ID   PROF2_CAEEL             Reviewed;         131 AA.
AC   Q20025; Q5GHR1;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 3.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Profilin-2;
GN   Name=pfn-2; ORFNames=F35C8.6;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=16317718; DOI=10.1002/cm.20102;
RA   Polet D., Lambrechts A., Ono K., Mah A., Peelman F., Vandekerckhove J.,
RA   Baillie D.L., Ampe C., Ono S.;
RT   "Caenorhabditis elegans expresses three functional profilins in a tissue-
RT   specific manner.";
RL   Cell Motil. Cytoskeleton 63:14-28(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Occurs in many kinds of cells as a complex with monomeric
CC       actin in a 1:1 ratio. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in the intestinal wall, the spermatheca,
CC       and the pharynx. {ECO:0000269|PubMed:16317718}.
CC   -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR   EMBL; AY530909; AAT01434.1; -; mRNA.
DR   EMBL; FO080312; CCD62785.1; -; Genomic_DNA.
DR   PIR; T16253; T16253.
DR   RefSeq; NP_508910.3; NM_076509.5.
DR   AlphaFoldDB; Q20025; -.
DR   SMR; Q20025; -.
DR   BioGRID; 45741; 23.
DR   STRING; 6239.F35C8.6; -.
DR   EPD; Q20025; -.
DR   PaxDb; Q20025; -.
DR   PeptideAtlas; Q20025; -.
DR   EnsemblMetazoa; F35C8.6.1; F35C8.6.1; WBGene00003990.
DR   GeneID; 180808; -.
DR   KEGG; cel:CELE_F35C8.6; -.
DR   UCSC; F35C8.6; c. elegans.
DR   CTD; 180808; -.
DR   WormBase; F35C8.6; CE39098; WBGene00003990; pfn-2.
DR   eggNOG; KOG1755; Eukaryota.
DR   HOGENOM; CLU_120772_3_0_1; -.
DR   InParanoid; Q20025; -.
DR   OMA; MSGWDDY; -.
DR   OrthoDB; 1428600at2759; -.
DR   PhylomeDB; Q20025; -.
DR   PRO; PR:Q20025; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00003990; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003785; F:actin monomer binding; IBA:GO_Central.
DR   GO; GO:0071689; P:muscle thin filament assembly; IGI:WormBase.
DR   GO; GO:0042989; P:sequestering of actin monomers; IBA:GO_Central.
DR   CDD; cd00148; PROF; 1.
DR   InterPro; IPR005455; PFN.
DR   InterPro; IPR036140; PFN_sf.
DR   PANTHER; PTHR11604; PTHR11604; 1.
DR   Pfam; PF00235; Profilin; 1.
DR   SMART; SM00392; PROF; 1.
DR   SUPFAM; SSF55770; SSF55770; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome.
FT   CHAIN           1..131
FT                   /note="Profilin-2"
FT                   /id="PRO_0000199591"
SQ   SEQUENCE   131 AA;  14244 MW;  717B923C13D59AD7 CRC64;
     MSGWDDYIKL LFGKSPAIKR AAIIGSDGSV WARSGDANAF RATEVELKRF AALFNDINSV
     PGTGADLEEI HYIVPRVEEK LIFGKKEQTG FFAAKTNQAI VIAMYEGDNA QSASVRAGVE
     YIAQYLASSG Y