CPYI_YEAST
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 03-AUG-2022, entry version 184.
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; 91.
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; P14306; -.
DR PRIDE; P14306; -.
DR TopDownProteomics; P14306; -.
DR EnsemblFungi; YLR178C_mRNA; YLR178C; YLR178C.
DR GeneID; 850875; -.
DR KEGG; sce:YLR178C; -.
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; VGVNWML; -.
DR BioCyc; YEAST:G3O-32303-MON; -.
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; -; 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; PTHR11362; 1.
DR Pfam; PF01161; PBP; 1.
DR SUPFAM; SSF49777; SSF49777; 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
