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B5RUL7 (KEX1_DEBHA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pheromone-processing carboxypeptidase KEX1

EC=3.4.16.6
Alternative name(s):
Carboxypeptidase D
Gene names
Name:KEX1
Ordered Locus Names:DEHA2F22352g
OrganismDebaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) [Complete proteome]
Taxonomic identifier284592 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeDebaryomyces

Protein attributes

Sequence length684 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

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.

Subcellular location

Golgi apparatustrans-Golgi network membrane; Single-pass type I membrane protein By similarity.

Sequence similarities

Belongs to the peptidase S10 family.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentGolgi apparatus
Membrane
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionCarboxypeptidase
Hydrolase
Protease
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionserine-type carboxypeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 684666Pheromone-processing carboxypeptidase KEX1
PRO_0000411919

Regions

Topological domain19 – 556538Lumenal Potential
Transmembrane557 – 57721Helical; Potential
Topological domain578 – 684107Cytoplasmic Potential
Compositional bias606 – 6116Poly-Glu

Sites

Active site1811 By similarity
Active site3881 By similarity
Active site4461 By similarity

Amino acid modifications

Glycosylation621N-linked (GlcNAc...) Potential
Glycosylation4241N-linked (GlcNAc...) Potential
Glycosylation4351N-linked (GlcNAc...) Potential
Glycosylation4741N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
B5RUL7 [UniParc].

Last modified November 4, 2008. Version 1.
Checksum: 8254AE19456BE382

FASTA68477,336
        10         20         30         40         50         60 
MVIKYLLLIL VQSFVAFALP FTSRSDPKAE YLVTSLPGLY SNIRTDERPL MFAGQLELYP 

        70         80         90        100        110        120 
ENQTHYFFWK YQDTNQIPEA KKRTIFWLNG GPGCSSMDGA LMEAGPFRIN KEGEVIYNEG 

       130        140        150        160        170        180 
SWHKSGDMVF VDQPAGTGFS YSDDYDHDLD QITVEFVRFM EKFFELFPED ASNEIYFAGE 

       190        200        210        220        230        240 
SYAGQYIPYI ADGILRRNKN LREGEKPFNL KGLMIGNGWI APNEQSLSYL PYSVQAGIIK 

       250        260        270        280        290        300 
TNNPRWSSIL RQHQECQDIV SENDGPDGSD VSQVVSNTCE RVLNLILEAT RDQSAADNEQ 

       310        320        330        340        350        360 
CVNMYDHTLR DSYPSCGMNW PPDLANVTPF LREQSVMNDL NLINHKKWSE CSGKVGNSFR 

       370        380        390        400        410        420 
AKNSKPAIHL FPSILEEIPI MLFNGNRDII CNYIGIEGFI KKLTWNGQTG FSEDLDTLDW 

       430        440        450        460        470        480 
VYDNKTAGYI QSERNLTVVN VFDASHMVPF DKPEISRSLI DIITGNFDEK EVDNKSDMKK 

       490        500        510        520        530        540 
KSIVTYPLGV RMAKQKEESE SKTSPTSVTQ SKTSSISAVS GKSLATSTTL DQEHSATPSA 

       550        560        570        580        590        600 
EAERAKNQQT SNRITRLIQL LVIVVLIWGV YILYSSYRSR PSSIIKTGPS GKKKNVQWAD 

       610        620        630        640        650        660 
QLRQFEEEEI EQNEQGILSR ALNKLKGGDS RGTYAPTSGK TYEDIEMNEG ITEHTDNRVD 

       670        680 
DFIIESDEED AHDENQTNKQ SVSK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR382138 Genomic DNA. Translation: CAR66395.1.
RefSeqXP_002770877.1. XM_002770831.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING4959.B5RUL7.

Protein family/group databases

MEROPSS10.007.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID8999041.
KEGGdha:DEHA2F22352g.

Phylogenomic databases

HOGENOMHOG000208879.
KOK01288.
OMATIMANTR.
OrthoDBEOG7TJ3SJ.

Family and domain databases

InterProIPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view]
PANTHERPTHR11802. PTHR11802. 1 hit.
PfamPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSPR00724. CRBOXYPTASEC.
PROSITEPS00560. CARBOXYPEPT_SER_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKEX1_DEBHA
AccessionPrimary (citable) accession number: B5RUL7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: November 4, 2008
Last modified: February 19, 2014
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries