Q9UNI1 · CELA1_HUMAN
- ProteinChymotrypsin-like elastase family member 1
- GeneCELA1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids258 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Serine proteases that hydrolyze many proteins in addition to elastin.
Catalytic activity
Cofactor
Note: Binds 1 Ca2+ ion per subunit.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 63 | Charge relay system | ||||
Sequence: H | ||||||
Binding site | 77 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 79 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 82 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 87 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 111 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 206 | Charge relay system | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular space | |
Molecular Function | metal ion binding | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | elastin catabolic process | |
Biological Process | exocrine pancreas development | |
Biological Process | inflammatory response | |
Biological Process | multicellular organism growth | |
Biological Process | negative regulation of transcription by RNA polymerase II | |
Biological Process | pancreas morphogenesis | |
Biological Process | positive regulation of angiogenesis | |
Biological Process | positive regulation of transcription by RNA polymerase II | |
Biological Process | post-embryonic development | |
Biological Process | proteolysis | |
Biological Process | regulation of cell differentiation | |
Biological Process | regulation of cell population proliferation | |
Biological Process | tissue remodeling | |
Biological Process | transcription by RNA polymerase II | |
Biological Process | Wnt signaling pathway |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameChymotrypsin-like elastase family member 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9UNI1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_033645 | 10 | in dbSNP:rs17860287 | |||
Sequence: Q → H | ||||||
Natural variant | VAR_033646 | 44 | in dbSNP:rs17860299 | |||
Sequence: R → W | ||||||
Natural variant | VAR_033647 | 59 | in dbSNP:rs17860300 | |||
Sequence: M → V | ||||||
Natural variant | VAR_036295 | 76 | in a breast cancer sample; somatic mutation | |||
Sequence: G → A | ||||||
Natural variant | VAR_033648 | 243 | in dbSNP:rs17860364 | |||
Sequence: Q → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 306 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, propeptide, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-8 | |||||
Sequence: MLVLYGHS | ||||||
Propeptide | PRO_0000027677 | 9-18 | Activation peptide | |||
Sequence: TQDLPETNAR | ||||||
Chain | PRO_0000027678 | 19-258 | Chymotrypsin-like elastase family member 1 | |||
Sequence: VVGGTEAGRNSWPSQISLQYRSGGSRYHTCGGTLIRQNWVMTAAHCVDYQKTFRVVAGDHNLSQNDGTEQYVSVQKIVVHPYWNSDNVAAGYDIALLRLAQSVTLNSYVQLGVLPQEGAILANNSPCYITGWGKTKTNGQLAQTLQQAYLPSVDYAICSSSSYWGSTVKNTMVCAGGDGVRSGCQGDSGGPLHCLVNGKYSVHGVTSFVSSRGCNVSRKPTVFTQVSAYISWINNVIASN | ||||||
Disulfide bond | 48↔64 | |||||
Sequence: CGGTLIRQNWVMTAAHC | ||||||
Glycosylation | 79 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 145↔212 | |||||
Sequence: CYITGWGKTKTNGQLAQTLQQAYLPSVDYAICSSSSYWGSTVKNTMVCAGGDGVRSGCQGDSGGPLHC | ||||||
Disulfide bond | 176↔192 | |||||
Sequence: CSSSSYWGSTVKNTMVC | ||||||
Disulfide bond | 202↔232 | |||||
Sequence: CQGDSGGPLHCLVNGKYSVHGVTSFVSSRGC | ||||||
Glycosylation | 233 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 19-256 | Peptidase S1 | ||||
Sequence: VVGGTEAGRNSWPSQISLQYRSGGSRYHTCGGTLIRQNWVMTAAHCVDYQKTFRVVAGDHNLSQNDGTEQYVSVQKIVVHPYWNSDNVAAGYDIALLRLAQSVTLNSYVQLGVLPQEGAILANNSPCYITGWGKTKTNGQLAQTLQQAYLPSVDYAICSSSSYWGSTVKNTMVCAGGDGVRSGCQGDSGGPLHCLVNGKYSVHGVTSFVSSRGCNVSRKPTVFTQVSAYISWINNVIA |
Sequence similarities
Belongs to the peptidase S1 family. Elastase subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length258
- Mass (Da)27,798
- Last updated2005-03-29 v2
- Checksum684EDE8F1F011F8D
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 220 | in Ref. 1; AAD28441 | ||||
Sequence: V → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF120493 EMBL· GenBank· DDBJ | AAD28441.1 EMBL· GenBank· DDBJ | mRNA | ||
AC046135 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC069454 EMBL· GenBank· DDBJ | AAH69454.1 EMBL· GenBank· DDBJ | mRNA | ||
BC075091 EMBL· GenBank· DDBJ | AAH75091.2 EMBL· GenBank· DDBJ | mRNA | ||
AY740424 EMBL· GenBank· DDBJ | AAV88109.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. |