PROF_NAEPR
ID PROF_NAEPR Reviewed; 132 AA.
AC Q6QNF8;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Profilin;
OS Naegleria pringsheimi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=234921;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 30961 / NB-1;
RA Kang S.M., Yang H.J., Lee J.H.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR EMBL; AY532620; AAS46037.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6QNF8; -.
DR SMR; Q6QNF8; -.
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 InterPro; IPR005455; PFN.
DR InterPro; IPR036140; PFN_sf.
DR PANTHER; PTHR11604; PTHR11604; 1.
DR Pfam; PF00235; Profilin; 1.
DR PRINTS; PR00392; PROFILIN.
DR SMART; SM00392; PROF; 1.
DR SUPFAM; SSF55770; SSF55770; 1.
PE 3: Inferred from homology;
KW Actin-binding; Cytoplasm; Cytoskeleton.
FT CHAIN 1..132
FT /note="Profilin"
FT /id="PRO_0000199599"
SQ SEQUENCE 132 AA; 13657 MW; 44148B9D03D08D9F CRC64;
MSWTPFVDSQ FVAPSNGLIQ KGLIMGRDGT VWGVSDGWAV TAQEAKNLAG QVANPSSVPA
SGITLGGVKY MGLVADEENF QGFSSSKKQG VSGVVLKSAV IIGLFGEPHK NPNAYSFLKG
VADSLVNAGT LQ