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Protein

Carboxypeptidase Y

Gene

PRC1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei2572 Publications1
Active sitei449By similarity1
Binding sitei452Substrate1
Active sitei5081 Publication1
Binding sitei509Substrate1

GO - Molecular functioni

  • serine-type carboxypeptidase activity Source: SGD

GO - Biological processi

  • phytochelatin biosynthetic process Source: SGD
  • protein catabolic process in the vacuole Source: SGD
  • proteolysis involved in cellular protein catabolic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Protease

Enzyme and pathway databases

BioCyciYEAST:YMR297W-MONOMER.
BRENDAi3.4.16.5. 984.
ReactomeiR-SCE-6798695. Neutrophil degranulation.

Protein family/group databases

ESTHERiyeast-cbpy1. Carboxypeptidase_S10.
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
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR297W.
SGDiS000004912. PRC1.

Subcellular locationi

  • Vacuole

  • Note: Lysosome-like vacuoles.

GO - Cellular componenti

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

Keywords - Cellular componenti

Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi508H → A or R: Inactivates enzyme. 1 Publication1

Protein family/group databases

Allergomei8267. Sac c Carboxypeptidase Y.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
PropeptideiPRO_000000429321 – 1111 PublicationAdd BLAST91
ChainiPRO_0000004294112 – 532Carboxypeptidase YAdd BLAST421

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi124N-linked (GlcNAc...)1
Disulfide bondi167 ↔ 409
Glycosylationi198N-linked (GlcNAc...)1
Glycosylationi279N-linked (GlcNAc...)1
Disulfide bondi304 ↔ 318
Disulfide bondi328 ↔ 351
Disulfide bondi335 ↔ 344
Disulfide bondi373 ↔ 379
Glycosylationi479N-linked (GlcNAc...)1

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.
PRIDEiP00729.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
DER1P383072EBI-4153,EBI-5761
HRD1Q0810911EBI-4153,EBI-37613
HRD3Q057876EBI-4153,EBI-31647
SEC61P329154EBI-4153,EBI-16400
YOS9Q992202EBI-4153,EBI-34938

Protein-protein interaction databases

BioGridi35477. 33 interactors.
DIPiDIP-2394N.
IntActiP00729. 17 interactors.
MINTiMINT-1956986.

Structurei

Secondary structure

1532
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi116 – 118Combined sources3
Beta strandi119 – 121Combined sources3
Beta strandi129 – 134Combined sources6
Turni135 – 138Combined sources4
Beta strandi139 – 146Combined sources8
Turni152 – 154Combined sources3
Beta strandi157 – 161Combined sources5
Turni164 – 166Combined sources3
Helixi170 – 173Combined sources4
Turni174 – 177Combined sources4
Beta strandi178 – 183Combined sources6
Turni184 – 186Combined sources3
Beta strandi187 – 190Combined sources4
Helixi195 – 198Combined sources4
Beta strandi199 – 202Combined sources4
Beta strandi214 – 217Combined sources4
Helixi224 – 240Combined sources17
Helixi242 – 244Combined sources3
Turni245 – 248Combined sources4
Beta strandi251 – 256Combined sources6
Helixi259 – 270Combined sources12
Beta strandi282 – 287Combined sources6
Helixi292 – 295Combined sources4
Helixi296 – 298Combined sources3
Helixi299 – 303Combined sources5
Beta strandi307 – 309Combined sources3
Helixi315 – 338Combined sources24
Helixi341 – 355Combined sources15
Helixi357 – 362Combined sources6
Beta strandi368 – 371Combined sources4
Beta strandi375 – 377Combined sources3
Helixi382 – 391Combined sources10
Helixi393 – 398Combined sources6
Beta strandi403 – 405Combined sources3
Helixi411 – 418Combined sources8
Turni419 – 421Combined sources3
Helixi422 – 424Combined sources3
Helixi428 – 436Combined sources9
Beta strandi441 – 446Combined sources6
Helixi454 – 463Combined sources10
Helixi469 – 474Combined sources6
Beta strandi478 – 481Combined sources4
Turni483 – 485Combined sources3
Beta strandi487 – 492Combined sources6
Beta strandi498 – 503Combined sources6
Helixi510 – 513Combined sources4
Helixi515 – 526Combined sources12
Turni527 – 529Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP00729.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi24 – 27Vacuolar targeting signal4

Sequence similaritiesi

Belongs to the peptidase S10 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

GeneTreeiENSGT00860000133774.
HOGENOMiHOG000198296.
InParanoidiP00729.
KOiK13289.
OMAiPDVKQYS.
OrthoDBiEOG092C1EU7.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR008442. Propeptide_carboxypepY.
IPR033124. Ser_caboxypep_his_AS.
IPR018202. Ser_caboxypep_ser_AS.
[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)DescriptionActionsGraphical viewLength
Sequence conflicti260 – 261GH → HG AA sequence (Ref. 4) Curated2
Sequence conflicti389Y → E AA sequence (Ref. 4) Curated1
Sequence conflicti529G → D AA sequence (Ref. 4) Curated1

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.
PIRiA26597. CPBYY.
RefSeqiNP_014026.1. NM_001182806.1.

3D structure databases

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

Protein-protein interaction databases

BioGridi35477. 33 interactors.
DIPiDIP-2394N.
IntActiP00729. 17 interactors.
MINTiMINT-1956986.

Protein family/group databases

Allergomei8267. Sac c Carboxypeptidase Y.
ESTHERiyeast-cbpy1. Carboxypeptidase_S10.
MEROPSiS10.001.

Proteomic databases

MaxQBiP00729.
PRIDEiP00729.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YMR297W.
SGDiS000004912. PRC1.

Phylogenomic databases

GeneTreeiENSGT00860000133774.
HOGENOMiHOG000198296.
InParanoidiP00729.
KOiK13289.
OMAiPDVKQYS.
OrthoDBiEOG092C1EU7.

Enzyme and pathway databases

BioCyciYEAST:YMR297W-MONOMER.
BRENDAi3.4.16.5. 984.
ReactomeiR-SCE-6798695. Neutrophil degranulation.

Miscellaneous databases

EvolutionaryTraceiP00729.
PROiP00729.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR008442. Propeptide_carboxypepY.
IPR033124. Ser_caboxypep_his_AS.
IPR018202. Ser_caboxypep_ser_AS.
[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]
ProtoNetiSearch...

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 30, 2016
This is version 184 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.