C4JTD3 · KEX1_UNCRE

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

  • Preferential release of a C-terminal arginine or lysine residue.
    EC:3.4.16.6 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site.

163850100150200250300350400450500550600
TypeIDPosition(s)Description
Active site184
Active site386
Active site448

GO annotations

AspectTerm
Cellular Componentmembrane
Cellular Componenttrans-Golgi network
Molecular Functionserine-type carboxypeptidase activity
Biological Processapoptotic process
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Pheromone-processing carboxypeptidase KEX1
  • EC number
  • Alternative names
    • Carboxypeptidase D

Gene names

    • Name
      KEX1
    • ORF names
      UREG_05722

Organism names

Accessions

  • Primary accession
    C4JTD3

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain33-519Lumenal
Transmembrane520-540Helical
Topological domain541-638Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-32
ChainPRO_000041194933-638Pheromone-processing carboxypeptidase KEX1
Glycosylation203N-linked (GlcNAc...) asparagine
Glycosylation246N-linked (GlcNAc...) asparagine
Glycosylation291N-linked (GlcNAc...) asparagine
Glycosylation437N-linked (GlcNAc...) asparagine
Glycosylation445N-linked (GlcNAc...) asparagine
Glycosylation497N-linked (GlcNAc...) asparagine

Keywords

PTM databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for compositional bias, region.

TypeIDPosition(s)Description
Compositional bias586-601Basic and acidic residues
Region586-638Disordered
Compositional bias609-626Basic and acidic residues

Sequence similarities

Belongs to the peptidase S10 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    638
  • Mass (Da)
    71,903
  • Last updated
    2009-07-07 v1
  • Checksum
    E9974ECF7A5C0FF0
MSSCQPPPFLSSMVVRWLSVWIILASSAFASAKCAADYYVRSLPGQPEGPLLKMHAGHIEVDHENNGNLFFWHFQNRHIANRQRTVIWLNGGPGCSSMDGAMMEVGPYRLKDDHTLKYNEGSWDEFANLLFVDQPVGTGYSYANTNSYLHELDEMAAHFVTFMERWFELFPEYEHDDLYFAGESYAGQYIPYIAKAILDRNKNETVIAQRRLWHLKGLLIGNGWFSPVEQYLSYLPYVYKEGMVKNDSDEAKGIERAHSDCVAELDRAKGDVKIHVDVCEKILSAILDVSNKSGHCVNMYDVRLTDTFPSCGMNWPPDLKHLAPYLRRDDVTSALHINKDKKTGWTECAGAVSSSFRPRKSKPSADLLPGLLESGVRIGLFSGAKDLICNHIGTEEFINKMEWSGGKGFELSPGVWAPRRDWTFEGETAGYYQEARNLTYVLFYNASHMVPFDYARRSRDMLDRFLGVDITSIGGNPTDSRIDGEKGALTSVGNHPNSTLAEQREKEKLKAATWKAYYKSGEVALVVVVIAAGAWGFFLWRSRRQRQGSGYLGIYPSLNGLSSGSLPRYRNKRSSRDIEAAAEFEASELETLHDMDDRSPGPSRDNYSVGEDSETEDEKRYPPTDFDRQDGTPSASRT

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias586-601Basic and acidic residues
Compositional bias609-626Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CH476617
EMBL· GenBank· DDBJ
EEP80880.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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