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P30574 (CBPY_CANAX) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 81. 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:
Carboxypeptidase Y

EC=3.4.16.5
Alternative name(s):
Carboxypeptidase YSCY
Gene names
Name:CPY1
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length542 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in degradation of small peptides.

Catalytic activity

Release of a C-terminal amino acid with broad specificity.

Subcellular location

Vacuole. Note: Lysosome-like vacuoles.

Induction

Transiently down-regulated during the early events of yeast to hyphae conversion.

Sequence similarities

Belongs to the peptidase S10 family.

Ontologies

Keywords
   Cellular componentVacuole
   DomainSignal
   Molecular functionCarboxypeptidase
Hydrolase
Protease
   PTMDisulfide bond
Glycoprotein
Zymogen
Gene Ontology (GO)
   Cellular_componentvacuole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 2121 Potential
Propeptide22 – 127106 Potential
PRO_0000004289
Chain128 – 542415Carboxypeptidase Y
PRO_0000004290

Sites

Active site2691 By similarity
Active site4611 By similarity
Active site5181 By similarity
Binding site4641Substrate By similarity
Binding site5191Substrate By similarity

Amino acid modifications

Glycosylation2131N-linked (GlcNAc...) Potential
Glycosylation2911N-linked (GlcNAc...) Potential
Disulfide bond182 ↔ 421 By similarity
Disulfide bond316 ↔ 330 By similarity
Disulfide bond340 ↔ 363 By similarity
Disulfide bond347 ↔ 356 By similarity
Disulfide bond385 ↔ 391 By similarity

Sequences

Sequence LengthMass (Da)Tools
P30574 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 7FA6B9F82F9D44AF

FASTA54261,044
        10         20         30         40         50         60 
MKLSKSTLIA TLALTATSTN ALVVQNPFSN IQQALKLDLS YDKLTSKLTD TFEQGKANII 

        70         80         90        100        110        120 
STIAKVMNEP LDGLTPEIKN IWSEMLMKFP NSITELNFKA PPKKGKITTQ QFDFHVTDAQ 

       130        140        150        160        170        180 
VPNHKLRIKS TPKDLGIDTV KQYSGYLDVV DEDKHFFYYF FESRNDPKND PVILWLNGGP 

       190        200        210        220        230        240 
GCSSLTGLFF ELGPSSIDKN LKPVYNPHSW NANASVIFLD QPINVGYSYS SQSVSNTIAA 

       250        260        270        280        290        300 
GKDVYAFLQL FFKNFPEYAN LDFHIAGESY AGHYIPAFAS EILTHPERNF NLTSVLIGNG 

       310        320        330        340        350        360 
LTDPLVQYEY YEPMACGEGG EPSVLEPEEC DGMLNSLPRC LSLIESCYES GSVWSCVPAT 

       370        380        390        400        410        420 
IYCNNGQMGP YQKTGRNVYD IRTMCEGSSL CYSQLEYIDQ YLNLPEVKKA LGAEVDEYQS 

       430        440        450        460        470        480 
CNFDINRNFM FAGDWMKPYQ KNVIDLLEKE LPVLIYAGDK DFICNWLGNQ AWTNRLEWSG 

       490        500        510        520        530        540 
SKGFTKAPVK SWKVGKNAAG EVKNYKHFTF LRVFGGGHMV PYDQPENALD MVNRWISGDY 


KY 

« Hide

References

[1]"The carboxypeptidase Y-encoding gene from Candida albicans and its transcription during yeast-to-hyphae conversion."
Mukhtar M., Logan D.A., Kaufer N.F.
Gene 121:173-177(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M95182 Genomic DNA. Translation: AAA34326.2.
PIRJC1380.

3D structure databases

ProteinModelPortalP30574.
SMRP30574. Positions 132-540.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS10.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG2939.

Family and domain databases

Gene3D3.40.50.1820. 2 hits.
InterProIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
IPR008442. Propeptide_carboxypepY.
[Graphical view]
PANTHERPTHR11802. PTHR11802. 1 hit.
PfamPF05388. Carbpep_Y_N. 1 hit.
PF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSPR00724. CRBOXYPTASEC.
SUPFAMSSF53474. SSF53474. 1 hit.
PROSITEPS00560. CARBOXYPEPT_SER_HIS. 1 hit.
PS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCBPY_CANAX
AccessionPrimary (citable) accession number: P30574
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 1, 1995
Last modified: June 11, 2014
This is version 81 of the entry and version 2 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