Reviewed, UniProtKB/Swiss-Prot P27614 (CBPS_YEAST)

Names and origin

Protein names

Recommended name:
    Carboxypeptidase S
    EC=3.4.17.4
Alternative name(s):
    YSCS
    GLY-X carboxypeptidase

Gene names

Name:	CPS1
Synonyms:	CPS
Ordered Locus Names:	YJL172W
ORF Names:	J0510

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	576 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Necessary for use of certain peptides as sole nitrogen source. May also cleave intracellularly generated peptides to recycle amino acids for protein synthesis.
Catalytic activity	Release of a C-terminal amino acid from a peptide in which glycine is the penultimate amino acid, e.g. Z-Gly-|-Leu.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Subunit structure	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.
Subcellular location	Vacuole membrane; Single-pass membrane protein. Note: Lysosome-like vacuoles. Ref.4 Ref.6
Domain	The transmembrane domain contains polar residues that mediate the recognition by TUL1.
Post-translational modification	Glycosylated. Ubiquitinated. Ubiquitination mediates sorting into internal vesicles in late endosomes. TUL1 is required for ubiquitination. Ref.7
Miscellaneous	Present with 721 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the peptidase M20A family.

Ontologies

Keywords
Cellular component	Membrane Vacuole
Domain	Transmembrane
Ligand	Metal-binding Zinc
Molecular function	Carboxypeptidase Hydrolase Protease
PTM	Glycoprotein Ubl conjugation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	nitrogen compound metabolic process Ref.1 Inferred from mutant phenotype. Source: SGD proteolysis Ref.1 Inferred from mutant phenotype. Source: SGD
Cellular component	fungal-type vacuole Ref.1 Traceable author statement. Source: SGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	carboxypeptidase activity Ref.1 Inferred from mutant phenotype. Source: SGD metallopeptidase activity Inferred from electronic annotation. Source: InterPro protein dimerization activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 576	576	Carboxypeptidase S		PRO_0000185271
Regions
	Topological domain	1 – 19	19	Cytoplasmic Potential
	Transmembrane	20 – 40	21	Potential
	Topological domain	41 – 576	536	Lumenal Potential
Sites
	Active site	170	1	By similarity
	Active site	239	1	Proton acceptor By similarity
	Metal binding	168	1	Zinc 2 By similarity
	Metal binding	205	1	Zinc 1 By similarity
	Metal binding	205	1	Zinc 2 By similarity
	Metal binding	240	1	Zinc 1 By similarity
	Metal binding	268	1	Zinc 2 By similarity
	Metal binding	547	1	Zinc 1 By similarity
Amino acid modifications
	Glycosylation	88	1	N-linked (GlcNAc...) Potential
	Glycosylation	176	1	N-linked (GlcNAc...) Potential
	Glycosylation	228	1	N-linked (GlcNAc...) Potential
	Glycosylation	381	1	N-linked (GlcNAc...) Potential
	Glycosylation	525	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	387	1	S → T in CAA40571. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P27614-1 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: 5CBB536D421B5F70	FASTA	576	64,597
	10 20 30 40 50 60 MIALPVEKAP RKSLWQRHRA FISGIVALII IGTFFLTSGL HPAPPHEAKR PHHGKGPMHS 70 80 90 100 110 120 PKCEKIEPLS PSFKHSVDTI LHDPAFRNSS IEKLSNAVRI PTVVQDKNPN PADDPDFYKH 130 140 150 160 170 180 FYELHDYFEK TFPNIHKHLK LEKVNELGLL YTWEGSDPDL KPLLLMAHQD VVPVNNETLS 190 200 210 220 230 240 SWKFPPFSGH YDPETDFVWG RGSNDCKNLL IAEFEAIEQL LIDGFKPNRT IVMSLGFDEE 250 260 270 280 290 300 ASGTLGAASL ASFLHERYGD DGIYSIIDEG EGIMEVDKDV FVATPINAEK GYVDFEVSIL 310 320 330 340 350 360 GHGGHSSVPP DHTTIGIASE LITEFEANPF DYEFEFDNPI YGLLTCAAEH SKSLSKDVKK 370 380 390 400 410 420 TILGAPFCPR RKDKLVEYIS NQSHLRSLIR TTQAVDIING GVKANALPET TRFLINHRIN 430 440 450 460 470 480 LHSSVAEVFE RNIEYAKKIA EKYGYGLSKN GDDYIIPETE LGHIDITLLR ELEPAPLSPS 490 500 510 520 530 540 SGPVWDILAG TIQDVFENGV LQNNEEFYVT TGLFSGNTDT KYYWNLSKNI YRFVGSIIDI 550 560 570 DLLKTLHSVN EHVDVPGHLS AIAFVYEYIV NVNEYA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Carboxypeptidase yscS: gene structure and function of the vacuolar enzyme." Spormann D.O., Heim J., Wolf D.H. Eur. J. Biochem. 197:399-405(1991) [PubMed: 2026161] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"Molecular cloning and sequencing of genomic DNA encoding yeast vacuolar carboxypeptidase yscS." Bordallo J., Bordallo C., Gascon S., Suarez-Rendueles P. FEBS Lett. 283:27-32(1991) [PubMed: 1709881] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204510 / AB320.
[3]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L. EMBO J. 15:2031-2049(1996) [PubMed: 8641269] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	"Biogenesis of the yeast vacuole (lysosome). The precursor forms of the soluble hydrolase carboxypeptidase yscS are associated with the vacuolar membrane." Spormann D.O., Heim J., Wolf D.H. J. Biol. Chem. 267:8021-8029(1992) [PubMed: 1569061] [Abstract] Cited for: SUBCELLULAR LOCATION.
[5]	"Protein family classification based on searching a database of blocks." Henikoff S., Henikoff J.G. Genomics 19:97-107(1994) [PubMed: 8188249] [Abstract] Cited for: SIMILARITY TO ARGE/DAPE/ACY1/CPG2/YSCS FAMILY.
[6]	"Sorting of proteins into multivesicular bodies: ubiquitin-dependent and -independent targeting." Reggiori F., Pelham H.R.B. EMBO J. 20:5176-5186(2001) [PubMed: 11566881] [Abstract] Cited for: SUBCELLULAR LOCATION.
[7]	"A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies." Reggiori F., Pelham H.R.B. Nat. Cell Biol. 4:117-123(2002) [PubMed: 11788821] [Abstract] Cited for: UBIQUITINATION BY TUL1.
[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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X57316 Genomic DNA. Translation: CAA40571.1. X63068 Genomic DNA. Translation: CAA44790.1. Z49447 Genomic DNA. Translation: CAA89467.1.
PIR	S16693.
RefSeq	NP_012363.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:5566N.
IntAct	P27614. 2 interactions.
STRING	P27614.
Protein family/group databases
MEROPS	M20.002.
Proteomic databases
PeptideAtlas	P27614.
Genome annotation databases
Ensembl	YJL172W; YJL172W; YJL172W; Saccharomyces cerevisiae. [Genome view]
GeneID	853267.
KEGG	sce:YJL172W.
NMPDR	fig|4932.3.peg.3327.
Organism-specific databases
CYGD	YJL172w.
SGD	S000003708. CPS1.
Phylogenomic databases
HOGENOM	P27614.
OMA	LAHQDVV
OrthoDB	EOG9Q5B5M
Enzyme and pathway databases
BRENDA	3.4.17.4. 250.
Gene expression databases
ArrayExpress	P27614.
Genevestigator	P27614.
GermOnline	YJL172W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001261. ArgE/DapE_CS. IPR017141. Pept_M20_carboxypep. IPR002933. Peptidase_M20. IPR011650. Peptidase_M20_dimer. [Graphical view]
Pfam	PF07687. M20_dimer. 1 hit. PF01546. Peptidase_M20. 1 hit. [Graphical view]
PIRSF	PIRSF037217. Carboxypeptidase_S. 1 hit.
PROSITE	PS00758. ARGE_DAPE_CPG2_1. 1 hit. PS00759. ARGE_DAPE_CPG2_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	973535.

Entry information

Entry name

CBPS_YEAST

Accession

Primary (citable) accession number: P27614

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	November 1, 1995
Last modified:	November 24, 2009
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)