ID   CPYI_YEAST              Reviewed;         219 AA.
AC   P14306; D6VYI2; P30312;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 2.
DT   27-MAR-2024, entry version 191.
DE   RecName: Full=Carboxypeptidase Y inhibitor;
DE            Short=CPY inhibitor;
DE   AltName: Full=CDC25 suppressor 1;
DE   AltName: Full=I(C);
DE   AltName: Full=Ic;
DE   AltName: Full=Protein DKA1;
DE   AltName: Full=Protein NSP1;
GN   Name=TFS1; Synonyms=DKA1, NSP1; OrderedLocusNames=YLR178C;
GN   ORFNames=L9470.19;
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=X241;
RX   PubMed=2693892; DOI=10.1111/j.1365-2958.1989.tb00113.x;
RA   Tripp M.L., Bouchard R.A., Pinon R.;
RT   "Cloning and characterization of NSP1, a locus encoding a component of a
RT   CDC25-dependent, nutrient-responsive pathway in Saccharomyces cerevisiae.";
RL   Mol. Microbiol. 3:1319-1327(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1745232; DOI=10.1007/bf00290674;
RA   Robinson L.C., Tatchell K.;
RT   "TFS1: a suppressor of cdc25 mutations in Saccharomyces cerevisiae.";
RL   Mol. Gen. Genet. 230:241-250(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
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   FUNCTION.
RX   PubMed=9521655; DOI=10.1021/bi971286w;
RA   Bruun A.W., Svendsen I., Sorensen S.O., Kielland-Brandt M.C., Winther J.R.;
RT   "A high-affinity inhibitor of yeast carboxypeptidase Y is encoded by TFS1
RT   and shows homology to a family of lipid binding proteins.";
RL   Biochemistry 37:3351-3357(1998).
RN   [6]
RP   CHARACTERIZATION, AND ACETYLATION AT MET-1.
RX   PubMed=12473200; DOI=10.1093/oxfordjournals.jbchem.a003311;
RA   Mima J., Suzuki H., Takahashi M., Hayashi R.;
RT   "Overexpression and functional characterization of a serine
RT   carboxypeptidase inhibitor (I(C)) from Saccharomyces cerevisiae.";
RL   J. Biochem. 132:967-973(2002).
RN   [7]
RP   CHARACTERIZATION.
RX   PubMed=12459491; DOI=10.1016/s0014-5793(02)03676-1;
RA   Mima J., Kondo T., Hayashi R.;
RT   "N-terminal acetyl group is essential for the inhibitory function of
RT   carboxypeptidase Y inhibitor (I(C)).";
RL   FEBS Lett. 532:207-210(2002).
RN   [8]
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   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: Specific and potent inhibitor of carboxypeptidase Y.
CC       {ECO:0000269|PubMed:9521655}.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: Present with 1030 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the phosphatidylethanolamine-binding protein
CC       family. {ECO:0000305}.
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DR   EMBL; X15409; CAA33456.1; -; Genomic_DNA.
DR   EMBL; X62105; CAA44015.1; -; Genomic_DNA.
DR   EMBL; U17246; AAB67471.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09498.1; -; Genomic_DNA.
DR   PIR; S18843; S18843.
DR   RefSeq; NP_013279.1; NM_001182065.1.
DR   PDB; 1WPX; X-ray; 2.70 A; B=1-219.
DR   PDBsum; 1WPX; -.
DR   AlphaFoldDB; P14306; -.
DR   SMR; P14306; -.
DR   BioGRID; 31449; 97.
DR   DIP; DIP-669N; -.
DR   IntAct; P14306; 3.
DR   MINT; P14306; -.
DR   STRING; 4932.YLR178C; -.
DR   MEROPS; I51.001; -.
DR   iPTMnet; P14306; -.
DR   MaxQB; P14306; -.
DR   PaxDb; 4932-YLR178C; -.
DR   PeptideAtlas; P14306; -.
DR   TopDownProteomics; P14306; -.
DR   EnsemblFungi; YLR178C_mRNA; YLR178C; YLR178C.
DR   GeneID; 850875; -.
DR   KEGG; sce:YLR178C; -.
DR   AGR; SGD:S000004168; -.
DR   SGD; S000004168; TFS1.
DR   VEuPathDB; FungiDB:YLR178C; -.
DR   eggNOG; KOG3346; Eukaryota.
DR   GeneTree; ENSGT00940000167139; -.
DR   HOGENOM; CLU_043994_3_1_1; -.
DR   InParanoid; P14306; -.
DR   OMA; VIDDFPP; -.
DR   OrthoDB; 3412953at2759; -.
DR   BioCyc; YEAST:G3O-32303-MONOMER; -.
DR   BioGRID-ORCS; 850875; 9 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P14306; -.
DR   PRO; PR:P14306; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P14306; Protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0000328; C:fungal-type vacuole lumen; IDA:SGD.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR   GO; GO:0030414; F:peptidase inhibitor activity; IDA:SGD.
DR   GO; GO:0005543; F:phospholipid binding; IDA:SGD.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0030162; P:regulation of proteolysis; IDA:SGD.
DR   GO; GO:0046578; P:regulation of Ras protein signal transduction; IMP:SGD.
DR   CDD; cd00866; PEBP_euk; 1.
DR   Gene3D; 3.90.280.10; PEBP-like; 1.
DR   InterPro; IPR008914; PEBP.
DR   InterPro; IPR036610; PEBP-like_sf.
DR   InterPro; IPR035810; PEBP_euk.
DR   InterPro; IPR001858; Phosphatidylethanolamine-bd_CS.
DR   PANTHER; PTHR11362:SF148; CARBOXYPEPTIDASE Y INHIBITOR; 1.
DR   PANTHER; PTHR11362; PHOSPHATIDYLETHANOLAMINE-BINDING PROTEIN; 1.
DR   Pfam; PF01161; PBP; 1.
DR   SUPFAM; SSF49777; PEBP-like; 1.
DR   PROSITE; PS01220; PBP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Protease inhibitor;
KW   Reference proteome; Serine protease inhibitor.
FT   CHAIN           1..219
FT                   /note="Carboxypeptidase Y inhibitor"
FT                   /id="PRO_0000204753"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|PubMed:12473200"
FT   CONFLICT        56
FT                   /note="K -> N (in Ref. 2; CAA44015)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        165
FT                   /note="F -> L (in Ref. 1; CAA33456)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        211..219
FT                   /note="SNFFYAETK -> VQFLLCGNEIGIYIYICICIYFLDFSAFHLTFYYFCFIY
FT                   VFVTNGQMFVGTNVYVKQNT (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   HELIX           2..4
FT                   /evidence="ECO:0007829|PDB:1WPX"
FT   HELIX           7..17
FT                   /evidence="ECO:0007829|PDB:1WPX"
FT   HELIX           20..23
FT                   /evidence="ECO:0007829|PDB:1WPX"
FT   STRAND          33..41
FT                   /evidence="ECO:0007829|PDB:1WPX"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:1WPX"
FT   HELIX           54..57
FT                   /evidence="ECO:0007829|PDB:1WPX"
FT   STRAND          62..68
FT                   /evidence="ECO:0007829|PDB:1WPX"
FT   STRAND          89..99
FT                   /evidence="ECO:0007829|PDB:1WPX"
FT   STRAND          108..119
FT                   /evidence="ECO:0007829|PDB:1WPX"
FT   STRAND          133..139
FT                   /evidence="ECO:0007829|PDB:1WPX"
FT   STRAND          144..147
FT                   /evidence="ECO:0007829|PDB:1WPX"
FT   STRAND          161..169
FT                   /evidence="ECO:0007829|PDB:1WPX"
FT   HELIX           176..178
FT                   /evidence="ECO:0007829|PDB:1WPX"
FT   HELIX           187..189
FT                   /evidence="ECO:0007829|PDB:1WPX"
FT   STRAND          192..194
FT                   /evidence="ECO:0007829|PDB:1WPX"
FT   HELIX           197..202
FT                   /evidence="ECO:0007829|PDB:1WPX"
FT   TURN            203..205
FT                   /evidence="ECO:0007829|PDB:1WPX"
FT   STRAND          207..216
FT                   /evidence="ECO:0007829|PDB:1WPX"
SQ   SEQUENCE   219 AA;  24357 MW;  37D4FEC17677A573 CRC64;
     MNQAIDFAQA SIDSYKKHGI LEDVIHDTSF QPSGILAVEY SSSAPVAMGN TLPTEKARSK
     PQFQFTFNKQ MQKSVPQANA YVPQDDDLFT LVMTDPDAPS KTDHKWSEFC HLVECDLKLL
     NEATHETSGA TEFFASEFNT KGSNTLIEYM GPAPPKGSGP HRYVFLLYKQ PKGVDSSKFS
     KIKDRPNWGY GTPATGVGKW AKENNLQLVA SNFFYAETK
//