ID   PROF2_PHYPO             Reviewed;         125 AA.
AC   P18322;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Profilin-P;
GN   Name=PROP;
OS   Physarum polycephalum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Myxogastria;
OC   Myxogastromycetidae; Physariida; Physaraceae; Physarum.
OX   NCBI_TaxID=5791;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2372376; DOI=10.1089/dna.1990.9.323;
RA   Binette F., Benard M., Laroche A., Pierron G., Lemieux G., Pallotta D.;
RT   "Cell-specific expression of a profilin gene family.";
RL   DNA Cell Biol. 9:323-334(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-125, AND ACETYLATION AT SER-2.
RX   PubMed=2209623; DOI=10.1111/j.1432-1033.1990.tb19289.x;
RA   Takagi T., Mabuchi I., Hosoya H., Furuhashi K., Hatano S.;
RT   "Primary structure of profilins from two species of Echinoidea and Physarum
RT   polycephalum.";
RL   Eur. J. Biochem. 192:777-781(1990).
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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR   EMBL; M38038; AAD13630.1; -; Genomic_DNA.
DR   PIR; B35273; B35273.
DR   PIR; S13199; S13199.
DR   AlphaFoldDB; P18322; -.
DR   SMR; P18322; -.
DR   iPTMnet; P18322; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
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   Acetylation; Actin-binding; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2209623"
FT   CHAIN           2..125
FT                   /note="Profilin-P"
FT                   /id="PRO_0000199601"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:2209623"
FT   CONFLICT        8
FT                   /note="D -> H (in Ref. 1; AAD13630)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        86
FT                   /note="V -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   125 AA;  13192 MW;  F2345987755769F6 CRC64;
     MSWQTYVDEQ LVGTGQLDGA IIIGLDGNSW ASKNLTLKAG EGQAIAALFK TPANVFASGI
     TINGIKYMGI KGDSRSIYGK KGATGVATVI TGQCILIGYY NEKQQPGNAA LVVEKLADYL
     IENGY