PROF1_CAEEL
ID PROF1_CAEEL Reviewed; 132 AA.
AC Q9XW16; Q5GHR2;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Profilin-1;
GN Name=pfn-1; ORFNames=Y18D10A.20;
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, SUBCELLULAR LOCATION, AND TISSUE
RP 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 {ECO:0000269|PubMed:16317718}. Note=Also localized at cell-cell
CC contacts at the early embryonic stages.
CC -!- TISSUE SPECIFICITY: Expressed in the nerve ring during late embryonic
CC stages. In adults, expression is seen in the neurons, vulva and somatic
CC gonad. {ECO:0000269|PubMed:16317718}.
CC -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR EMBL; AY530908; AAT01433.1; -; mRNA.
DR EMBL; AL034393; CAA22318.1; -; Genomic_DNA.
DR PIR; T26527; T26527.
DR RefSeq; NP_493258.1; NM_060857.5.
DR AlphaFoldDB; Q9XW16; -.
DR SMR; Q9XW16; -.
DR BioGRID; 38558; 33.
DR STRING; 6239.Y18D10A.20; -.
DR EPD; Q9XW16; -.
DR PaxDb; Q9XW16; -.
DR PeptideAtlas; Q9XW16; -.
DR EnsemblMetazoa; Y18D10A.20.1; Y18D10A.20.1; WBGene00003989.
DR GeneID; 173161; -.
DR KEGG; cel:CELE_Y18D10A.20; -.
DR UCSC; Y18D10A.20; c. elegans.
DR CTD; 173161; -.
DR WormBase; Y18D10A.20; CE21418; WBGene00003989; pfn-1.
DR eggNOG; KOG1755; Eukaryota.
DR HOGENOM; CLU_120772_3_0_1; -.
DR InParanoid; Q9XW16; -.
DR OMA; VESMQTY; -.
DR OrthoDB; 1428600at2759; -.
DR PhylomeDB; Q9XW16; -.
DR PRO; PR:Q9XW16; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00003989; Expressed in germ line (C elegans) 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:0003785; F:actin monomer binding; IBA:GO_Central.
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 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; Reference proteome.
FT CHAIN 1..132
FT /note="Profilin-1"
FT /id="PRO_0000199590"
SQ SEQUENCE 132 AA; 14255 MW; 9801D9AC314E95E1 CRC64;
MSGWNAYIDT MTAAAPSIKR CAIVGAADGS VWARTEADNV FKASEEELKT FVALFNDVTQ
VPAKGADIEG VHYVVPRTEE SLIFGKKENT GFFAVKTKSA VLIAVYEGPN EVAAQVRKAV
ESMQTYLNNA GY
