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Carboxypeptidase S (EC 3.4.17.4) (GLY-X carboxypeptidase) (YSCS)

 CBPS_YEAST              Reviewed;         576 AA.
P27614; D6VW16;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 2.
05-DEC-2018, entry version 165.
RecName: Full=Carboxypeptidase S;
EC=3.4.17.4;
AltName: Full=GLY-X carboxypeptidase;
AltName: Full=YSCS;
Name=CPS1; Synonyms=CPS; OrderedLocusNames=YJL172W; ORFNames=J0510;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=2026161; DOI=10.1111/j.1432-1033.1991.tb15924.x;
Spormann D.O., Heim J., Wolf D.H.;
"Carboxypeptidase yscS: gene structure and function of the vacuolar
enzyme.";
Eur. J. Biochem. 197:399-405(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204510 / AB320;
PubMed=1709881; DOI=10.1016/0014-5793(91)80546-F;
Bordallo J., Bordallo C., Gascon S., Suarez-Rendueles P.;
"Molecular cloning and sequencing of genomic DNA encoding yeast
vacuolar carboxypeptidase yscS.";
FEBS Lett. 283:27-32(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8641269;
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.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
X.";
EMBO J. 15:2031-2049(1996).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
SUBCELLULAR LOCATION.
PubMed=1569061;
Spormann D.O., Heim J., Wolf D.H.;
"Biogenesis of the yeast vacuole (lysosome). The precursor forms of
the soluble hydrolase carboxypeptidase yscS are associated with the
vacuolar membrane.";
J. Biol. Chem. 267:8021-8029(1992).
[6]
SIMILARITY TO ARGE/DAPE/ACY1/CPG2/YSCS FAMILY.
PubMed=8188249; DOI=10.1006/geno.1994.1018;
Henikoff S., Henikoff J.G.;
"Protein family classification based on searching a database of
blocks.";
Genomics 19:97-107(1994).
[7]
SUBCELLULAR LOCATION.
PubMed=11566881; DOI=10.1093/emboj/20.18.5176;
Reggiori F., Pelham H.R.B.;
"Sorting of proteins into multivesicular bodies: ubiquitin-dependent
and -independent targeting.";
EMBO J. 20:5176-5186(2001).
[8]
UBIQUITINATION BY TUL1.
PubMed=11788821; DOI=10.1038/ncb743;
Reggiori F., Pelham H.R.B.;
"A transmembrane ubiquitin ligase required to sort membrane proteins
into multivesicular bodies.";
Nat. Cell Biol. 4:117-123(2002).
[9]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[11]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-8, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
-!- 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:
Reaction=Release of a C-terminal amino acid from a peptide in
which glycine is the penultimate amino acid, e.g. Z-Gly-|-Leu.;
EC=3.4.17.4;
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
-!- SUBUNIT: 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
{ECO:0000269|PubMed:11566881, ECO:0000269|PubMed:1569061}; Single-
pass membrane protein {ECO:0000269|PubMed:11566881,
ECO:0000269|PubMed:1569061}. Note=Lysosome-like vacuoles.
-!- DOMAIN: The transmembrane domain contains polar residues that
mediate the recognition by TUL1.
-!- PTM: Glycosylated.
-!- PTM: Ubiquitinated. Ubiquitination mediates sorting into internal
vesicles in late endosomes. TUL1 is required for ubiquitination.
{ECO:0000269|PubMed:11788821}.
-!- MISCELLANEOUS: Present with 721 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X57316; CAA40571.1; -; Genomic_DNA.
EMBL; X63068; CAA44790.1; -; Genomic_DNA.
EMBL; Z49447; CAA89467.1; -; Genomic_DNA.
EMBL; BK006943; DAA08632.1; -; Genomic_DNA.
PIR; S16693; S16693.
RefSeq; NP_012363.1; NM_001181605.1.
ProteinModelPortal; P27614; -.
SMR; P27614; -.
BioGrid; 33588; 64.
DIP; DIP-5566N; -.
IntAct; P27614; 4.
MINT; P27614; -.
STRING; 4932.YJL172W; -.
MEROPS; M20.002; -.
iPTMnet; P27614; -.
MaxQB; P27614; -.
PaxDb; P27614; -.
PRIDE; P27614; -.
EnsemblFungi; YJL172W_mRNA; YJL172W_mRNA; YJL172W.
GeneID; 853267; -.
KEGG; sce:YJL172W; -.
SGD; S000003708; CPS1.
HOGENOM; HOG000194592; -.
InParanoid; P27614; -.
KO; K01293; -.
OMA; PGICIGN; -.
OrthoDB; EOG092C13PF; -.
BioCyc; MetaCyc:YJL172W-MONOMER; -.
BioCyc; YEAST:YJL172W-MONOMER; -.
Reactome; R-SCE-5423646; Aflatoxin activation and detoxification.
PRO; PR:P27614; -.
Proteomes; UP000002311; Chromosome X.
GO; GO:0000328; C:fungal-type vacuole lumen; IDA:SGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005775; C:vacuolar lumen; IDA:CAFA.
GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
GO; GO:0004180; F:carboxypeptidase activity; IMP:SGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
GO; GO:0006807; P:nitrogen compound metabolic process; IMP:SGD.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IMP:SGD.
InterPro; IPR001261; ArgE/DapE_CS.
InterPro; IPR036264; Bact_exopeptidase_dim_dom.
InterPro; IPR017141; Pept_M20_carboxypep.
InterPro; IPR002933; Peptidase_M20.
InterPro; IPR011650; Peptidase_M20_dimer.
Pfam; PF07687; M20_dimer; 1.
Pfam; PF01546; Peptidase_M20; 1.
PIRSF; PIRSF037217; Carboxypeptidase_S; 1.
SUPFAM; SSF55031; SSF55031; 1.
PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
1: Evidence at protein level;
Carboxypeptidase; Complete proteome; Glycoprotein; Hydrolase;
Isopeptide bond; Membrane; Metal-binding; Protease;
Reference proteome; Transmembrane; Transmembrane helix;
Ubl conjugation; Vacuole; Zinc.
CHAIN 1 576 Carboxypeptidase S.
/FTId=PRO_0000185271.
TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.
TRANSMEM 20 40 Helical. {ECO:0000255}.
TOPO_DOM 41 576 Lumenal. {ECO:0000255}.
ACT_SITE 170 170 {ECO:0000250}.
ACT_SITE 239 239 Proton acceptor. {ECO:0000250}.
METAL 168 168 Zinc 2. {ECO:0000250}.
METAL 205 205 Zinc 1. {ECO:0000250}.
METAL 205 205 Zinc 2. {ECO:0000250}.
METAL 240 240 Zinc 1. {ECO:0000250}.
METAL 268 268 Zinc 2. {ECO:0000250}.
METAL 547 547 Zinc 1. {ECO:0000250}.
CARBOHYD 88 88 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 176 176 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 228 228 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 381 381 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 525 525 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CROSSLNK 8 8 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CONFLICT 387 387 S -> T (in Ref. 2; CAA40571).
{ECO:0000305}.
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


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