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Protein

Carboxypeptidase Y inhibitor

Gene

TFS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Specific and potent inhibitor of carboxypeptidase Y.1 Publication

GO - Molecular functioni

  1. lipid binding Source: SGD
  2. peptidase inhibitor activity Source: SGD
  3. phospholipid binding Source: SGD
  4. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

GO - Biological processi

  1. regulation of proteolysis Source: SGD
  2. regulation of Ras protein signal transduction Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Enzyme and pathway databases

BioCyciYEAST:G3O-32303-MONOMER.

Protein family/group databases

MEROPSiI51.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxypeptidase Y inhibitor
Short name:
CPY inhibitor
Alternative name(s):
CDC25 suppressor 1
I(C)
Ic
Protein DKA1
Protein NSP1
Gene namesi
Name:TFS1
Synonyms:DKA1, NSP1
Ordered Locus Names:YLR178C
ORF Names:L9470.19
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XII

Organism-specific databases

CYGDiYLR178c.
SGDiS000004168. TFS1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. fungal-type vacuole lumen Source: SGD
  3. fungal-type vacuole membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 219219Carboxypeptidase Y inhibitorPRO_0000204753Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP14306.
PaxDbiP14306.
PeptideAtlasiP14306.

Expressioni

Gene expression databases

GenevestigatoriP14306.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi31449. 29 interactions.
DIPiDIP-669N.
IntActiP14306. 3 interactions.
MINTiMINT-2786931.
STRINGi4932.YLR178C.

Structurei

Secondary structure

1
219
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 43Combined sources
Helixi7 – 1711Combined sources
Helixi20 – 234Combined sources
Beta strandi33 – 419Combined sources
Beta strandi44 – 463Combined sources
Helixi54 – 574Combined sources
Beta strandi62 – 687Combined sources
Beta strandi89 – 9911Combined sources
Beta strandi108 – 11912Combined sources
Beta strandi133 – 1397Combined sources
Beta strandi144 – 1474Combined sources
Beta strandi161 – 1699Combined sources
Helixi176 – 1783Combined sources
Helixi187 – 1893Combined sources
Beta strandi192 – 1943Combined sources
Helixi197 – 2026Combined sources
Turni203 – 2053Combined sources
Beta strandi207 – 21610Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WPXX-ray2.70B1-219[»]
ProteinModelPortaliP14306.
SMRiP14306. Positions 1-219.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14306.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1881.
GeneTreeiENSGT00740000116453.
HOGENOMiHOG000237655.
InParanoidiP14306.
KOiK06910.
OMAiAPSNTDH.
OrthoDBiEOG70612X.

Family and domain databases

Gene3Di3.90.280.10. 1 hit.
InterProiIPR001858. Phosphotidylethanolamine-bd_CS.
IPR008914. PtdEtn-bd_prot_PEBP.
[Graphical view]
PfamiPF01161. PBP. 1 hit.
[Graphical view]
SUPFAMiSSF49777. SSF49777. 1 hit.
PROSITEiPS01220. PBP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P14306-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNQAIDFAQA SIDSYKKHGI LEDVIHDTSF QPSGILAVEY SSSAPVAMGN
60 70 80 90 100
TLPTEKARSK PQFQFTFNKQ MQKSVPQANA YVPQDDDLFT LVMTDPDAPS
110 120 130 140 150
KTDHKWSEFC HLVECDLKLL NEATHETSGA TEFFASEFNT KGSNTLIEYM
160 170 180 190 200
GPAPPKGSGP HRYVFLLYKQ PKGVDSSKFS KIKDRPNWGY GTPATGVGKW
210
AKENNLQLVA SNFFYAETK
Length:219
Mass (Da):24,357
Last modified:July 1, 1993 - v2
Checksum:i37D4FEC17677A573
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 561K → N in CAA44015 (PubMed:1745232).Curated
Sequence conflicti165 – 1651F → L in CAA33456 (PubMed:2693892).Curated
Sequence conflicti211 – 2199SNFFYAETK → VQFLLCGNEIGIYIYICICI YFLDFSAFHLTFYYFCFIYV FVTNGQMFVGTNVYVKQNT (PubMed:2693892).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15409 Genomic DNA. Translation: CAA33456.1.
X62105 Genomic DNA. Translation: CAA44015.1.
U17246 Genomic DNA. Translation: AAB67471.1.
BK006945 Genomic DNA. Translation: DAA09498.1.
PIRiS18843.
RefSeqiNP_013279.1. NM_001182065.1.

Genome annotation databases

EnsemblFungiiYLR178C; YLR178C; YLR178C.
GeneIDi850875.
KEGGisce:YLR178C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15409 Genomic DNA. Translation: CAA33456.1.
X62105 Genomic DNA. Translation: CAA44015.1.
U17246 Genomic DNA. Translation: AAB67471.1.
BK006945 Genomic DNA. Translation: DAA09498.1.
PIRiS18843.
RefSeqiNP_013279.1. NM_001182065.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WPXX-ray2.70B1-219[»]
ProteinModelPortaliP14306.
SMRiP14306. Positions 1-219.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31449. 29 interactions.
DIPiDIP-669N.
IntActiP14306. 3 interactions.
MINTiMINT-2786931.
STRINGi4932.YLR178C.

Protein family/group databases

MEROPSiI51.001.

Proteomic databases

MaxQBiP14306.
PaxDbiP14306.
PeptideAtlasiP14306.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR178C; YLR178C; YLR178C.
GeneIDi850875.
KEGGisce:YLR178C.

Organism-specific databases

CYGDiYLR178c.
SGDiS000004168. TFS1.

Phylogenomic databases

eggNOGiCOG1881.
GeneTreeiENSGT00740000116453.
HOGENOMiHOG000237655.
InParanoidiP14306.
KOiK06910.
OMAiAPSNTDH.
OrthoDBiEOG70612X.

Enzyme and pathway databases

BioCyciYEAST:G3O-32303-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP14306.
NextBioi967218.

Gene expression databases

GenevestigatoriP14306.

Family and domain databases

Gene3Di3.90.280.10. 1 hit.
InterProiIPR001858. Phosphotidylethanolamine-bd_CS.
IPR008914. PtdEtn-bd_prot_PEBP.
[Graphical view]
PfamiPF01161. PBP. 1 hit.
[Graphical view]
SUPFAMiSSF49777. SSF49777. 1 hit.
PROSITEiPS01220. PBP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of NSP1, a locus encoding a component of a CDC25-dependent, nutrient-responsive pathway in Saccharomyces cerevisiae."
    Tripp M.L., Bouchard R.A., Pinon R.
    Mol. Microbiol. 3:1319-1327(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: X241.
  2. "TFS1: a suppressor of cdc25 mutations in Saccharomyces cerevisiae."
    Robinson L.C., Tatchell K.
    Mol. Gen. Genet. 230:241-250(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "A high-affinity inhibitor of yeast carboxypeptidase Y is encoded by TFS1 and shows homology to a family of lipid binding proteins."
    Bruun A.W., Svendsen I., Sorensen S.O., Kielland-Brandt M.C., Winther J.R.
    Biochemistry 37:3351-3357(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Overexpression and functional characterization of a serine carboxypeptidase inhibitor (I(C)) from Saccharomyces cerevisiae."
    Mima J., Suzuki H., Takahashi M., Hayashi R.
    J. Biochem. 132:967-973(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, ACETYLATION AT MET-1.
  7. "N-terminal acetyl group is essential for the inhibitory function of carboxypeptidase Y inhibitor (I(C))."
    Mima J., Kondo T., Hayashi R.
    FEBS Lett. 532:207-210(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCPYI_YEAST
AccessioniPrimary (citable) accession number: P14306
Secondary accession number(s): D6VYI2, P30312
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: July 1, 1993
Last modified: January 7, 2015
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1030 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.