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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.
13-FEB-2019, entry version 167.
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}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
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; -.
EuPathDB; FungiDB:YJL172W; -.
SGD; S000003708; CPS1.
HOGENOM; HOG000194592; -.
InParanoid; P27614; -.
KO; K01293; -.
OMA; PGICIGN; -.
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:0000324; C:fungal-type vacuole; HDA:SGD.
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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[CPQ LCH1 PGCP] Carboxypeptidase Q (EC 3.4.17.-) (Lysosomal dipeptidase) (Plasma glutamate carboxypeptidase)
[CTSA PPGB] Lysosomal protective protein (EC 3.4.16.5) (Carboxypeptidase C) (Carboxypeptidase L) (Cathepsin A) (Protective protein cathepsin A) (PPCA) (Protective protein for beta-galactosidase) [Cleaved into: Lysosomal protective protein 32 kDa chain; Lysosomal protective protein 20 kDa chain]
[pyrG A6592_02570 A8M42_16405 A9R57_06965 AC067_22330 AC789_1c31020 ACN002_2797 ACN77_07080 ACN81_20385 ACU57_24415 ACU90_23015 AJ318_22735 AKG99_03555 AM270_00945 AM446_06950 AM464_05605 AM465_10605 AML07_12460 AML35_05300 APT94_17890 APU18_18535 APZ14_09290 ARC77_10140 AU473_08010 AUQ13_17535 AUS26_15660 AW059_10675 AW106_00665 AWP75_20610 AZZ83_003241 B1K96_20050 B7C53_10055 B9M99_21725 B9N33_09475 B9T59_19685 BB545_13920 BE963_03670 BEN53_16995 BET08_07180 BH694_13410 BHF46_05050 BHS81_16640 BHS87_15735 BIQ87_15835 BIU72_09520 BIZ41_16885 BJJ90_05265 BK248_12970 BK292_23205 BK334_11935 BK373_15870 BK375_10085 BK383_11680 BK400_05820 BMT49_17330 BMT53_21250 BMT91_11105 BN17_26661 BTQ04_11510 BTQ06_23845 BUE81_06975 BVL39_12970 BW690_04975 BWP17_05185 BXT93_24405 BZL31_00820 BZL69_02125 C1I57_04860 C2M16_17770 C2U48_20025 C3K24_08940 C4J69_11655 C4K41_05275 C4M78_00835 C5715_23540 C5N07_06155 C5P01_05005 C5P43_15935 C5P44_09340 C6669_14670 C6986_17750 C6B13_03370 C7235_05745 C7B02_19400 C7B06_11630 C7B07_14530 C7B08_01430 C9E25_03325 CA593_12975 CCZ14_04445 CCZ17_10850 CDL37_13440 CG691_07365 CG692_07005 CG705_05530 CG706_07860 CIJ94_12220 COD30_01795 COD46_07095 CR538_05495 CR539_18815 CRE06_03485 CRM83_26360 CSB64_15850 CT143_09630 CT146_00680 CV83915_03339 CVH05_06295 CWM24_00790 CWS33_03125 CXB56_08765 D0X26_06660 D1900_12730 D2183_19100 D2F89_14380 D3I61_16000 DD762_13665 DIV22_29760 DIV25_29790 DL545_05995 DL800_20505 DNQ41_18960 DNR41_08670 DQE83_04685 DS732_20695 DS966_06010 DTL43_09355 DTL84_00105 DTL90_02675 DTM10_03745 DTM25_22630 DTM27_13675 DTM45_13530 EC1094V2_904 EC3234A_48c00890 EC95NR1_02021 ECONIH1_15890 ECs3640 EL75_0914 EL79_0915 EL80_0918 ERS085365_02427 ERS085366_03042 ERS085374_03279 ERS085386_03410 ERS085416_02898 ERS139211_02072 ERS150873_02003 ERS150876_01467 FORC28_1110 GJ11_18025 HMPREF3040_01161 HW43_18180 JD73_16335 MJ49_17095 MS6198_30910 MS8345_02965 NCTC10082_03473 NCTC10090_04050 NCTC10418_01701 NCTC10764_00296 NCTC10766_00690 NCTC10767_02309 NCTC11022_02860 NCTC11112_00121 NCTC11181_03277 NCTC12950_01251 NCTC13125_04353 NCTC13127_01436 NCTC13462_04807 NCTC13846_01212 NCTC7152_00995 NCTC7927_01209 NCTC8500_01090 NCTC8960_03783 NCTC9007_03892 NCTC9010_01168 NCTC9036_01135 NCTC9037_01243 NCTC9045_01221 NCTC9050_04166 NCTC9058_00847 NCTC9062_02131 NCTC9075_01630 NCTC9077_01409 NCTC9081_05851 NCTC9117_01609 NCTC9119_01271 NCTC9434_01004 NCTC9706_03296 NCTC9775_04845 NCTC9777_02704 NCTC9969_01292 PU06_02080 RG28_07675 RK56_023165 SAMEA3472033_01264 SAMEA3472044_02272 SAMEA3472047_00339 SAMEA3472056_05455 SAMEA3472067_02540 SAMEA3472070_01673 SAMEA3472080_03155 SAMEA3472090_00131 SAMEA3472108_00527 SAMEA3472110_03462 SAMEA3472112_03722 SAMEA3472114_02432 SAMEA3472147_03296 SAMEA3484427_03298 SAMEA3484429_03415 SAMEA3484433_01660 SAMEA3484434_01581 SAMEA3485101_02257 SAMEA3485113_02257 SAMEA3752372_03639 SAMEA3752557_03040 SAMEA3752559_02995 SAMEA3752620_01282 SAMEA3753064_02287 SAMEA3753097_02219 SAMEA3753106_03183 SAMEA3753164_01192 SAMEA3753290_02847 SAMEA3753300_01107 SAMEA3753391_02580 SAMEA3753397_04005 SK85_03024 SY51_15605 UC41_20365 UN91_03645 WM48_14990 WQ89_10170 WR15_06090 YDC107_1339] CTP synthase (EC 6.3.4.2) (Cytidine 5'-triphosphate synthase) (Cytidine triphosphate synthetase) (CTP synthetase) (CTPS) (UTP--ammonia ligase)
[CBP2] Serine carboxypeptidase 2 (EC 3.4.16.6) (CPDW-II) (CP-WII) (Carboxypeptidase D) (Serine carboxypeptidase II) [Cleaved into: Serine carboxypeptidase 2 chain A (Serine carboxypeptidase II chain A); Serine carboxypeptidase 2 chain B (Serine carboxypeptidase II chain B)]
[egl-21 F01D4.4] Carboxypeptidase E (CPE) (EC 3.4.17.10) (Egg-laying defective protein 21)
[CPM] Carboxypeptidase M (CPM) (EC 3.4.17.12)
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Non-structural protein 2A-alpha (NS2A-alpha); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]

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