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Protein

Carboxypeptidase S

Gene

CPS1

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

Necessary for use of certain peptides as sole nitrogen source. May also cleave intracellularly generated peptides to recycle amino acids for protein synthesis.

Catalytic activityi

Release of a C-terminal amino acid from a peptide in which glycine is the penultimate amino acid, e.g. Z-Gly-|-Leu.

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi168 – 1681Zinc 2By similarity
Active sitei170 – 1701By similarity
Metal bindingi205 – 2051Zinc 1By similarity
Metal bindingi205 – 2051Zinc 2By similarity
Active sitei239 – 2391Proton acceptorBy similarity
Metal bindingi240 – 2401Zinc 1By similarity
Metal bindingi268 – 2681Zinc 2By similarity
Metal bindingi547 – 5471Zinc 1By similarity

GO - Molecular functioni

  • carboxypeptidase activity Source: SGD
  • metallocarboxypeptidase activity Source: InterPro
  • metallodipeptidase activity Source: GO_Central
  • zinc ion binding Source: GO_Central

GO - Biological processi

  • nitrogen compound metabolic process Source: SGD
  • peptide catabolic process Source: GO_Central
  • proteolysis involved in cellular protein catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:YJL172W-MONOMER.

Protein family/group databases

MEROPSiM20.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxypeptidase S (EC:3.4.17.4)
Alternative name(s):
GLY-X carboxypeptidase
YSCS
Gene namesi
Name:CPS1
Synonyms:CPS
Ordered Locus Names:YJL172W
ORF Names:J0510
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL172W.
SGDiS000003708. CPS1.

Subcellular locationi

  • Vacuole membrane 2 Publications; Single-pass membrane protein 2 Publications

  • Note: Lysosome-like vacuoles.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1919CytoplasmicSequence analysisAdd
BLAST
Transmembranei20 – 4021HelicalSequence analysisAdd
BLAST
Topological domaini41 – 576536LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

  • fungal-type vacuole lumen Source: SGD
  • integral component of membrane Source: UniProtKB-KW
  • vacuolar membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 576576Carboxypeptidase SPRO_0000185271Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki8 – 8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Glycosylationi88 – 881N-linked (GlcNAc...)Sequence analysis
Glycosylationi176 – 1761N-linked (GlcNAc...)Sequence analysis
Glycosylationi228 – 2281N-linked (GlcNAc...)Sequence analysis
Glycosylationi381 – 3811N-linked (GlcNAc...)Sequence analysis
Glycosylationi525 – 5251N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Glycosylated.
Ubiquitinated. Ubiquitination mediates sorting into internal vesicles in late endosomes. TUL1 is required for ubiquitination.1 Publication

Keywords - PTMi

Glycoprotein, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP27614.

Interactioni

Subunit structurei

yscS is synthesized as one polypeptide chain precursor which after carbohydrate modification in the secretory pathway yields two active precursor molecules. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble.

Protein-protein interaction databases

BioGridi33588. 17 interactions.
DIPiDIP-5566N.
IntActiP27614. 4 interactions.
MINTiMINT-561556.

Structurei

3D structure databases

ProteinModelPortaliP27614.
SMRiP27614. Positions 152-246.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The transmembrane domain contains polar residues that mediate the recognition by TUL1.

Sequence similaritiesi

Belongs to the peptidase M20A family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00840000129850.
HOGENOMiHOG000194592.
InParanoidiP27614.
KOiK01293.
OMAiGSNDCKN.
OrthoDBiEOG092C13PF.

Family and domain databases

Gene3Di3.30.70.360. 2 hits.
InterProiIPR001261. ArgE/DapE_CS.
IPR017141. Pept_M20_carboxypep.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamiPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFiPIRSF037217. Carboxypeptidase_S. 1 hit.
SUPFAMiSSF55031. SSF55031. 2 hits.
PROSITEiPS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P27614-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIALPVEKAP RKSLWQRHRA FISGIVALII IGTFFLTSGL HPAPPHEAKR
60 70 80 90 100
PHHGKGPMHS PKCEKIEPLS PSFKHSVDTI LHDPAFRNSS IEKLSNAVRI
110 120 130 140 150
PTVVQDKNPN PADDPDFYKH FYELHDYFEK TFPNIHKHLK LEKVNELGLL
160 170 180 190 200
YTWEGSDPDL KPLLLMAHQD VVPVNNETLS SWKFPPFSGH YDPETDFVWG
210 220 230 240 250
RGSNDCKNLL IAEFEAIEQL LIDGFKPNRT IVMSLGFDEE ASGTLGAASL
260 270 280 290 300
ASFLHERYGD DGIYSIIDEG EGIMEVDKDV FVATPINAEK GYVDFEVSIL
310 320 330 340 350
GHGGHSSVPP DHTTIGIASE LITEFEANPF DYEFEFDNPI YGLLTCAAEH
360 370 380 390 400
SKSLSKDVKK TILGAPFCPR RKDKLVEYIS NQSHLRSLIR TTQAVDIING
410 420 430 440 450
GVKANALPET TRFLINHRIN LHSSVAEVFE RNIEYAKKIA EKYGYGLSKN
460 470 480 490 500
GDDYIIPETE LGHIDITLLR ELEPAPLSPS SGPVWDILAG TIQDVFENGV
510 520 530 540 550
LQNNEEFYVT TGLFSGNTDT KYYWNLSKNI YRFVGSIIDI DLLKTLHSVN
560 570
EHVDVPGHLS AIAFVYEYIV NVNEYA
Length:576
Mass (Da):64,597
Last modified:November 1, 1995 - v2
Checksum:i5CBB536D421B5F70
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti387 – 3871S → T in CAA40571 (PubMed:1709881).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57316 Genomic DNA. Translation: CAA40571.1.
X63068 Genomic DNA. Translation: CAA44790.1.
Z49447 Genomic DNA. Translation: CAA89467.1.
BK006943 Genomic DNA. Translation: DAA08632.1.
PIRiS16693.
RefSeqiNP_012363.1. NM_001181605.1.

Genome annotation databases

EnsemblFungiiYJL172W; YJL172W; YJL172W.
GeneIDi853267.
KEGGisce:YJL172W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57316 Genomic DNA. Translation: CAA40571.1.
X63068 Genomic DNA. Translation: CAA44790.1.
Z49447 Genomic DNA. Translation: CAA89467.1.
BK006943 Genomic DNA. Translation: DAA08632.1.
PIRiS16693.
RefSeqiNP_012363.1. NM_001181605.1.

3D structure databases

ProteinModelPortaliP27614.
SMRiP27614. Positions 152-246.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33588. 17 interactions.
DIPiDIP-5566N.
IntActiP27614. 4 interactions.
MINTiMINT-561556.

Protein family/group databases

MEROPSiM20.002.

Proteomic databases

MaxQBiP27614.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL172W; YJL172W; YJL172W.
GeneIDi853267.
KEGGisce:YJL172W.

Organism-specific databases

EuPathDBiFungiDB:YJL172W.
SGDiS000003708. CPS1.

Phylogenomic databases

GeneTreeiENSGT00840000129850.
HOGENOMiHOG000194592.
InParanoidiP27614.
KOiK01293.
OMAiGSNDCKN.
OrthoDBiEOG092C13PF.

Enzyme and pathway databases

BioCyciYEAST:YJL172W-MONOMER.

Miscellaneous databases

PROiP27614.

Family and domain databases

Gene3Di3.30.70.360. 2 hits.
InterProiIPR001261. ArgE/DapE_CS.
IPR017141. Pept_M20_carboxypep.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamiPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFiPIRSF037217. Carboxypeptidase_S. 1 hit.
SUPFAMiSSF55031. SSF55031. 2 hits.
PROSITEiPS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCBPS_YEAST
AccessioniPrimary (citable) accession number: P27614
Secondary accession number(s): D6VW16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: November 1, 1995
Last modified: September 7, 2016
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 721 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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