ID   PROF_HELCR              Reviewed;         140 AA.
AC   P18320;
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   Heliocidaris crassispina (Sea urchin) (Anthocidaris crassispina).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Echinometridae;
OC   Heliocidaris.
OX   NCBI_TaxID=1043166;
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; S13198; S13198.
DR   AlphaFoldDB; P18320; -.
DR   SMR; P18320; -.
DR   iPTMnet; P18320; -.
DR   PRIDE; P18320; -.
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_0000199586"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:2209623"
SQ   SEQUENCE   140 AA;  14701 MW;  D8E19DD5A392065E CRC64;
     MSWDSYIDNL IAQTKDASGT GHSDKACIIG IDGGAPWTTA GHANALKLEG QEGPNIARCF
     KSKDFTPFMS SGIVADGTKY QFLREEDGKL VLAKKKGQGA LTLQSSKTAI VIGHAPEGGQ
     QGNTNKGVAV IAEYLESLGM