Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P00729 (CBPY_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carboxypeptidase Y

Short name=cpY
EC=3.4.16.5
Alternative name(s):
Carboxypeptidase YSCY
Gene names
Name:PRC1
Ordered Locus Names:YMR297W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length532 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate.

Catalytic activity

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

Enzyme regulation

Inhibited by ZPCK.

Subcellular location

Vacuole. Note: Lysosome-like vacuoles.

Post-translational modification

Enters the endoplasmic reticulum as an inactive zymogen and is modified by four N-linked core oligosaccharides, giving rise to a precursor known as P1 (67 kDa). As P1 transits through the Golgi, extension of its core oligosaccharides leads to the Golgi-modified P2 precursor (69 kDa). P2 is sorted away from secretory proteins at or beyond a late Golgi compartment and is subsequently delivered to the vacuole via a prevacuolar endosome-like compartment. Upon arrival in the vacuole, the N-terminal prosegment of P2 is cleaved to yield the enzymatically active mature vacuolar form of CPY (61 kDa).

Miscellaneous

Present with 44000 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the peptidase S10 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 11191
PRO_0000004293
Chain112 – 532421Carboxypeptidase Y
PRO_0000004294

Regions

Motif24 – 274Vacuolar targeting signal

Sites

Active site2571 Ref.5 Ref.9
Active site4491 By similarity
Active site5081 Ref.6
Binding site4521Substrate
Binding site5091Substrate

Amino acid modifications

Glycosylation1241N-linked (GlcNAc...)
Glycosylation1981N-linked (GlcNAc...)
Glycosylation2791N-linked (GlcNAc...)
Glycosylation4791N-linked (GlcNAc...)
Disulfide bond167 ↔ 409
Disulfide bond304 ↔ 318
Disulfide bond328 ↔ 351
Disulfide bond335 ↔ 344
Disulfide bond373 ↔ 379

Experimental info

Mutagenesis5081H → A or R: Inactivates enzyme.
Sequence conflict260 – 2612GH → HG AA sequence Ref.4
Sequence conflict3891Y → E AA sequence Ref.4
Sequence conflict5291G → D AA sequence Ref.4

Secondary structure

................................................................................... 532
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00729 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: 7227F3489CBDD952

FASTA53259,802
        10         20         30         40         50         60 
MKAFTSLLCG LGLSTTLAKA ISLQRPLGLD KDVLLQAAEK FGLDLDLDHL LKELDSNVLD 

        70         80         90        100        110        120 
AWAQIEHLYP NQVMSLETST KPKFPEAIKT KKDWDFVVKN DAIENYQLRV NKIKDPKILG 

       130        140        150        160        170        180 
IDPNVTQYTG YLDVEDEDKH FFFWTFESRN DPAKDPVILW LNGGPGCSSL TGLFFELGPS 

       190        200        210        220        230        240 
SIGPDLKPIG NPYSWNSNAT VIFLDQPVNV GFSYSGSSGV SNTVAAGKDV YNFLELFFDQ 

       250        260        270        280        290        300 
FPEYVNKGQD FHIAGESYAG HYIPVFASEI LSHKDRNFNL TSVLIGNGLT DPLTQYNYYE 

       310        320        330        340        350        360 
PMACGEGGEP SVLPSEECSA MEDSLERCLG LIESCYDSQS VWSCVPATIY CNNAQLAPYQ 

       370        380        390        400        410        420 
RTGRNVYDIR KDCEGGNLCY PTLQDIDDYL NQDYVKEAVG AEVDHYESCN FDINRNFLFA 

       430        440        450        460        470        480 
GDWMKPYHTA VTDLLNQDLP ILVYAGDKDF ICNWLGNKAW TDVLPWKYDE EFASQKVRNW 

       490        500        510        520        530 
TASITDEVAG EVKSYKHFTY LRVFNGGHMV PFDVPENALS MVNEWIHGGF SL 

« Hide

References

« Hide 'large scale' references
[1]"Protein sorting in yeast: the localization determinant of yeast vacuolar carboxypeptidase Y resides in the propeptide."
Valls L.A., Hunter C.P., Rothman J.H., Stevens T.H.
Cell 48:887-897(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Amino acid sequence of carboxypeptidase Y. II. Peptides from enzymatic cleavages."
Svendsen I., Martin B.M., Viswanatha T., Johansen J.T.
Carlsberg Res. Commun. 47:15-27(1982)
Cited for: PROTEIN SEQUENCE OF 112-532.
[5]"Identification of methionyl and cysteinyl residues in the substrate binding site of carboxypeptidase Y."
Breddam K., Svendsen I.
Carlsberg Res. Commun. 49:639-645(1984)
Cited for: SEQUENCE REVISION, ACTIVE SITE SER-257.
[6]"Inactivation of carboxypeptidase Y by mutational removal of the putative essential histidyl residue."
Bech L.M., Breddam K.
Carlsberg Res. Commun. 54:165-171(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE HIS-508.
[7]"Site-directed mutagenesis on (serine) carboxypeptidase Y. A hydrogen bond network stabilizes the transition state by interaction with the C-terminal carboxylate group of the substrate."
Mortensen U.H., Remington S.J., Breddam K.
Biochemistry 33:508-517(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]"2.8-A structure of yeast serine carboxypeptidase."
Endrizzi J.A., Breddam K., Remington S.J.
Biochemistry 33:11106-11120(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15482 Genomic DNA. Translation: AAA34902.1.
X80836 Genomic DNA. Translation: CAA56806.1.
BK006946 Genomic DNA. Translation: DAA10198.1.
PIRCPBYY. A26597.
RefSeqNP_014026.1. NM_001182806.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CPYX-ray2.60A112-532[»]
1WPXX-ray2.70A112-532[»]
1YSCX-ray2.80A112-532[»]
ProteinModelPortalP00729.
SMRP00729. Positions 112-532.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35477. 31 interactions.
DIPDIP-2394N.
IntActP00729. 16 interactions.
MINTMINT-1956986.
STRING4932.YMR297W.

Protein family/group databases

Allergome8267. Sac c Carboxypeptidase Y.
MEROPSS10.001.

Proteomic databases

MaxQBP00729.
PaxDbP00729.
PeptideAtlasP00729.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR297W; YMR297W; YMR297W.
GeneID855343.
KEGGsce:YMR297W.

Organism-specific databases

CYGDYMR297w.
SGDS000004912. PRC1.

Phylogenomic databases

eggNOGCOG2939.
GeneTreeENSGT00560000077221.
HOGENOMHOG000198296.
KOK13289.
OMAECSAMED.
OrthoDBEOG7XDBR1.

Enzyme and pathway databases

BioCycYEAST:YMR297W-MONOMER.

Gene expression databases

GenevestigatorP00729.

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...

Other

EvolutionaryTraceP00729.
NextBio979085.

Entry information

Entry nameCBPY_YEAST
AccessionPrimary (citable) accession number: P00729
Secondary accession number(s): D6W0C4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1988
Last modified: June 11, 2014
This is version 161 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references