ID   PROF_TETPY              Reviewed;         153 AA.
AC   P23412;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Profilin;
OS   Tetrahymena pyriformis.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=5908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1902095; DOI=10.1016/0006-291x(91)91599-8;
RA   Edamatsu M., Hirono M., Takemasa T., Watanabe Y.;
RT   "The primary structure of Tetrahymena profilin.";
RL   Biochem. Biophys. Res. Commun. 175:543-550(1991).
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; D00813; BAA00694.1; -; mRNA.
DR   PIR; JT0572; JT0572.
DR   AlphaFoldDB; P23412; -.
DR   SMR; P23412; -.
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   SMART; SM00392; PROF; 1.
DR   SUPFAM; SSF55770; SSF55770; 1.
DR   PROSITE; PS00414; PROFILIN; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; Cytoplasm; Cytoskeleton.
FT   CHAIN           1..153
FT                   /note="Profilin"
FT                   /id="PRO_0000199604"
SQ   SEQUENCE   153 AA;  16785 MW;  C2D8D9D08000728F CRC64;
     MSGWDQYVQY LTANQQVEYG LILGKTDGTI WASNVGLTTL YNNYQIDVEG QKANVNETAN
     LLAAMNNNGV PTDPLCGIRI MNQKYYTVKY DADSQVWYLK KDHGGACIAI TNQALVIGTF
     DITKKQQNGV AQNPGQVNKV VESLAATLKQ AGY