C4JTD3 · KEX1_UNCRE
- ProteinPheromone-processing carboxypeptidase KEX1
- GeneKEX1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids638 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from protein precursors. Promotes cell fusion and is involved in the programmed cell death (By similarity).
Catalytic activity
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 184 | |||||
Sequence: S | ||||||
Active site | 386 | |||||
Sequence: D | ||||||
Active site | 448 | |||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Cellular Component | trans-Golgi network | |
Molecular Function | serine-type carboxypeptidase activity | |
Biological Process | apoptotic process | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePheromone-processing carboxypeptidase KEX1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Onygenales > Onygenaceae > Uncinocarpus
Accessions
- Primary accessionC4JTD3
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus, trans-Golgi network membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 33-519 | Lumenal | ||||
Sequence: KCAADYYVRSLPGQPEGPLLKMHAGHIEVDHENNGNLFFWHFQNRHIANRQRTVIWLNGGPGCSSMDGAMMEVGPYRLKDDHTLKYNEGSWDEFANLLFVDQPVGTGYSYANTNSYLHELDEMAAHFVTFMERWFELFPEYEHDDLYFAGESYAGQYIPYIAKAILDRNKNETVIAQRRLWHLKGLLIGNGWFSPVEQYLSYLPYVYKEGMVKNDSDEAKGIERAHSDCVAELDRAKGDVKIHVDVCEKILSAILDVSNKSGHCVNMYDVRLTDTFPSCGMNWPPDLKHLAPYLRRDDVTSALHINKDKKTGWTECAGAVSSSFRPRKSKPSADLLPGLLESGVRIGLFSGAKDLICNHIGTEEFINKMEWSGGKGFELSPGVWAPRRDWTFEGETAGYYQEARNLTYVLFYNASHMVPFDYARRSRDMLDRFLGVDITSIGGNPTDSRIDGEKGALTSVGNHPNSTLAEQREKEKLKAATWKAYYK | ||||||
Transmembrane | 520-540 | Helical | ||||
Sequence: SGEVALVVVVIAAGAWGFFLW | ||||||
Topological domain | 541-638 | Cytoplasmic | ||||
Sequence: RSRRQRQGSGYLGIYPSLNGLSSGSLPRYRNKRSSRDIEAAAEFEASELETLHDMDDRSPGPSRDNYSVGEDSETEDEKRYPPTDFDRQDGTPSASRT |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-32 | |||||
Sequence: MSSCQPPPFLSSMVVRWLSVWIILASSAFASA | ||||||
Chain | PRO_0000411949 | 33-638 | Pheromone-processing carboxypeptidase KEX1 | |||
Sequence: KCAADYYVRSLPGQPEGPLLKMHAGHIEVDHENNGNLFFWHFQNRHIANRQRTVIWLNGGPGCSSMDGAMMEVGPYRLKDDHTLKYNEGSWDEFANLLFVDQPVGTGYSYANTNSYLHELDEMAAHFVTFMERWFELFPEYEHDDLYFAGESYAGQYIPYIAKAILDRNKNETVIAQRRLWHLKGLLIGNGWFSPVEQYLSYLPYVYKEGMVKNDSDEAKGIERAHSDCVAELDRAKGDVKIHVDVCEKILSAILDVSNKSGHCVNMYDVRLTDTFPSCGMNWPPDLKHLAPYLRRDDVTSALHINKDKKTGWTECAGAVSSSFRPRKSKPSADLLPGLLESGVRIGLFSGAKDLICNHIGTEEFINKMEWSGGKGFELSPGVWAPRRDWTFEGETAGYYQEARNLTYVLFYNASHMVPFDYARRSRDMLDRFLGVDITSIGGNPTDSRIDGEKGALTSVGNHPNSTLAEQREKEKLKAATWKAYYKSGEVALVVVVIAAGAWGFFLWRSRRQRQGSGYLGIYPSLNGLSSGSLPRYRNKRSSRDIEAAAEFEASELETLHDMDDRSPGPSRDNYSVGEDSETEDEKRYPPTDFDRQDGTPSASRT | ||||||
Glycosylation | 203 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 246 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 291 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 437 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 445 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 497 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 586-601 | Basic and acidic residues | ||||
Sequence: ASELETLHDMDDRSPG | ||||||
Region | 586-638 | Disordered | ||||
Sequence: ASELETLHDMDDRSPGPSRDNYSVGEDSETEDEKRYPPTDFDRQDGTPSASRT | ||||||
Compositional bias | 609-626 | Basic and acidic residues | ||||
Sequence: VGEDSETEDEKRYPPTDF |
Sequence similarities
Belongs to the peptidase S10 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length638
- Mass (Da)71,903
- Last updated2009-07-07 v1
- ChecksumE9974ECF7A5C0FF0
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 586-601 | Basic and acidic residues | ||||
Sequence: ASELETLHDMDDRSPG | ||||||
Compositional bias | 609-626 | Basic and acidic residues | ||||
Sequence: VGEDSETEDEKRYPPTDF |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CH476617 EMBL· GenBank· DDBJ | EEP80880.1 EMBL· GenBank· DDBJ | Genomic DNA |