PROF_SCHPO
ID PROF_SCHPO Reviewed; 127 AA.
AC P39825;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Profilin;
GN Name=cdc3; ORFNames=SPAC4A8.15c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=8207058; DOI=10.1083/jcb.125.6.1289;
RA Balasubramanian M.K., Hirani B.R., Burke J.D., Gould K.L.;
RT "The Schizosaccharomyces pombe cdc3+ gene encodes a profilin essential for
RT cytokinesis.";
RL J. Cell Biol. 125:1289-1301(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Binds to actin and affects the structure of the cytoskeleton.
CC At high concentrations, profilin prevents the polymerization of actin,
CC whereas it enhances it at low concentrations. By binding to PIP2, it
CC inhibits the formation of IP3 and DG. In S.pombe, it is essential for
CC cytokinesis.
CC -!- SUBUNIT: Occurs in many kinds of cells as a complex with monomeric
CC actin in a 1:1 ratio.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR EMBL; Z30648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU329670; CAB38578.1; -; Genomic_DNA.
DR PIR; A53952; A53952.
DR RefSeq; NP_593827.1; NM_001019256.2.
DR PDB; 3D9Y; X-ray; 1.65 A; A/B=1-127.
DR PDB; 3DAV; X-ray; 2.20 A; A/B=1-127.
DR PDBsum; 3D9Y; -.
DR PDBsum; 3DAV; -.
DR AlphaFoldDB; P39825; -.
DR SMR; P39825; -.
DR BioGRID; 279944; 25.
DR STRING; 4896.SPAC4A8.15c.1; -.
DR MaxQB; P39825; -.
DR PaxDb; P39825; -.
DR PRIDE; P39825; -.
DR EnsemblFungi; SPAC4A8.15c.1; SPAC4A8.15c.1:pep; SPAC4A8.15c.
DR GeneID; 2543526; -.
DR KEGG; spo:SPAC4A8.15c; -.
DR PomBase; SPAC4A8.15c; cdc3.
DR VEuPathDB; FungiDB:SPAC4A8.15c; -.
DR eggNOG; KOG1755; Eukaryota.
DR HOGENOM; CLU_120772_1_0_1; -.
DR InParanoid; P39825; -.
DR OMA; WAQSSGF; -.
DR PhylomeDB; P39825; -.
DR EvolutionaryTrace; P39825; -.
DR PRO; PR:P39825; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0030479; C:actin cortical patch; TAS:PomBase.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR GO; GO:0043332; C:mating projection tip; IDA:PomBase.
DR GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR GO; GO:0003785; F:actin monomer binding; IDA:PomBase.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:PomBase.
DR GO; GO:0044396; P:actin cortical patch organization; IMP:PomBase.
DR GO; GO:0030041; P:actin filament polymerization; IDA:PomBase.
DR GO; GO:1904670; P:actin filament polymerization involved in mitotic actomyosin contractile ring assembly; IMP:PomBase.
DR GO; GO:0000755; P:cytogamy; IMP:PomBase.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IMP:PomBase.
DR GO; GO:1904530; P:negative regulation of actin filament binding; IDA:PomBase.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IDA:PomBase.
DR GO; GO:2000812; P:regulation of barbed-end actin filament capping; IDA:PomBase.
DR GO; GO:0042989; P:sequestering of actin monomers; IBA:GO_Central.
DR CDD; cd00148; PROF; 1.
DR InterPro; IPR005455; PFN.
DR InterPro; IPR036140; PFN_sf.
DR InterPro; IPR027310; Profilin_CS.
DR PANTHER; PTHR11604; PTHR11604; 1.
DR Pfam; PF00235; Profilin; 1.
DR PRINTS; PR00392; PROFILIN.
DR PRINTS; PR01640; PROFILINPLNT.
DR SMART; SM00392; PROF; 1.
DR SUPFAM; SSF55770; SSF55770; 1.
DR PROSITE; PS00414; PROFILIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..127
FT /note="Profilin"
FT /id="PRO_0000199607"
FT HELIX 3..8
FT /evidence="ECO:0007829|PDB:3D9Y"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:3D9Y"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:3D9Y"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:3D9Y"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:3D9Y"
FT HELIX 41..52
FT /evidence="ECO:0007829|PDB:3D9Y"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:3D9Y"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:3D9Y"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:3D9Y"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:3D9Y"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:3D9Y"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:3D9Y"
FT HELIX 108..125
FT /evidence="ECO:0007829|PDB:3D9Y"
SQ SEQUENCE 127 AA; 13411 MW; 1D3BE221AAA73594 CRC64;
MSWQAYVDTS LLGTGKIDRA AIVSRAGDSV WAASAGFNLS PQEIQGLAAG FQDPPSMFGT
GIILAGQKYI TIRAEGRSIY GKLQKEGIIC VATKLCILVS HYPETTLPGE AAKITEALAD
YLVGVGY
