PROF1_RAT
ID PROF1_RAT Reviewed; 140 AA.
AC P62963; P10924;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Profilin-1;
DE AltName: Full=Profilin I;
GN Name=Pfn1;
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 STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=8651905; DOI=10.1006/bbrc.1996.0804;
RA Tamura M., Tanaka H., Hirano T., Ueta Y., Higashi K., Hirano H.;
RT "Enhanced glomerular profilin gene and protein expression in experimental
RT mesangial proliferative glomerulonephritis.";
RL Biochem. Biophys. Res. Commun. 222:683-687(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 39-54; 57-70 AND 76-89, 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.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Inhibits androgen receptor (AR)
CC and HTT aggregation and binding of G-actin is essential for its
CC inhibition of AR (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with VASP. Occurs in many kinds of cells as a
CC complex with monomeric actin in a 1:1 ratio. Found in a complex with
CC XPO6, Ran, ACTB and PFN1 (By similarity). Interacts with HTT (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- PTM: Phosphorylation at Ser-138 reduces its affinity for G-actin and
CC blocks its interaction with HTT, reducing its ability to inhibit
CC androgen receptor (AR) and HTT aggregation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR EMBL; X96967; CAA65655.1; -; mRNA.
DR EMBL; BC062405; AAH62405.1; -; mRNA.
DR PIR; PC4172; PC4172.
DR RefSeq; NP_071956.2; NM_022511.2.
DR AlphaFoldDB; P62963; -.
DR SMR; P62963; -.
DR BioGRID; 249018; 6.
DR IntAct; P62963; 3.
DR MINT; P62963; -.
DR STRING; 10116.ENSRNOP00000005370; -.
DR iPTMnet; P62963; -.
DR PhosphoSitePlus; P62963; -.
DR SwissPalm; P62963; -.
DR jPOST; P62963; -.
DR PaxDb; P62963; -.
DR PRIDE; P62963; -.
DR Ensembl; ENSRNOT00000005370; ENSRNOP00000005370; ENSRNOG00000003975.
DR GeneID; 64303; -.
DR KEGG; rno:64303; -.
DR UCSC; RGD:621825; rat.
DR CTD; 5216; -.
DR RGD; 621825; Pfn1.
DR eggNOG; KOG1755; Eukaryota.
DR GeneTree; ENSGT00940000153664; -.
DR HOGENOM; CLU_123405_1_0_1; -.
DR InParanoid; P62963; -.
DR OMA; NKKCFEM; -.
DR OrthoDB; 1428600at2759; -.
DR PhylomeDB; P62963; -.
DR TreeFam; TF331744; -.
DR Reactome; R-RNO-4086400; PCP/CE pathway.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR PRO; PR:P62963; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003975; Expressed in thymus and 19 other tissues.
DR Genevisible; P62963; RN.
DR GO; GO:0005938; C:cell cortex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IDA:SynGO.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0003785; F:actin monomer binding; ISO:RGD.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; ISO:RGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:RGD.
DR GO; GO:0001784; F:phosphotyrosine residue binding; ISO:RGD.
DR GO; GO:0070064; F:proline-rich region binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IDA:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0008154; P:actin polymerization or depolymerization; TAS:RGD.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
DR GO; GO:0098885; P:modification of postsynaptic actin cytoskeleton; ISO:RGD.
DR GO; GO:0032232; P:negative regulation of actin filament bundle assembly; ISO:RGD.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; ISO:RGD.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:RGD.
DR GO; GO:0001843; P:neural tube closure; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISO:RGD.
DR GO; GO:0051054; P:positive regulation of DNA metabolic process; IDA:RGD.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:RGD.
DR GO; GO:1900029; P:positive regulation of ruffle assembly; ISO:RGD.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0050434; P:positive regulation of viral transcription; IMP:RGD.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0060074; P:synapse maturation; ISO:RGD.
DR CDD; cd00148; PROF; 1.
DR InterPro; IPR005455; PFN.
DR InterPro; IPR029892; PFN1.
DR InterPro; IPR036140; PFN_sf.
DR InterPro; IPR005454; Profilin1/2/3_vertebrate.
DR InterPro; IPR027310; Profilin_CS.
DR PANTHER; PTHR13936:SF14; PTHR13936:SF14; 1.
DR Pfam; PF00235; Profilin; 1.
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; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02584"
FT CHAIN 2..140
FT /note="Profilin-1"
FT /id="PRO_0000199573"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P02584"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07737"
FT MOD_RES 108
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07737"
FT MOD_RES 129
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P07737"
FT MOD_RES 138
FT /note="Phosphoserine; by ROCK1"
FT /evidence="ECO:0000250|UniProtKB:P07737"
FT CROSSLNK 54
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P07737"
FT CROSSLNK 54
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P07737"
SQ SEQUENCE 140 AA; 14957 MW; 1DC8B60D545FF70E CRC64;
MAGWNAYIDS LMADGTCQDA AIVGYKDSPS VWAAVPGKTF VSITPAEVGV LVGKDRSSFF
VNGLTLGGQK CSVIRDSLLQ DGEFTMDLRT KSTGGAPTFN VTVTMTAKTL VLLMGKEGVH
GGLINKKCYE MASHLRRSQY
