Q91VE3 · KLK7_MOUSE
- ProteinKallikrein-7
- GeneKlk7
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids249 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May catalyze the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. Cleaves insulin A chain at '14-Tyr-|-Gln-15' and insulin B chain at '6-Leu-|-Cys-7', '16-Tyr-|-Leu-17', '25-Phe-|-Tyr-26' and '26-Tyr-|-Thr-27'. Could play a role in the activation of precursors to inflammatory cytokines.
Catalytic activity
Activity regulation
Inhibited by Zn2+ and Cu2+ at low micromolar concentrations. Inhibited by SERPINA12 (By similarity).
Features
Showing features for active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 66 | Charge relay system | ||||
Sequence: H | ||||||
Site | 105 | Major binding site for inhibitory zinc or copper | ||||
Sequence: H | ||||||
Active site | 108 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 201 | Charge relay system | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cornified envelope | |
Cellular Component | epidermal lamellar body | |
Cellular Component | extracellular space | |
Cellular Component | secretory granule | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | positive regulation of antibacterial peptide production | |
Biological Process | proteolysis |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameKallikrein-7
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ91VE3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 10 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for signal, propeptide, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MGVWLLSLITVLLSLALETAG | ||||||
Propeptide | PRO_0000027944 | 22-25 | Activation peptide | |||
Sequence: QGER | ||||||
Chain | PRO_0000027945 | 26-249 | Kallikrein-7 | |||
Sequence: IIDGYKCKEGSHPWQVALLKGNQLHCGGVLVDKYWVLTAAHCKMGQYQVQLGSDKIGDQSAQKIKATKSFRHPGYSTKTHVNDIMLVRLDEPVKMSSKVEAVQLPEHCEPPGTSCTVSGWGTTTSPDVTFPSDLMCSDVKLISSRECKKVYKDLLGKTMLCAGIPDSKTNTCNGDSGGPLVCNDTLQGLVSWGTYPCGQPNDPGVYTQVCKYKRWVMETMKTHR | ||||||
Disulfide bond | 32↔161 | |||||
Sequence: CKEGSHPWQVALLKGNQLHCGGVLVDKYWVLTAAHCKMGQYQVQLGSDKIGDQSAQKIKATKSFRHPGYSTKTHVNDIMLVRLDEPVKMSSKVEAVQLPEHCEPPGTSCTVSGWGTTTSPDVTFPSDLMC | ||||||
Disulfide bond | 51↔67 | |||||
Sequence: CGGVLVDKYWVLTAAHC | ||||||
Disulfide bond | 133↔235 | |||||
Sequence: CEPPGTSCTVSGWGTTTSPDVTFPSDLMCSDVKLISSRECKKVYKDLLGKTMLCAGIPDSKTNTCNGDSGGPLVCNDTLQGLVSWGTYPCGQPNDPGVYTQVC | ||||||
Disulfide bond | 140↔207 | |||||
Sequence: CTVSGWGTTTSPDVTFPSDLMCSDVKLISSRECKKVYKDLLGKTMLCAGIPDSKTNTCNGDSGGPLVC | ||||||
Disulfide bond | 172↔186 | |||||
Sequence: CKKVYKDLLGKTMLC | ||||||
Disulfide bond | 197↔222 | |||||
Sequence: CNGDSGGPLVCNDTLQGLVSWGTYPC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in skin and, at lower levels, in lung, kidney, brain, heart and spleen. In skin, expressed in high suprabasal keratinocytes and in the luminal parts of hair follicles. Not detected in liver and skeletal muscle.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 26-246 | Serine protease | ||||
Sequence: IIDGYKCKEGSHPWQVALLKGNQLHCGGVLVDKYWVLTAAHCKMGQYQVQLGSDKIGDQSAQKIKATKSFRHPGYSTKTHVNDIMLVRLDEPVKMSSKVEAVQLPEHCEPPGTSCTVSGWGTTTSPDVTFPSDLMCSDVKLISSRECKKVYKDLLGKTMLCAGIPDSKTNTCNGDSGGPLVCNDTLQGLVSWGTYPCGQPNDPGVYTQVCKYKRWVMETMK |
Sequence similarities
Belongs to the peptidase S1 family. Kallikrein subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length249
- Mass (Da)27,257
- Last updated2001-12-01 v1
- Checksum0D4E380F12D14F87
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 215-217 | in Ref. 5; AAF01139 | ||||
Sequence: VSW → ASR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB008371 EMBL· GenBank· DDBJ | BAB55604.1 EMBL· GenBank· DDBJ | mRNA | ||
AF339930 EMBL· GenBank· DDBJ | AAK69652.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK029477 EMBL· GenBank· DDBJ | BAC26467.1 EMBL· GenBank· DDBJ | mRNA | ||
AK077406 EMBL· GenBank· DDBJ | BAC36787.1 EMBL· GenBank· DDBJ | mRNA | ||
BC027823 EMBL· GenBank· DDBJ | AAH27823.1 EMBL· GenBank· DDBJ | mRNA | ||
AF124299 EMBL· GenBank· DDBJ | AAF01139.1 EMBL· GenBank· DDBJ | mRNA |