CBPS_YEAST
ID CBPS_YEAST Reviewed; 576 AA.
AC P27614; D6VW16;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Carboxypeptidase S;
DE EC=3.4.17.4;
DE AltName: Full=GLY-X carboxypeptidase;
DE AltName: Full=YSCS;
GN Name=CPS1; Synonyms=CPS; OrderedLocusNames=YJL172W; ORFNames=J0510;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=2026161; DOI=10.1111/j.1432-1033.1991.tb15924.x;
RA Spormann D.O., Heim J., Wolf D.H.;
RT "Carboxypeptidase yscS: gene structure and function of the vacuolar
RT enzyme.";
RL Eur. J. Biochem. 197:399-405(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204510 / AB320;
RX PubMed=1709881; DOI=10.1016/0014-5793(91)80546-f;
RA Bordallo J., Bordallo C., Gascon S., Suarez-Rendueles P.;
RT "Molecular cloning and sequencing of genomic DNA encoding yeast vacuolar
RT carboxypeptidase yscS.";
RL FEBS Lett. 283:27-32(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=1569061; DOI=10.1016/s0021-9258(18)42402-7;
RA Spormann D.O., Heim J., Wolf D.H.;
RT "Biogenesis of the yeast vacuole (lysosome). The precursor forms of the
RT soluble hydrolase carboxypeptidase yscS are associated with the vacuolar
RT membrane.";
RL J. Biol. Chem. 267:8021-8029(1992).
RN [6]
RP SIMILARITY TO ARGE/DAPE/ACY1/CPG2/YSCS FAMILY.
RX PubMed=8188249; DOI=10.1006/geno.1994.1018;
RA Henikoff S., Henikoff J.G.;
RT "Protein family classification based on searching a database of blocks.";
RL Genomics 19:97-107(1994).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=11566881; DOI=10.1093/emboj/20.18.5176;
RA Reggiori F., Pelham H.R.B.;
RT "Sorting of proteins into multivesicular bodies: ubiquitin-dependent and
RT -independent targeting.";
RL EMBO J. 20:5176-5186(2001).
RN [8]
RP UBIQUITINATION BY TUL1.
RX PubMed=11788821; DOI=10.1038/ncb743;
RA Reggiori F., Pelham H.R.B.;
RT "A transmembrane ubiquitin ligase required to sort membrane proteins into
RT multivesicular bodies.";
RL Nat. Cell Biol. 4:117-123(2002).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-8, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Necessary for use of certain peptides as sole nitrogen
CC source. May also cleave intracellularly generated peptides to recycle
CC amino acids for protein synthesis.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of a C-terminal amino acid from a peptide in which
CC glycine is the penultimate amino acid, e.g. Z-Gly-|-Leu.;
CC EC=3.4.17.4;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: yscS is synthesized as one polypeptide chain precursor which
CC after carbohydrate modification in the secretory pathway yields two
CC active precursor molecules. The proteolytically unprocessed forms are
CC associated with the membrane, whereas the mature forms of the enzyme
CC are soluble.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:11566881,
CC ECO:0000269|PubMed:1569061}; Single-pass membrane protein
CC {ECO:0000269|PubMed:11566881, ECO:0000269|PubMed:1569061}.
CC Note=Lysosome-like vacuoles.
CC -!- DOMAIN: The transmembrane domain contains polar residues that mediate
CC the recognition by TUL1.
CC -!- PTM: Glycosylated.
CC -!- PTM: Ubiquitinated. Ubiquitination mediates sorting into internal
CC vesicles in late endosomes. TUL1 is required for ubiquitination.
CC {ECO:0000269|PubMed:11788821}.
CC -!- MISCELLANEOUS: Present with 721 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR EMBL; X57316; CAA40571.1; -; Genomic_DNA.
DR EMBL; X63068; CAA44790.1; -; Genomic_DNA.
DR EMBL; Z49447; CAA89467.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08632.1; -; Genomic_DNA.
DR PIR; S16693; S16693.
DR RefSeq; NP_012363.1; NM_001181605.1.
DR AlphaFoldDB; P27614; -.
DR SMR; P27614; -.
DR BioGRID; 33588; 69.
DR DIP; DIP-5566N; -.
DR IntAct; P27614; 4.
DR MINT; P27614; -.
DR STRING; 4932.YJL172W; -.
DR MEROPS; M20.002; -.
DR iPTMnet; P27614; -.
DR MaxQB; P27614; -.
DR PaxDb; P27614; -.
DR PRIDE; P27614; -.
DR DNASU; 853267; -.
DR EnsemblFungi; YJL172W_mRNA; YJL172W; YJL172W.
DR GeneID; 853267; -.
DR KEGG; sce:YJL172W; -.
DR SGD; S000003708; CPS1.
DR VEuPathDB; FungiDB:YJL172W; -.
DR eggNOG; KOG2275; Eukaryota.
DR HOGENOM; CLU_021802_11_0_1; -.
DR InParanoid; P27614; -.
DR OMA; NYRVALH; -.
DR BioCyc; MetaCyc:YJL172W-MON; -.
DR BioCyc; YEAST:YJL172W-MON; -.
DR Reactome; R-SCE-9673163; Oleoyl-phe metabolism.
DR PRO; PR:P27614; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P27614; protein.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0000328; C:fungal-type vacuole lumen; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005775; C:vacuolar lumen; IDA:CAFA.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004180; F:carboxypeptidase activity; IMP:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IMP:SGD.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IMP:SGD.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR017141; Pept_M20_carboxypep.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037217; Carboxypeptidase_S; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Glycoprotein; Hydrolase; Isopeptide bond; Membrane;
KW Metal-binding; Protease; Reference proteome; Transmembrane;
KW Transmembrane helix; Ubl conjugation; Vacuole; Zinc.
FT CHAIN 1..576
FT /note="Carboxypeptidase S"
FT /id="PRO_0000185271"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..576
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 44..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 170
FT /evidence="ECO:0000250"
FT ACT_SITE 239
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 547
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 8
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 387
FT /note="S -> T (in Ref. 2; CAA40571)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 576 AA; 64597 MW; 5CBB536D421B5F70 CRC64;
MIALPVEKAP RKSLWQRHRA FISGIVALII IGTFFLTSGL HPAPPHEAKR PHHGKGPMHS
PKCEKIEPLS PSFKHSVDTI LHDPAFRNSS IEKLSNAVRI PTVVQDKNPN PADDPDFYKH
FYELHDYFEK TFPNIHKHLK LEKVNELGLL YTWEGSDPDL KPLLLMAHQD VVPVNNETLS
SWKFPPFSGH YDPETDFVWG RGSNDCKNLL IAEFEAIEQL LIDGFKPNRT IVMSLGFDEE
ASGTLGAASL ASFLHERYGD DGIYSIIDEG EGIMEVDKDV FVATPINAEK GYVDFEVSIL
GHGGHSSVPP DHTTIGIASE LITEFEANPF DYEFEFDNPI YGLLTCAAEH SKSLSKDVKK
TILGAPFCPR RKDKLVEYIS NQSHLRSLIR TTQAVDIING GVKANALPET TRFLINHRIN
LHSSVAEVFE RNIEYAKKIA EKYGYGLSKN GDDYIIPETE LGHIDITLLR ELEPAPLSPS
SGPVWDILAG TIQDVFENGV LQNNEEFYVT TGLFSGNTDT KYYWNLSKNI YRFVGSIIDI
DLLKTLHSVN EHVDVPGHLS AIAFVYEYIV NVNEYA
