PROF2_RAT
ID PROF2_RAT Reviewed; 140 AA.
AC Q9EPC6; Q9JHU7;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Profilin-2;
DE AltName: Full=Profilin II;
GN Name=Pfn2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=11027290; DOI=10.1128/mcb.20.21.8209-8219.2000;
RA Lambrechts A., Braun A., Jonckheere V., Aszodi A., Lanier L.M., Robbens J.,
RA Van Colen I., Vandekerckhove J., Faessler R., Ampe C.;
RT "Profilin II is alternatively spliced, resulting in profilin isoforms that
RT are differentially expressed and have distinct biochemical properties.";
RL Mol. Cell. Biol. 20:8209-8219(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Xiao H., Huang Q., Zhang F., Yang Z., Chen Z., Han Z., Zhang X.;
RT "Novel genes expression in rat brain.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 55-69; 92-105 AND 109-116, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
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 (By similarity). Interacts with PFN2 (By
CC similarity). {ECO:0000250|UniProtKB:P35080,
CC ECO:0000250|UniProtKB:Q9JJV2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=IIa;
CC IsoId=Q9EPC6-1; Sequence=Displayed;
CC Name=IIb;
CC IsoId=Q9EPC6-2; Sequence=Not described;
CC -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR EMBL; AF228736; AAG24947.1; -; mRNA.
DR EMBL; AF228737; AAG24948.1; -; mRNA.
DR EMBL; AY004289; AAF86616.1; -; mRNA.
DR RefSeq; NP_110500.1; NM_030873.1. [Q9EPC6-1]
DR RefSeq; XP_003749330.1; XM_003749282.3. [Q9EPC6-1]
DR RefSeq; XP_006232452.1; XM_006232390.3. [Q9EPC6-1]
DR PDB; 2VK3; X-ray; 1.70 A; A=1-140.
DR PDBsum; 2VK3; -.
DR AlphaFoldDB; Q9EPC6; -.
DR SMR; Q9EPC6; -.
DR BioGRID; 249528; 1.
DR CORUM; Q9EPC6; -.
DR IntAct; Q9EPC6; 2.
DR STRING; 10116.ENSRNOP00000061388; -.
DR iPTMnet; Q9EPC6; -.
DR PhosphoSitePlus; Q9EPC6; -.
DR SwissPalm; Q9EPC6; -.
DR jPOST; Q9EPC6; -.
DR PaxDb; Q9EPC6; -.
DR PRIDE; Q9EPC6; -.
DR Ensembl; ENSRNOT00000023469; ENSRNOP00000023469; ENSRNOG00000017427. [Q9EPC6-1]
DR GeneID; 81531; -.
DR KEGG; rno:81531; -.
DR UCSC; RGD:621826; rat. [Q9EPC6-1]
DR CTD; 5217; -.
DR RGD; 621826; Pfn2.
DR eggNOG; KOG1755; Eukaryota.
DR GeneTree; ENSGT00940000153664; -.
DR HOGENOM; CLU_123405_1_0_1; -.
DR InParanoid; Q9EPC6; -.
DR OMA; CCLEAAI; -.
DR OrthoDB; 1428600at2759; -.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR EvolutionaryTrace; Q9EPC6; -.
DR PRO; PR:Q9EPC6; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000017427; Expressed in frontal cortex and 20 other tissues.
DR ExpressionAtlas; Q9EPC6; baseline and differential.
DR Genevisible; Q9EPC6; RN.
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; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0003779; F:actin binding; IDA:RGD.
DR GO; GO:0003785; F:actin monomer binding; ISO:RGD.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:RGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0098885; P:modification of postsynaptic actin cytoskeleton; ISO:RGD.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; ISO:RGD.
DR GO; GO:0010633; P:negative regulation of epithelial cell migration; ISO:RGD.
DR GO; GO:1900028; P:negative regulation of ruffle assembly; ISO:RGD.
DR GO; GO:0032233; P:positive regulation of actin filament bundle assembly; ISO:RGD.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISO:RGD.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISO:RGD.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IDA:RGD.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:RGD.
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 3D-structure; Acetylation; Actin-binding; Alternative splicing; Cytoplasm;
KW Cytoskeleton; 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_0000199578"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P35080"
FT CONFLICT 139..140
FT /note="GF -> WVLAARQTVKY (in Ref. 2)"
FT /evidence="ECO:0000305"
FT HELIX 2..9
FT /evidence="ECO:0007829|PDB:2VK3"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:2VK3"
FT STRAND 15..24
FT /evidence="ECO:0007829|PDB:2VK3"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:2VK3"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:2VK3"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:2VK3"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:2VK3"
FT HELIX 58..62
FT /evidence="ECO:0007829|PDB:2VK3"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:2VK3"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:2VK3"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:2VK3"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:2VK3"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:2VK3"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:2VK3"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:2VK3"
FT HELIX 121..137
FT /evidence="ECO:0007829|PDB:2VK3"
SQ SEQUENCE 140 AA; 15002 MW; 0146DF257BD9C20B CRC64;
MAGWQSYVDN LMCDGCCQEA AIVGYCDAKY VWAATAGGVF QSITPAEIDV IIGKDREGFF
TNGLTLGGKK CSVIRDSLYV DSDCTMDIRT KSQGGEPTYN VAVGRAGRVL VFVMGKEGVH
GGGLNKKAYS MAKYLRDSGF
