PRF2_ARATH
ID PRF2_ARATH Reviewed; 131 AA.
AC Q42418; A0A178V4L3; C0Z3G0; Q8LCJ1; Q9FS48;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Profilin-2 {ECO:0000303|PubMed:8685262};
DE AltName: Full=AtPROF2 {ECO:0000305};
DE AltName: Full=AthPRF2 {ECO:0000303|PubMed:8685262};
GN Name=PRF2 {ECO:0000303|PubMed:8685262};
GN Synonyms=PFN2 {ECO:0000303|PubMed:8771785}, PRO2 {ECO:0000305};
GN OrderedLocusNames=At4g29350 {ECO:0000312|Araport:AT4G29350};
GN ORFNames=F17A13.170 {ECO:0000312|EMBL:CAB79693.1};
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 / MRNA], 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 [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Flower;
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 [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [7]
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 [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 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 [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19200149; DOI=10.1111/j.1744-7909.2008.00781.x;
RA Wang F., Jing Y., Wang Z., Mao T., Samaj J., Yuan M., Ren H.;
RT "Arabidopsis profilin isoforms, PRF1 and PRF2 show distinctive binding
RT activities and subcellular distributions.";
RL J. Integr. Plant Biol. 51:113-121(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, AND
RP INDUCTION BY BREFELDIN A.
RX PubMed=21090759; DOI=10.1021/pr100690f;
RA Takac T., Pechan T., Richter H., Mueller J., Eck C., Boehm N., Obert B.,
RA Ren H., Niehaus K., Samaj J.;
RT "Proteomics on brefeldin A-treated Arabidopsis roots reveals profilin 2 as
RT a new protein involved in the cross-talk between vesicular trafficking and
RT the actin cytoskeleton.";
RL J. Proteome Res. 10:488-501(2011).
RN [12]
RP DISRUPTION PHENOTYPE.
RX PubMed=26160044; DOI=10.1186/s12870-015-0551-0;
RA Muessar K.J., Kandasamy M.K., McKinney E.C., Meagher R.B.;
RT "Arabidopsis plants deficient in constitutive class profilins reveal
RT independent and quantitative genetic effects.";
RL BMC Plant Biol. 15:177-177(2015).
RN [13]
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 [14]
RP FUNCTION.
RX PubMed=26578694; DOI=10.1093/pcp/pcv176;
RA Kijima S.T., Hirose K., Kong S.G., Wada M., Uyeda T.Q.;
RT "Distinct biochemical properties of Arabidopsis thaliana actin isoforms.";
RL Plant Cell Physiol. 57:46-56(2016).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=30056100; DOI=10.1016/j.bbagen.2018.07.028;
RA Park S.C., Kim I.R., Kim J.Y., Lee Y., Kim E.J., Jung J.H., Jung Y.J.,
RA Jang M.K., Lee J.R.;
RT "Molecular mechanism of Arabidopsis thaliana profilins as antifungal
RT proteins.";
RL Biochim. Biophys. Acta 1862:2545-2554(2018).
RN [16]
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:21090759). At high concentrations, profilin
CC prevents the polymerization of actin, whereas it enhances it at low
CC concentrations (PubMed:26996265, PubMed:16313636, PubMed:29861135). At
CC low concentrations, associates with the poly-proline motif of formins
CC to enhance actin filament elongation rate (PubMed:29861135). Binds G-
CC actin and poly-L-proline with low affinity in vitro (PubMed:19200149).
CC Binds ACT1, ACT7 and ACT11 and inhibits actin polymerization
CC (PubMed:26578694). May be involved in the cross-talk between vesicular
CC trafficking and the actin cytoskeleton (PubMed:21090759). At high
CC concentrations, profilin prevents the polymerization of actin, whereas
CC it enhances it at low concentrations (By similarity). Inhibits cell
CC growth of various pathogenic fungal strains (PubMed:30056100). May play
CC a role as antifungal proteins in the defense system against fungal
CC pathogen attacks (PubMed:30056100). {ECO:0000250|UniProtKB:P07737,
CC ECO:0000269|PubMed:16313636, ECO:0000269|PubMed:19200149,
CC ECO:0000269|PubMed:21090759, ECO:0000269|PubMed:26578694,
CC ECO:0000269|PubMed:26996265, ECO:0000269|PubMed:29861135,
CC ECO:0000269|PubMed:30056100}.
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 Endoplasmic reticulum {ECO:0000269|PubMed:19200149}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:21090759}. Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in vascular bundles of roots, hypocotyls,
CC cotyledons, leaves, sepals, petals, stamen filaments and stalks of
CC developing seeds (PubMed:8771785, PubMed:16361517). Expressed in leaf
CC epidermal cells, trichomes and stem epidermal cells (PubMed:19200149).
CC Detected in phloem exudates (at protein level) (PubMed:30056100).
CC {ECO:0000269|PubMed:16361517, ECO:0000269|PubMed:19200149,
CC ECO:0000269|PubMed:30056100, ECO:0000269|PubMed:8771785}.
CC -!- INDUCTION: Induced by treatment with brefeldin A.
CC {ECO:0000269|PubMed:21090759}.
CC -!- DISRUPTION PHENOTYPE: Defects in rosette leaf and inflorescence
CC development. {ECO:0000269|PubMed:26160044}.
CC -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR EMBL; U43326; AAB39481.1; -; mRNA.
DR EMBL; U43323; AAB39478.1; -; Genomic_DNA.
DR EMBL; U43591; AAG10088.1; -; mRNA.
DR EMBL; AL161574; CAB79693.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85620.1; -; Genomic_DNA.
DR EMBL; AY074350; AAL67046.1; -; mRNA.
DR EMBL; AY114048; AAM45096.1; -; mRNA.
DR EMBL; AK319124; BAH57239.1; -; mRNA.
DR EMBL; AY086576; AAM63638.1; -; mRNA.
DR PIR; E85342; E85342.
DR RefSeq; NP_194664.1; NM_119080.4.
DR PDB; 6IQI; X-ray; 2.40 A; A/B=1-131.
DR PDB; 6IQJ; X-ray; 1.92 A; A/B=1-131.
DR PDBsum; 6IQI; -.
DR PDBsum; 6IQJ; -.
DR AlphaFoldDB; Q42418; -.
DR SMR; Q42418; -.
DR BioGRID; 14343; 7.
DR IntAct; Q42418; 3.
DR STRING; 3702.AT4G29350.1; -.
DR PaxDb; Q42418; -.
DR PRIDE; Q42418; -.
DR ProteomicsDB; 226374; -.
DR EnsemblPlants; AT4G29350.1; AT4G29350.1; AT4G29350.
DR GeneID; 829056; -.
DR Gramene; AT4G29350.1; AT4G29350.1; AT4G29350.
DR KEGG; ath:AT4G29350; -.
DR Araport; AT4G29350; -.
DR TAIR; locus:2118324; AT4G29350.
DR eggNOG; KOG1755; Eukaryota.
DR HOGENOM; CLU_120772_0_1_1; -.
DR InParanoid; Q42418; -.
DR OMA; CEVEGNH; -.
DR OrthoDB; 1428600at2759; -.
DR PhylomeDB; Q42418; -.
DR PRO; PR:Q42418; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q42418; baseline and differential.
DR Genevisible; Q42418; AT.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; TAS:TAIR.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0003785; F:actin monomer binding; IBA:GO_Central.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IDA:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0010229; P:inflorescence development; IMP:TAIR.
DR GO; GO:0048527; P:lateral root development; IMP:TAIR.
DR GO; GO:0048366; P:leaf development; IMP: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 3D-structure; Actin-binding; Cytoplasm; Cytoskeleton;
KW Endoplasmic reticulum; Nucleus; Plant defense; Reference proteome.
FT CHAIN 1..131
FT /note="Profilin-2"
FT /id="PRO_0000199616"
FT CONFLICT 110
FT /note="M -> V (in Ref. 2; AAG10088)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="V -> F (in Ref. 2; AAG10088)"
FT /evidence="ECO:0000305"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:6IQJ"
FT STRAND 21..27
FT /evidence="ECO:0007829|PDB:6IQJ"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:6IQJ"
FT HELIX 44..55
FT /evidence="ECO:0007829|PDB:6IQJ"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:6IQJ"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:6IQJ"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:6IQJ"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:6IQJ"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:6IQJ"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:6IQJ"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:6IQJ"
FT HELIX 112..128
FT /evidence="ECO:0007829|PDB:6IQJ"
SQ SEQUENCE 131 AA; 13998 MW; 181918B3EA05B62A CRC64;
MSWQSYVDDH LMCEVEGNHL THAAIFGQDG SVWAQSSAFP QLKPAEIAGI NKDFEEAGHL
APTGLFLGGE KYMVVQGEAG AVIRGKKGPG GVTIKKTTQA LVFGIYDEPM TGGQCNLVVE
RLGDYLIESG L
