PRF5_ARATH
ID PRF5_ARATH Reviewed; 134 AA.
AC Q38905; A0MEN1; Q1PF40;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Profilin-5 {ECO:0000303|PubMed:16361517};
DE AltName: Full=AtPROF4 {ECO:0000305};
DE AltName: Full=AthPRF4 {ECO:0000303|PubMed:8685262};
GN Name=PRF5 {ECO:0000303|PubMed:16361517};
GN Synonyms=PFN4 {ECO:0000303|PubMed:8771785},
GN PRF4 {ECO:0000303|PubMed:8685262}, PRO4 {ECO:0000305};
GN OrderedLocusNames=At2g19770 {ECO:0000312|Araport:AT2G19770};
GN ORFNames=F6F22.20 {ECO:0000312|EMBL:AAC62139.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=8771785; DOI=10.1046/j.1365-313x.1996.10020269.x;
RA Christensen H.E.M., Ramachandran S., Tan C.T., Surana U., Dong C.H.,
RA Chua N.-H.;
RT "Arabidopsis profilins are functionally similar to yeast profilins:
RT identification of a vascular bundle-specific profilin and a pollen-specific
RT profilin.";
RL Plant J. 10:269-279(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=8685262; DOI=10.1104/pp.111.1.115;
RA Huang S., McDowell J.M., Weise M.J., Meagher R.B.;
RT "The Arabidopsis profilin gene family. Evidence for an ancient split
RT between constitutive and pollen-specific profilin genes.";
RL Plant Physiol. 111:115-126(1996).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=11977080; DOI=10.1002/cm.10029;
RA Kandasamy M.K., McKinney E.C., Meagher R.B.;
RT "Plant profilin isovariants are distinctly regulated in vegetative and
RT reproductive tissues.";
RL Cell Motil. Cytoskeleton 52:22-32(2002).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=16361517; DOI=10.1104/pp.105.071316;
RA Jeong Y.M., Mun J.H., Lee I., Woo J.C., Hong C.B., Kim S.G.;
RT "Distinct roles of the first introns on the expression of Arabidopsis
RT profilin gene family members.";
RL Plant Physiol. 140:196-209(2006).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26433093; DOI=10.1016/j.molp.2015.09.013;
RA Liu X., Qu X., Jiang Y., Chang M., Zhang R., Wu Y., Fu Y., Huang S.;
RT "Profilin regulates apical actin polymerization to control polarized pollen
RT tube growth.";
RL Mol. Plant 8:1694-1709(2015).
RN [10]
RP FUNCTION.
RX PubMed=29861135; DOI=10.1016/j.cub.2018.04.045;
RA Sun H., Qiao Z., Chua K.P., Tursic A., Liu X., Gao Y.G., Mu Y., Hou X.,
RA Miao Y.;
RT "Profilin negatively regulates formin-mediated actin assembly to modulate
RT PAMP-triggered plant immunity.";
RL Curr. Biol. 28:1882-1895(2018).
CC -!- FUNCTION: Binds to actin monomers and regulates the organization of the
CC actin cytoskeleton (PubMed:29861135). At high concentrations, profilin
CC prevents the polymerization of actin, whereas it enhances it at low
CC concentrations (PubMed:29861135). At low concentrations, associates
CC with the poly-proline motif of formins to enhance actin filament
CC elongation rate (PubMed:29861135). Acts redundantly with PRF4 to
CC regulate apical actin polymerization at the tip of pollen tube and
CC control polarized pollen tube growth (PubMed:26433093). Functions
CC probably by favoring formin-mediated actin polymerization at pollen
CC tube tips (PubMed:26433093). {ECO:0000269|PubMed:26433093,
CC ECO:0000269|PubMed:29861135}.
CC -!- SUBUNIT: Occurs in many kinds of cells as a complex with monomeric
CC actin in a 1:1 ratio. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in mature pollen grains
CC (PubMed:8771785, PubMed:8685262, PubMed:11977080, PubMed:16361517).
CC Expressed in germinating pollen grains (PubMed:8771785,
CC PubMed:11977080). Expressed in growing pollen tubes (at protein level)
CC (PubMed:11977080). {ECO:0000269|PubMed:11977080,
CC ECO:0000269|PubMed:16361517, ECO:0000269|PubMed:8685262,
CC ECO:0000269|PubMed:8771785}.
CC -!- DISRUPTION PHENOTYPE: In germinating pollen grain, the double mutant
CC prf4 and prf5 reduces the amount of F-actin and induces disorganization
CC of actin filaments within the apical and subapical regions of the
CC pollen tube. {ECO:0000269|PubMed:26433093}.
CC -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28500.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; U43324; AAB39479.1; -; Genomic_DNA.
DR EMBL; AC005169; AAC62139.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06924.1; -; Genomic_DNA.
DR EMBL; DQ446526; ABE65830.1; -; mRNA.
DR EMBL; DQ653003; ABK28500.1; ALT_SEQ; mRNA.
DR EMBL; AY085645; AAM62866.1; -; mRNA.
DR PIR; H84580; H84580.
DR RefSeq; NP_179567.1; NM_127535.3.
DR AlphaFoldDB; Q38905; -.
DR SMR; Q38905; -.
DR STRING; 3702.AT2G19770.1; -.
DR PaxDb; Q38905; -.
DR PRIDE; Q38905; -.
DR ProteomicsDB; 226372; -.
DR EnsemblPlants; AT2G19770.1; AT2G19770.1; AT2G19770.
DR GeneID; 816496; -.
DR Gramene; AT2G19770.1; AT2G19770.1; AT2G19770.
DR KEGG; ath:AT2G19770; -.
DR Araport; AT2G19770; -.
DR TAIR; locus:2051945; AT2G19770.
DR eggNOG; KOG1755; Eukaryota.
DR HOGENOM; CLU_120772_0_1_1; -.
DR InParanoid; Q38905; -.
DR OMA; CEIENTG; -.
DR OrthoDB; 1428600at2759; -.
DR PhylomeDB; Q38905; -.
DR PRO; PR:Q38905; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q38905; baseline and differential.
DR Genevisible; Q38905; AT.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; HDA:TAIR.
DR GO; GO:0003785; F:actin monomer binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; TAS:TAIR.
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 PRINTS; PR00392; PROFILIN.
DR PRINTS; PR01640; PROFILINPLNT.
DR SMART; SM00392; PROF; 1.
DR SUPFAM; SSF55770; SSF55770; 1.
DR PROSITE; PS00414; PROFILIN; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..134
FT /note="Profilin-5"
FT /id="PRO_0000199618"
SQ SEQUENCE 134 AA; 14550 MW; D6DB21CFF5DF46EE CRC64;
MSWQAYVDEH LMCDVGDGQG HHLTAAAIIG HDGSVWAQSA NFPQFKPQEI TDIMKDFDEP
GHLAPTGMFL AGLKYMVIQG EPNAVIRGKK GAGGITIKKT GQSMVFGLYE EPVTPGQCNM
VVERLGDYLI EQGL
