PROF2_BOVIN
ID PROF2_BOVIN Reviewed; 140 AA.
AC Q09430; A4FUW7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Profilin-2;
DE AltName: Full=Profilin II;
GN Name=PFN2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 30-140.
RC TISSUE=Brain;
RX PubMed=7601111; DOI=10.1111/j.1432-1033.1995.0281i.x;
RA Lambrechts A., van Damme J., Goethals M., Vandekerckhove J., Ampe C.;
RT "Purification and characterization of bovine profilin II. Actin, poly(L-
RT proline) and inositolphospholipid binding.";
RL Eur. J. Biochem. 230:281-286(1995).
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 (By similarity). Interacts with PFN2 (By
CC similarity). {ECO:0000250|UniProtKB:P35080,
CC ECO:0000250|UniProtKB:Q9JJV2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR EMBL; BC122616; AAI22617.1; -; mRNA.
DR PIR; S65365; S65365.
DR RefSeq; NP_001121669.1; NM_001128197.1.
DR AlphaFoldDB; Q09430; -.
DR BMRB; Q09430; -.
DR SMR; Q09430; -.
DR STRING; 9913.ENSBTAP00000014805; -.
DR PaxDb; Q09430; -.
DR PRIDE; Q09430; -.
DR Ensembl; ENSBTAT00000014805; ENSBTAP00000014805; ENSBTAG00000011150.
DR GeneID; 539034; -.
DR KEGG; bta:539034; -.
DR CTD; 5217; -.
DR VEuPathDB; HostDB:ENSBTAG00000011150; -.
DR VGNC; VGNC:32776; PFN2.
DR eggNOG; KOG1755; Eukaryota.
DR GeneTree; ENSGT00940000153664; -.
DR HOGENOM; CLU_123405_1_0_1; -.
DR InParanoid; Q09430; -.
DR OMA; CCLEAAI; -.
DR OrthoDB; 1428600at2759; -.
DR TreeFam; TF331744; -.
DR Reactome; R-BTA-376176; Signaling by ROBO receptors.
DR Reactome; R-BTA-5663220; RHO GTPases Activate Formins.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000011150; Expressed in occipital lobe and 104 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR GO; GO:0098793; C:presynapse; IEA:Ensembl.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0003785; F:actin monomer binding; IEA:Ensembl.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Ensembl.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0098885; P:modification of postsynaptic actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IEA:Ensembl.
DR GO; GO:0010633; P:negative regulation of epithelial cell migration; IEA:Ensembl.
DR GO; GO:1900028; P:negative regulation of ruffle assembly; IEA:Ensembl.
DR GO; GO:0032233; P:positive regulation of actin filament bundle assembly; IBA:GO_Central.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IEA:Ensembl.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IBA:GO_Central.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR CDD; cd00148; PROF; 1.
DR InterPro; IPR005455; PFN.
DR InterPro; IPR029891; PFN2.
DR InterPro; IPR036140; PFN_sf.
DR InterPro; IPR005454; Profilin1/2/3_vertebrate.
DR InterPro; IPR027310; Profilin_CS.
DR PANTHER; PTHR13936:SF15; PTHR13936:SF15; 1.
DR Pfam; PF00235; Profilin; 1.
DR PRINTS; PR00392; PROFILIN.
DR PRINTS; PR01639; PROFILINMAML.
DR SMART; SM00392; PROF; 1.
DR SUPFAM; SSF55770; SSF55770; 1.
DR PROSITE; PS00414; PROFILIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P35080"
FT CHAIN 2..140
FT /note="Profilin-2"
FT /id="PRO_0000199574"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P35080"
SQ SEQUENCE 140 AA; 15032 MW; E780BF62E9EC8476 CRC64;
MAGWQSYVDN LMCDGCCQEA AIVGYCDAKY VWAATAGGVF QSITPVEIDM IVGKDREGFF
TNGLTLGAKK CSVIRDSLYV DGDCTMDIRT KSQGGEPTYN VAVGRAGRVL VFVMGKEGVH
GGGLNKKAYS MAKYLRDSGF
