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Protein

Profilin

Gene

PFY1

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

Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.

GO - Molecular functioni

  • actin monomer binding Source: SGD
  • phosphatidylinositol-4,5-bisphosphate binding Source: SGD
  • proline-rich region binding Source: SGD

GO - Biological processi

  • intracellular transport Source: SGD
  • positive regulation of formin-nucleated actin cable assembly Source: SGD
  • sequestering of actin monomers Source: SGD
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33649-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Profilin
Gene namesi
Name:PFY1
Synonyms:PFY, PRF1
Ordered Locus Names:YOR122C
ORF Names:O3275, YOR3275C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR122C.
SGDiS000005648. PFY1.

Subcellular locationi

GO - Cellular componenti

  • cytoskeleton Source: UniProtKB-SubCell
  • cytosol Source: SGD
  • extrinsic component of plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 126126ProfilinPRO_0000199608Add
BLAST

Proteomic databases

MaxQBiP07274.
PeptideAtlasiP07274.

PTM databases

iPTMnetiP07274.

Interactioni

Subunit structurei

Occurs in many kinds of cells as a complex with monomeric actin in a 1:1 ratio.

Binary interactionsi

WithEntry#Exp.IntActNotes
Bin1Q9VEX93EBI-13892,EBI-129424From a different organism.

GO - Molecular functioni

  • actin monomer binding Source: SGD
  • proline-rich region binding Source: SGD

Protein-protein interaction databases

BioGridi34517. 177 interactions.
DIPiDIP-46N.
IntActiP07274. 4 interactions.
MINTiMINT-575006.

Structurei

Secondary structure

1
126
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1210Combined sources
Beta strandi17 – 237Combined sources
Beta strandi29 – 346Combined sources
Helixi40 – 4910Combined sources
Helixi54 – 596Combined sources
Beta strandi61 – 633Combined sources
Beta strandi66 – 738Combined sources
Beta strandi75 – 828Combined sources
Beta strandi85 – 917Combined sources
Beta strandi93 – 1019Combined sources
Helixi107 – 12317Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K0KX-ray2.35A2-126[»]
1YPRX-ray2.30A/B2-126[»]
ProteinModelPortaliP07274.
SMRiP07274. Positions 2-126.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07274.

Family & Domainsi

Sequence similaritiesi

Belongs to the profilin family.Curated

Phylogenomic databases

GeneTreeiENSGT00730000112841.
HOGENOMiHOG000171591.
InParanoidiP07274.
KOiK05759.
OMAiSAFPKFK.
OrthoDBiEOG77T1H1.

Family and domain databases

InterProiIPR005455. PFN.
IPR027310. Profilin_CS.
[Graphical view]
PANTHERiPTHR11604. PTHR11604. 1 hit.
PfamiPF00235. Profilin. 1 hit.
[Graphical view]
PRINTSiPR00392. PROFILIN.
PR01640. PROFILINPLNT.
SMARTiSM00392. PROF. 1 hit.
[Graphical view]
SUPFAMiSSF55770. SSF55770. 1 hit.
PROSITEiPS00414. PROFILIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07274-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSWQAYTDNL IGTGKVDKAV IYSRAGDAVW ATSGGLSLQP NEIGEIVQGF
60 70 80 90 100
DNPAGLQSNG LHIQGQKFML LRADDRSIYG RHDAEGVVCV RTKQTVIIAH
110 120
YPPTVQAGEA TKIVEQLADY LIGVQY
Length:126
Mass (Da):13,677
Last modified:November 1, 1990 - v2
Checksum:i2485E413AB30DEAD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23369 Genomic DNA. Translation: AAA34861.1.
Y00469 mRNA. Translation: CAA68532.1.
X90518 Genomic DNA. Translation: CAA62128.1.
X94335 Genomic DNA. Translation: CAA64041.1.
Z75030 Genomic DNA. Translation: CAA99321.1.
BK006948 Genomic DNA. Translation: DAA10896.1.
PIRiA31360.
RefSeqiNP_014765.3. NM_001183541.3.

Genome annotation databases

EnsemblFungiiYOR122C; YOR122C; YOR122C.
GeneIDi854289.
KEGGisce:YOR122C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23369 Genomic DNA. Translation: AAA34861.1.
Y00469 mRNA. Translation: CAA68532.1.
X90518 Genomic DNA. Translation: CAA62128.1.
X94335 Genomic DNA. Translation: CAA64041.1.
Z75030 Genomic DNA. Translation: CAA99321.1.
BK006948 Genomic DNA. Translation: DAA10896.1.
PIRiA31360.
RefSeqiNP_014765.3. NM_001183541.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K0KX-ray2.35A2-126[»]
1YPRX-ray2.30A/B2-126[»]
ProteinModelPortaliP07274.
SMRiP07274. Positions 2-126.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34517. 177 interactions.
DIPiDIP-46N.
IntActiP07274. 4 interactions.
MINTiMINT-575006.

PTM databases

iPTMnetiP07274.

Proteomic databases

MaxQBiP07274.
PeptideAtlasiP07274.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR122C; YOR122C; YOR122C.
GeneIDi854289.
KEGGisce:YOR122C.

Organism-specific databases

EuPathDBiFungiDB:YOR122C.
SGDiS000005648. PFY1.

Phylogenomic databases

GeneTreeiENSGT00730000112841.
HOGENOMiHOG000171591.
InParanoidiP07274.
KOiK05759.
OMAiSAFPKFK.
OrthoDBiEOG77T1H1.

Enzyme and pathway databases

BioCyciYEAST:G3O-33649-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP07274.
NextBioi976272.
PROiP07274.

Family and domain databases

InterProiIPR005455. PFN.
IPR027310. Profilin_CS.
[Graphical view]
PANTHERiPTHR11604. PTHR11604. 1 hit.
PfamiPF00235. Profilin. 1 hit.
[Graphical view]
PRINTSiPR00392. PROFILIN.
PR01640. PROFILINPLNT.
SMARTiSM00392. PROF. 1 hit.
[Graphical view]
SUPFAMiSSF55770. SSF55770. 1 hit.
PROSITEiPS00414. PROFILIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The intron-containing gene for yeast profilin (PFY) encodes a vital function."
    Magdolen V., Oechsner U., Mueller G., Bandlow W.
    Mol. Cell. Biol. 8:5108-5115(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The cDNA and deduced amino acid sequence of profilin from Saccharomyces cerevisiae."
    Oechsner U., Magdolen V., Bandlow W.
    Nucleic Acids Res. 15:9078-9078(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ATCC 26787 / X2180-1B.
  3. "Sequencing and analysis of 51 kb on the right arm of chromosome XV from Saccharomyces cerevisiae reveals 30 open reading frames."
    Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C., Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.
    Yeast 12:281-288(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  7. "Structure determination and characterization of Saccharomyces cerevisiae profilin."
    Eads J.C., Mahoney N.M., Vorobiev S., Bresnick A.R., Wen K.K., Rubenstein P.A., Haarer B.K., Almo S.C.
    Biochemistry 37:11171-11181(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Entry informationi

Entry nameiPROF_YEAST
AccessioniPrimary (citable) accession number: P07274
Secondary accession number(s): D6W2I0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 1, 1990
Last modified: May 11, 2016
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

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 one 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.