PROF3_CAEEL
ID PROF3_CAEEL Reviewed; 126 AA.
AC Q21193; Q5GHR0;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Profilin-3;
GN Name=pfn-3; ORFNames=K03E6.6;
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], FUNCTION, 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. Also binds to poly(L-proline) and
CC phosphatidylinositol 4,5-bisphosphate micelles.
CC {ECO:0000269|PubMed:16317718}.
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.
CC -!- TISSUE SPECIFICITY: In embryos, expression is specifically detected in
CC body wall muscle cells. In adults, expression is localized to a
CC striking dot-like fashion in body wall muscle.
CC {ECO:0000269|PubMed:16317718}.
CC -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR EMBL; AY530910; AAT01435.1; -; mRNA.
DR EMBL; FO080324; CCD62864.1; -; Genomic_DNA.
DR PIR; T34327; T34327.
DR RefSeq; NP_508205.1; NM_075804.3.
DR AlphaFoldDB; Q21193; -.
DR SMR; Q21193; -.
DR BioGRID; 45413; 9.
DR IntAct; Q21193; 1.
DR STRING; 6239.K03E6.6; -.
DR iPTMnet; Q21193; -.
DR EPD; Q21193; -.
DR PaxDb; Q21193; -.
DR PeptideAtlas; Q21193; -.
DR EnsemblMetazoa; K03E6.6.1; K03E6.6.1; WBGene00003991.
DR GeneID; 180460; -.
DR KEGG; cel:CELE_K03E6.6; -.
DR UCSC; K03E6.6; c. elegans.
DR CTD; 180460; -.
DR WormBase; K03E6.6; CE07332; WBGene00003991; pfn-3.
DR eggNOG; KOG1755; Eukaryota.
DR GeneTree; ENSGT00730000112841; -.
DR HOGENOM; CLU_120772_1_0_1; -.
DR InParanoid; Q21193; -.
DR OMA; WAQSSGF; -.
DR OrthoDB; 1428600at2759; -.
DR PhylomeDB; Q21193; -.
DR PRO; PR:Q21193; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003991; Expressed in larva and 4 other tissues.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0055120; C:striated muscle dense body; IDA:WormBase.
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 PRINTS; PR00392; PROFILIN.
DR PRINTS; PR01640; PROFILINPLNT.
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..126
FT /note="Profilin-3"
FT /id="PRO_0000199592"
SQ SEQUENCE 126 AA; 13531 MW; 9E8437D38314F6BB CRC64;
MSWSDIINNN LIGSGNVSKA AILGFDGAVW AKSDNFNISV EEAVAAGKAF TSLDALLGTG
LRLEGQKFLV LNADNDRIIG KQGGSGFFIY KTIQAVIISI YEKGLQPEMC SKTTGALADY
FRSIKY