ID   PROF_CLYJA              Reviewed;         140 AA.
AC   P18321;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Profilin;
OS   Clypeaster japonicus (Sand dollar).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Gnathostomata; Clypeasteroida; Clypeasteridae; Clypeaster.
OX   NCBI_TaxID=7644;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-140, 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   PIR; S13197; S13197.
DR   AlphaFoldDB; P18321; -.
DR   SMR; P18321; -.
DR   iPTMnet; P18321; -.
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   GO; GO:0044087; P:regulation of cellular component biogenesis; IEA:UniProt.
DR   GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
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   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..140
FT                   /note="Profilin"
FT                   /id="PRO_0000199593"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:2209623"
SQ   SEQUENCE   140 AA;  14672 MW;  48F539CB53EB093C CRC64;
     MSWDSYIDNL VAQTKDASGT AHSDRACIIG LDGGAPWTTA GHANALKLQG TEGANIAKCF
     KSKDFSAFMA GGVHAEGLKY QFLREEDAKL VLAKKKGEGA ITLQASKTAI VIAHCPEGGQ
     QGNTNKGVSV IAEYLESLGM