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P00729

- CBPY_YEAST

UniProt

P00729 - CBPY_YEAST

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Protein

Carboxypeptidase Y

Gene

PRC1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

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

Enzyme regulationi

Inhibited by ZPCK.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei257 – 25712 Publications
Active sitei449 – 4491By similarity
Binding sitei452 – 4521Substrate
Active sitei508 – 50811 Publication
Binding sitei509 – 5091Substrate

GO - Molecular functioni

  1. serine-type carboxypeptidase activity Source: SGD

GO - Biological processi

  1. phytochelatin biosynthetic process Source: SGD
  2. protein catabolic process in the vacuole Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Protease

Enzyme and pathway databases

BioCyciYEAST:YMR297W-MONOMER.

Protein family/group databases

MEROPSiS10.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxypeptidase Y (EC:3.4.16.5)
Short name:
cpY
Alternative name(s):
Carboxypeptidase YSCY
Gene namesi
Name:PRC1
Ordered Locus Names:YMR297W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIII

Organism-specific databases

CYGDiYMR297w.
SGDiS000004912. PRC1.

Subcellular locationi

Vacuole
Note: Lysosome-like vacuoles.

GO - Cellular componenti

  1. fungal-type vacuole Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi508 – 5081H → A or R: Inactivates enzyme. 1 Publication

Protein family/group databases

Allergomei8267. Sac c Carboxypeptidase Y.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Propeptidei21 – 111911 PublicationPRO_0000004293Add
BLAST
Chaini112 – 532421Carboxypeptidase YPRO_0000004294Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi124 – 1241N-linked (GlcNAc...)
Disulfide bondi167 ↔ 409
Glycosylationi198 – 1981N-linked (GlcNAc...)
Glycosylationi279 – 2791N-linked (GlcNAc...)
Disulfide bondi304 ↔ 318
Disulfide bondi328 ↔ 351
Disulfide bondi335 ↔ 344
Disulfide bondi373 ↔ 379
Glycosylationi479 – 4791N-linked (GlcNAc...)

Post-translational modificationi

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).

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiP00729.
PaxDbiP00729.
PeptideAtlasiP00729.

Expressioni

Gene expression databases

GenevestigatoriP00729.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
DER1P383072EBI-4153,EBI-5761
HRD1Q081094EBI-4153,EBI-37613
HRD3Q057876EBI-4153,EBI-31647
SEC61P329154EBI-4153,EBI-16400
YOS9Q992202EBI-4153,EBI-34938

Protein-protein interaction databases

BioGridi35477. 31 interactions.
DIPiDIP-2394N.
IntActiP00729. 16 interactions.
MINTiMINT-1956986.
STRINGi4932.YMR297W.

Structurei

Secondary structure

1
532
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi116 – 1183Combined sources
Beta strandi119 – 1213Combined sources
Beta strandi129 – 1346Combined sources
Turni135 – 1384Combined sources
Beta strandi139 – 1468Combined sources
Turni152 – 1543Combined sources
Beta strandi157 – 1615Combined sources
Turni164 – 1663Combined sources
Helixi170 – 1734Combined sources
Turni174 – 1774Combined sources
Beta strandi178 – 1836Combined sources
Turni184 – 1863Combined sources
Beta strandi187 – 1904Combined sources
Helixi195 – 1984Combined sources
Beta strandi199 – 2024Combined sources
Beta strandi214 – 2174Combined sources
Helixi224 – 24017Combined sources
Helixi242 – 2443Combined sources
Turni245 – 2484Combined sources
Beta strandi251 – 2566Combined sources
Helixi259 – 27012Combined sources
Beta strandi282 – 2876Combined sources
Helixi292 – 2954Combined sources
Helixi296 – 2983Combined sources
Helixi299 – 3035Combined sources
Beta strandi307 – 3093Combined sources
Helixi315 – 33824Combined sources
Helixi341 – 35515Combined sources
Helixi357 – 3626Combined sources
Beta strandi368 – 3714Combined sources
Beta strandi375 – 3773Combined sources
Helixi382 – 39110Combined sources
Helixi393 – 3986Combined sources
Beta strandi403 – 4053Combined sources
Helixi411 – 4188Combined sources
Turni419 – 4213Combined sources
Helixi422 – 4243Combined sources
Helixi428 – 4369Combined sources
Beta strandi441 – 4466Combined sources
Helixi454 – 46310Combined sources
Helixi469 – 4746Combined sources
Beta strandi478 – 4814Combined sources
Turni483 – 4853Combined sources
Beta strandi487 – 4926Combined sources
Beta strandi498 – 5036Combined sources
Helixi510 – 5134Combined sources
Helixi515 – 52612Combined sources
Turni527 – 5293Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CPYX-ray2.60A112-532[»]
1WPXX-ray2.70A112-532[»]
1YSCX-ray2.80A112-532[»]
ProteinModelPortaliP00729.
SMRiP00729. Positions 112-532.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00729.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi24 – 274Vacuolar targeting signal

Sequence similaritiesi

Belongs to the peptidase S10 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2939.
GeneTreeiENSGT00770000120552.
HOGENOMiHOG000198296.
InParanoidiP00729.
KOiK13289.
OMAiECSAMED.
OrthoDBiEOG7XDBR1.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
IPR008442. Propeptide_carboxypepY.
[Graphical view]
PANTHERiPTHR11802. PTHR11802. 1 hit.
PfamiPF05388. Carbpep_Y_N. 1 hit.
PF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSiPR00724. CRBOXYPTASEC.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00560. CARBOXYPEPT_SER_HIS. 1 hit.
PS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00729-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKAFTSLLCG LGLSTTLAKA ISLQRPLGLD KDVLLQAAEK FGLDLDLDHL
60 70 80 90 100
LKELDSNVLD AWAQIEHLYP NQVMSLETST KPKFPEAIKT KKDWDFVVKN
110 120 130 140 150
DAIENYQLRV NKIKDPKILG IDPNVTQYTG YLDVEDEDKH FFFWTFESRN
160 170 180 190 200
DPAKDPVILW LNGGPGCSSL TGLFFELGPS SIGPDLKPIG NPYSWNSNAT
210 220 230 240 250
VIFLDQPVNV GFSYSGSSGV SNTVAAGKDV YNFLELFFDQ FPEYVNKGQD
260 270 280 290 300
FHIAGESYAG HYIPVFASEI LSHKDRNFNL TSVLIGNGLT DPLTQYNYYE
310 320 330 340 350
PMACGEGGEP SVLPSEECSA MEDSLERCLG LIESCYDSQS VWSCVPATIY
360 370 380 390 400
CNNAQLAPYQ RTGRNVYDIR KDCEGGNLCY PTLQDIDDYL NQDYVKEAVG
410 420 430 440 450
AEVDHYESCN FDINRNFLFA GDWMKPYHTA VTDLLNQDLP ILVYAGDKDF
460 470 480 490 500
ICNWLGNKAW TDVLPWKYDE EFASQKVRNW TASITDEVAG EVKSYKHFTY
510 520 530
LRVFNGGHMV PFDVPENALS MVNEWIHGGF SL
Length:532
Mass (Da):59,802
Last modified:November 1, 1988 - v1
Checksum:i7227F3489CBDD952
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti260 – 2612GH → HG AA sequence 1 PublicationCurated
Sequence conflicti389 – 3891Y → E AA sequence 1 PublicationCurated
Sequence conflicti529 – 5291G → D AA sequence 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15482 Genomic DNA. Translation: AAA34902.1.
X80836 Genomic DNA. Translation: CAA56806.1.
BK006946 Genomic DNA. Translation: DAA10198.1.
PIRiA26597. CPBYY.
RefSeqiNP_014026.1. NM_001182806.1.

Genome annotation databases

EnsemblFungiiYMR297W; YMR297W; YMR297W.
GeneIDi855343.
KEGGisce:YMR297W.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15482 Genomic DNA. Translation: AAA34902.1 .
X80836 Genomic DNA. Translation: CAA56806.1 .
BK006946 Genomic DNA. Translation: DAA10198.1 .
PIRi A26597. CPBYY.
RefSeqi NP_014026.1. NM_001182806.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CPY X-ray 2.60 A 112-532 [» ]
1WPX X-ray 2.70 A 112-532 [» ]
1YSC X-ray 2.80 A 112-532 [» ]
ProteinModelPortali P00729.
SMRi P00729. Positions 112-532.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 35477. 31 interactions.
DIPi DIP-2394N.
IntActi P00729. 16 interactions.
MINTi MINT-1956986.
STRINGi 4932.YMR297W.

Protein family/group databases

Allergomei 8267. Sac c Carboxypeptidase Y.
MEROPSi S10.001.

Proteomic databases

MaxQBi P00729.
PaxDbi P00729.
PeptideAtlasi P00729.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YMR297W ; YMR297W ; YMR297W .
GeneIDi 855343.
KEGGi sce:YMR297W.

Organism-specific databases

CYGDi YMR297w.
SGDi S000004912. PRC1.

Phylogenomic databases

eggNOGi COG2939.
GeneTreei ENSGT00770000120552.
HOGENOMi HOG000198296.
InParanoidi P00729.
KOi K13289.
OMAi ECSAMED.
OrthoDBi EOG7XDBR1.

Enzyme and pathway databases

BioCyci YEAST:YMR297W-MONOMER.

Miscellaneous databases

EvolutionaryTracei P00729.
NextBioi 979085.

Gene expression databases

Genevestigatori P00729.

Family and domain databases

Gene3Di 3.40.50.1820. 2 hits.
InterProi IPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
IPR008442. Propeptide_carboxypepY.
[Graphical view ]
PANTHERi PTHR11802. PTHR11802. 1 hit.
Pfami PF05388. Carbpep_Y_N. 1 hit.
PF00450. Peptidase_S10. 1 hit.
[Graphical view ]
PRINTSi PR00724. CRBOXYPTASEC.
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00560. CARBOXYPEPT_SER_HIS. 1 hit.
PS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. 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. 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).

Entry informationi

Entry nameiCBPY_YEAST
AccessioniPrimary (citable) accession number: P00729
Secondary accession number(s): D6W0C4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1988
Last modified: November 26, 2014
This is version 164 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 44000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

External Data

Dasty 3