGTQYWRYDSENDQAYIKDAQGNQYPRLISEGFPKIPSPINTAFFDRRDQFIYFFKDAHVYAFDVKRNMVANHYPKRIIDVFPAVVRNNHPFGNIDAAYYAYTHNSIFLFKGKEYWKVVSDKDRQQNPKLPRNGLFLKKNISEQWTDICNVHSSMLKMR | ||||||
Disulfide bond | 375↔606 | |||||
Sequence: CEGSFDAVFDWIWKERNQYGELVLRYNTYFFRNAWYWLYENRKNRTRYGDPVTVSLGWHGIPAEGIDAFVHVWTWTEDATYFFKGTQYWRYDSENDQAYIKDAQGNQYPRLISEGFPKIPSPINTAFFDRRDQFIYFFKDAHVYAFDVKRNMVANHYPKRIIDVFPAVVRNNHPFGNIDAAYYAYTHNSIFLFKGKEYWKVVSDKDRQQNPKLPRNGLFLKKNISEQWTDIC | ||||||
Glycosylation | 418 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 597 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
The precursor is cleaved by a furin endopeptidase.
Keywords
- PTM
PTM databases
Expression
Developmental stage
Detected during early embryogenesis, then, gradually decreased, but increased again starting in late gastrula. There are regional diiferences in the level of expression at late gastrula: the involved archenteron roof is the predominant site, while there is weak expression in the neuroectoderm and epidermal ectoderm.
Structure
Family & Domains
Features
Showing features for motif, region, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 139-146 | Cysteine switch | ||||
Sequence: PRCGVPDN | ||||||
Region | 157-186 | Disordered | ||||
Sequence: SNSNNVTEKASGKSLNTTTNQNPENGTSTS | ||||||
Repeat | 376-435 | Hemopexin 1 | ||||
Sequence: EGSFDAVFDWIWKERNQYGELVLRYNTYFFRNAWYWLYENRKNRTRYGDPVTVSLGWHGI | ||||||
Repeat | 437-493 | Hemopexin 2 | ||||
Sequence: AEGIDAFVHVWTWTEDATYFFKGTQYWRYDSENDQAYIKDAQGNQYPRLISEGFPKI | ||||||
Repeat | 494-542 | Hemopexin 3 | ||||
Sequence: PSPINTAFFDRRDQFIYFFKDAHVYAFDVKRNMVANHYPKRIIDVFPAV | ||||||
Repeat | 549-605 | Hemopexin 4 | ||||
Sequence: FGNIDAAYYAYTHNSIFLFKGKEYWKVVSDKDRQQNPKLPRNGLFLKKNISEQWTDI |
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
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length616
- Mass (Da)70,428
- Last updated2001-12-01 v1
- ChecksumABFC72D8B13E5003