PROF_YEAST
ID PROF_YEAST Reviewed; 126 AA.
AC P07274; D6W2I0;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Profilin;
GN Name=PFY1; Synonyms=PFY, PRF1; OrderedLocusNames=YOR122C;
GN ORFNames=O3275, YOR3275C;
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].
RX PubMed=3072473; DOI=10.1128/mcb.8.12.5108-5115.1988;
RA Magdolen V., Oechsner U., Mueller G., Bandlow W.;
RT "The intron-containing gene for yeast profilin (PFY) encodes a vital
RT function.";
RL Mol. Cell. Biol. 8:5108-5115(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 26787 / X2180-1B;
RX PubMed=3317275; DOI=10.1093/nar/15.21.9078;
RA Oechsner U., Magdolen V., Bandlow W.;
RT "The cDNA and deduced amino acid sequence of profilin from Saccharomyces
RT cerevisiae.";
RL Nucleic Acids Res. 15:9078-9078(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8904341;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<281::aid-yea904>3.0.co;2-o;
RA Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C.,
RA Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.;
RT "Sequencing and analysis of 51 kb on the right arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 30 open reading frames.";
RL Yeast 12:281-288(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [6]
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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=9698363; DOI=10.1021/bi9720033;
RA Eads J.C., Mahoney N.M., Vorobiev S., Bresnick A.R., Wen K.K.,
RA Rubenstein P.A., Haarer B.K., Almo S.C.;
RT "Structure determination and characterization of Saccharomyces cerevisiae
RT profilin.";
RL Biochemistry 37:11171-11181(1998).
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.
CC -!- SUBUNIT: Occurs in many kinds of cells as a complex with monomeric
CC actin in a 1:1 ratio.
CC -!- INTERACTION:
CC P07274; P60010: ACT1; NbExp=4; IntAct=EBI-13892, EBI-2169;
CC P07274; Q9VEX9: Bin1; Xeno; NbExp=3; IntAct=EBI-13892, EBI-129424;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR EMBL; M23369; AAA34861.1; -; Genomic_DNA.
DR EMBL; Y00469; CAA68532.1; -; mRNA.
DR EMBL; X90518; CAA62128.1; -; Genomic_DNA.
DR EMBL; X94335; CAA64041.1; -; Genomic_DNA.
DR EMBL; Z75030; CAA99321.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10896.1; -; Genomic_DNA.
DR PIR; A31360; A31360.
DR RefSeq; NP_014765.3; NM_001183541.3.
DR PDB; 1K0K; X-ray; 2.35 A; A=2-126.
DR PDB; 1YPR; X-ray; 2.30 A; A/B=2-126.
DR PDBsum; 1K0K; -.
DR PDBsum; 1YPR; -.
DR AlphaFoldDB; P07274; -.
DR SMR; P07274; -.
DR BioGRID; 34517; 738.
DR DIP; DIP-46N; -.
DR IntAct; P07274; 6.
DR MINT; P07274; -.
DR STRING; 4932.YOR122C; -.
DR iPTMnet; P07274; -.
DR MaxQB; P07274; -.
DR PaxDb; P07274; -.
DR PRIDE; P07274; -.
DR EnsemblFungi; YOR122C_mRNA; YOR122C; YOR122C.
DR GeneID; 854289; -.
DR KEGG; sce:YOR122C; -.
DR SGD; S000005648; PFY1.
DR VEuPathDB; FungiDB:YOR122C; -.
DR eggNOG; KOG1755; Eukaryota.
DR GeneTree; ENSGT00730000112841; -.
DR HOGENOM; CLU_120772_1_0_1; -.
DR InParanoid; P07274; -.
DR OMA; WAQSSGF; -.
DR BioCyc; YEAST:G3O-33649-MON; -.
DR EvolutionaryTrace; P07274; -.
DR PRO; PR:P07274; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P07274; protein.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:SGD.
DR GO; GO:0003785; F:actin monomer binding; IDA:SGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:SGD.
DR GO; GO:0070064; F:proline-rich region binding; IDA:SGD.
DR GO; GO:0046907; P:intracellular transport; IGI:SGD.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IMP:SGD.
DR GO; GO:0090338; P:positive regulation of formin-nucleated actin cable assembly; IDA:SGD.
DR GO; GO:0042989; P:sequestering of actin monomers; IDA:SGD.
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..126
FT /note="Profilin"
FT /id="PRO_0000199608"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:1YPR"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:1YPR"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:1YPR"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:1YPR"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:1YPR"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1YPR"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:1YPR"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:1YPR"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:1YPR"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:1YPR"
FT HELIX 107..123
FT /evidence="ECO:0007829|PDB:1YPR"
SQ SEQUENCE 126 AA; 13677 MW; 2485E413AB30DEAD CRC64;
MSWQAYTDNL IGTGKVDKAV IYSRAGDAVW ATSGGLSLQP NEIGEIVQGF DNPAGLQSNG
LHIQGQKFML LRADDRSIYG RHDAEGVVCV RTKQTVIIAH YPPTVQAGEA TKIVEQLADY
LIGVQY
