PRF4_ARATH
ID PRF4_ARATH Reviewed; 134 AA.
AC Q38904; A0A178UXH3; Q29PU0; Q84WD4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Profilin-4;
DE AltName: Full=AtPROF3 {ECO:0000305};
DE AltName: Full=AthPRF4 {ECO:0000305};
GN Name=PRF4 {ECO:0000303|PubMed:17933902};
GN Synonyms=PFN3 {ECO:0000303|PubMed:8771785}, PRO3 {ECO:0000305};
GN OrderedLocusNames=At4g29340 {ECO:0000312|Araport:AT4G29340};
GN ORFNames=F17A13.160 {ECO:0000312|EMBL:CAB79692.1};
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].
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [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 FUNCTION.
RX PubMed=16313636; DOI=10.1111/j.1469-8137.2005.01582.x;
RA Deeks M.J., Cvrckova F., Machesky L.M., Mikitova V., Ketelaar T.,
RA Zarsky V., Davies B., Hussey P.J.;
RT "Arabidopsis group Ie formins localize to specific cell membrane domains,
RT interact with actin-binding proteins and cause defects in cell expansion
RT upon aberrant expression.";
RL New Phytol. 168:529-540(2005).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=17933902; DOI=10.1105/tpc.107.052621;
RA Kandasamy M.K., Burgos-Rivera B., McKinney E.C., Ruzicka D.R.,
RA Meagher R.B.;
RT "Class-specific interaction of profilin and ADF isovariants with actin in
RT the regulation of plant development.";
RL Plant Cell 19:3111-3126(2007).
RN [10]
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 [11]
RP FUNCTION.
RX PubMed=26996265; DOI=10.1016/j.molp.2016.03.006;
RA Zhang S., Liu C., Wang J., Ren Z., Staiger C.J., Ren H.;
RT "A processive Arabidopsis formin modulates actin filament dynamics in
RT association with profilin.";
RL Mol. Plant 9:900-910(2016).
RN [12]
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, PubMed:26996265, PubMed:16313636).
CC Acts redundantly with PRF5 to regulate apical actin polymerization at
CC the tip of pollen tube and control polarized pollen tube growth
CC (PubMed:26433093). Functions probably by favoring formin-mediated actin
CC polymerization at pollen tube tips (PubMed:26433093).
CC {ECO:0000269|PubMed:16313636, ECO:0000269|PubMed:26433093,
CC ECO:0000269|PubMed:26996265, 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}. Cytoplasm
CC {ECO:0000269|PubMed:17933902}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in mature and germinating
CC pollen grains, and growing pollen tubes (at protein level).
CC {ECO:0000269|PubMed:11977080}.
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}.
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DR EMBL; U43323; AAB39477.1; -; Genomic_DNA.
DR EMBL; U43594; AAG10091.1; -; Genomic_DNA.
DR EMBL; AL161574; CAB79692.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85619.1; -; Genomic_DNA.
DR EMBL; BT003946; AAO41991.1; -; mRNA.
DR EMBL; BT024816; ABD60699.1; -; mRNA.
DR EMBL; AY085179; AAM61730.1; -; mRNA.
DR PIR; D85342; D85342.
DR RefSeq; NP_194663.1; NM_119079.4.
DR AlphaFoldDB; Q38904; -.
DR SMR; Q38904; -.
DR STRING; 3702.AT4G29340.1; -.
DR PaxDb; Q38904; -.
DR PRIDE; Q38904; -.
DR ProteomicsDB; 226216; -.
DR EnsemblPlants; AT4G29340.1; AT4G29340.1; AT4G29340.
DR GeneID; 829055; -.
DR Gramene; AT4G29340.1; AT4G29340.1; AT4G29340.
DR KEGG; ath:AT4G29340; -.
DR Araport; AT4G29340; -.
DR TAIR; locus:2118309; AT4G29340.
DR eggNOG; KOG1755; Eukaryota.
DR HOGENOM; CLU_120772_0_1_1; -.
DR InParanoid; Q38904; -.
DR OMA; TIQPAEM; -.
DR OrthoDB; 1428600at2759; -.
DR PhylomeDB; Q38904; -.
DR PRO; PR:Q38904; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q38904; baseline and differential.
DR Genevisible; Q38904; 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:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0003785; F:actin monomer binding; IBA:GO_Central.
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-4"
FT /id="PRO_0000199617"
FT CONFLICT 132
FT /note="Q -> R (in Ref. 4; AAO41991)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 134 AA; 14418 MW; E81BABD416562FA5 CRC64;
MSWQTYVDEH LMCDVGDGQG HHLTAAAIVG HDGSVWAQSA NFPQFKGQEF SDIMKDFDEP
GHLAPTGLFM AGAKYMVIQG EPGAVIRGKK GAGGITIKKT GQSCVFGIYE EPVTPGQCNM
VVERLGDYLL EQGL
