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Protein

Profilin

Gene

cdc3

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: -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. In S.pombe, it is essential for cytokinesis.

GO - Molecular functioni

  • actin monomer binding Source: PomBase
  • guanyl-nucleotide exchange factor activity Source: PomBase

GO - Biological processi

  • actin cortical patch organization Source: PomBase
  • actin filament polymerization Source: PomBase
  • cytogamy Source: PomBase
  • mitotic actomyosin contractile ring assembly Source: PomBase
  • negative regulation of actin filament binding Source: PomBase
  • negative regulation of actin filament polymerization Source: PomBase
  • regulation of barbed-end actin filament capping Source: PomBase
  • sequestering of actin monomers Source: GO_Central

Keywordsi

Molecular functionActin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Profilin
Gene namesi
Name:cdc3
ORF Names:SPAC4A8.15c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC4A8.15c
PomBaseiSPAC4A8.15c cdc3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001996071 – 127ProfilinAdd BLAST127

Proteomic databases

MaxQBiP39825
PaxDbiP39825
PRIDEiP39825

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • actin monomer binding Source: PomBase
  • guanyl-nucleotide exchange factor activity Source: PomBase

Protein-protein interaction databases

BioGridi279944, 20 interactors
STRINGi4896.SPAC4A8.15c.1

Structurei

Secondary structure

1127
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 8Combined sources6
Turni9 – 11Combined sources3
Helixi12 – 14Combined sources3
Beta strandi19 – 24Combined sources6
Beta strandi30 – 33Combined sources4
Helixi41 – 52Combined sources12
Helixi56 – 60Combined sources5
Beta strandi62 – 64Combined sources3
Beta strandi67 – 74Combined sources8
Beta strandi76 – 83Combined sources8
Beta strandi86 – 92Combined sources7
Beta strandi94 – 102Combined sources9
Helixi108 – 125Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3D9YX-ray1.65A/B1-127[»]
3DAVX-ray2.20A/B1-127[»]
ProteinModelPortaliP39825
SMRiP39825
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39825

Family & Domainsi

Sequence similaritiesi

Belongs to the profilin family.Curated

Phylogenomic databases

HOGENOMiHOG000171591
InParanoidiP39825
KOiK05759
OMAiAGQKFFT
OrthoDBiEOG092C53JE
PhylomeDBiP39825

Family and domain databases

CDDicd00148 PROF, 1 hit
InterProiView protein in InterPro
IPR005455 PFN
IPR036140 PFN_sf
IPR027310 Profilin_CS
PANTHERiPTHR11604 PTHR11604, 1 hit
PfamiView protein in Pfam
PF00235 Profilin, 1 hit
PRINTSiPR00392 PROFILIN
PR01640 PROFILINPLNT
SMARTiView protein in SMART
SM00392 PROF, 1 hit
SUPFAMiSSF55770 SSF55770, 1 hit
PROSITEiView protein in PROSITE
PS00414 PROFILIN, 1 hit

Sequencei

Sequence statusi: Complete.

P39825-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSWQAYVDTS LLGTGKIDRA AIVSRAGDSV WAASAGFNLS PQEIQGLAAG
60 70 80 90 100
FQDPPSMFGT GIILAGQKYI TIRAEGRSIY GKLQKEGIIC VATKLCILVS
110 120
HYPETTLPGE AAKITEALAD YLVGVGY
Length:127
Mass (Da):13,411
Last modified:February 1, 1995 - v1
Checksum:i1D3BE221AAA73594
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z30648 Genomic DNA No translation available.
CU329670 Genomic DNA Translation: CAB38578.1
PIRiA53952
RefSeqiNP_593827.1, NM_001019256.2

Genome annotation databases

EnsemblFungiiSPAC4A8.15c.1; SPAC4A8.15c.1:pep; SPAC4A8.15c
GeneIDi2543526
KEGGispo:SPAC4A8.15c

Similar proteinsi

Entry informationi

Entry nameiPROF_SCHPO
AccessioniPrimary (citable) accession number: P39825
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: March 28, 2018
This is version 132 of the entry and version 1 of the sequence. See 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. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

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