PRF3_ARATH
ID PRF3_ARATH Reviewed; 168 AA.
AC Q9FE63; B3H795; C0Z2Z0; Q8H123; Q8H2C7;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2020, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Profilin-3 {ECO:0000303|PubMed:8685262};
DE AltName: Full=AtPRF3 {ECO:0000303|PubMed:29861135};
DE AltName: Full=AthPRF3 {ECO:0000303|PubMed:8685262};
GN Name=PRF3 {ECO:0000303|PubMed:23052593}; Synonyms=PRO5 {ECO:0000305};
GN OrderedLocusNames=At5g56600 {ECO:0000312|Araport:AT5G56600};
GN ORFNames=MIK19.4 {ECO:0000312|EMBL:BAB09877.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-168 (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-168 (ISOFORM 2).
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-168.
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 [7]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF 1-MET--ASN-37.
RX PubMed=23052593; DOI=10.1007/s00299-012-1349-2;
RA Fan T., Zhai H., Shi W., Wang J., Jia H., Xiang Y., An L.;
RT "Overexpression of profilin 3 affects cell elongation and F-actin
RT organization in Arabidopsis thaliana.";
RL Plant Cell Rep. 32:149-160(2013).
RN [8]
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 [9]
RP FUNCTION, AND INDUCTION BY HYDROGEN SULFIDE.
RX PubMed=25652660; DOI=10.1038/srep08251;
RA Jia H., Hu Y., Fan T., Li J.;
RT "Hydrogen sulfide modulates actin-dependent auxin transport via regulating
RT ABPs results in changing of root development in Arabidopsis.";
RL Sci. Rep. 5:8251-8251(2015).
RN [10]
RP FUNCTION, SUBUNIT, INDUCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 1-MET--ASN-37.
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:23052593, PubMed:29861135). Can increase the
CC critical concentration (Cc) of actin assembly in vitro
CC (PubMed:23052593). Acts as downstream effector of the hydrogen sulfide
CC signaling to regulate the assembly and depolymerization of F-actin
CC (PubMed:25652660). At high concentrations, profilin prevents the
CC polymerization of actin, whereas it enhances it at low concentrations
CC (Probable). Binding to the poly-proline motif of formin induces
CC oligomerization of PRF3 (PubMed:29861135). PRF3 oligomers inhibit
CC formin-mediated actin assembly to modulate plant immunity triggered by
CC pathogen-associated molecular patterns (PAMPs) (PubMed:29861135).
CC {ECO:0000269|PubMed:23052593, ECO:0000269|PubMed:25652660,
CC ECO:0000269|PubMed:29861135, ECO:0000305|PubMed:29861135}.
CC -!- SUBUNIT: Occurs in many kinds of cells as a complex with monomeric
CC actin in a 1:1 ratio (Probable). Binding to the poly-proline motif of
CC formins induces formation of oligomers through the N-terminal
CC hydrophobic residues of PRF3 (PubMed:29861135).
CC {ECO:0000269|PubMed:29861135, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FE63-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FE63-2; Sequence=VSP_042421;
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette leaves, cauline leaves,
CC stems and flowers. {ECO:0000269|PubMed:23052593}.
CC -!- INDUCTION: Induced by hydrogen sulfide (PubMed:25652660). Down-
CC regulated by treatment with the flagellin peptide flg22 elicitor
CC (PubMed:29861135). {ECO:0000269|PubMed:25652660,
CC ECO:0000269|PubMed:29861135}.
CC -!- DISRUPTION PHENOTYPE: Slight elongation of leaf petioles
CC (PubMed:26160044). Increased length of primary roots in seedlings
CC (PubMed:29861135). {ECO:0000269|PubMed:26160044,
CC ECO:0000269|PubMed:29861135}.
CC -!- MISCELLANEOUS: Plants overexpressing PRF3 exhibit a dwarf phenotype
CC with delayed seed germination, reduced lengths of roots and hypocotyls,
CC and inhibition of hypocotyl cell elongation due to F-actin
CC rearrangement. {ECO:0000269|PubMed:23052593}.
CC -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG10089.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM60876.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AED96785.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AED96786.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB09877.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAH57069.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U43592; AAG10089.1; ALT_INIT; mRNA.
DR EMBL; AB013392; BAB09877.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED96785.2; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED96786.2; ALT_INIT; Genomic_DNA.
DR EMBL; AY034989; AAK59494.2; -; mRNA.
DR EMBL; BT000885; AAN41285.1; -; mRNA.
DR EMBL; AK318954; BAH57069.1; ALT_INIT; mRNA.
DR EMBL; AY084285; AAM60876.1; ALT_INIT; mRNA.
DR RefSeq; NP_001119446.2; NM_001125974.2.
DR RefSeq; NP_200471.3; NM_125043.4.
DR PDB; 6IQF; X-ray; 1.46 A; A=1-131.
DR PDB; 6IQK; X-ray; 3.60 A; A/B/C/D/E/F/G/H/I/J=1-131.
DR PDBsum; 6IQF; -.
DR PDBsum; 6IQK; -.
DR AlphaFoldDB; Q9FE63; -.
DR SMR; Q9FE63; -.
DR BioGRID; 21005; 5.
DR IntAct; Q9FE63; 3.
DR STRING; 3702.AT5G56600.1; -.
DR PaxDb; Q9FE63; -.
DR PRIDE; Q9FE63; -.
DR ProteomicsDB; 226505; -. [Q9FE63-1]
DR EnsemblPlants; AT5G56600.1; AT5G56600.1; AT5G56600.
DR GeneID; 835761; -.
DR Gramene; AT5G56600.1; AT5G56600.1; AT5G56600.
DR KEGG; ath:AT5G56600; -.
DR Araport; AT5G56600; -.
DR eggNOG; KOG1755; Eukaryota.
DR HOGENOM; CLU_120772_0_0_1; -.
DR InParanoid; Q9FE63; -.
DR OrthoDB; 1428600at2759; -.
DR PhylomeDB; Q9FE63; -.
DR PRO; PR:Q9FE63; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FE63; baseline and differential.
DR Genevisible; Q9FE63; AT.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0003785; F:actin monomer binding; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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 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; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Plant defense; Reference proteome.
FT CHAIN 1..168
FT /note="Profilin-3"
FT /id="PRO_0000199619"
FT REGION 14..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 125..167
FT /note="GAGGVTIKKTTLALVFGIYDEPMTPGQCNMVVENLGEYLIESG -> VTRLF
FT EYCLIFDELLLILLP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_042421"
FT MUTAGEN 1..37
FT /note="Missing: Increases binding to G-actin; increases
FT protein thermostability."
FT /evidence="ECO:0000269|PubMed:23052593,
FT ECO:0000269|PubMed:29861135"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:6IQF"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:6IQF"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:6IQF"
FT HELIX 81..92
FT /evidence="ECO:0007829|PDB:6IQF"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:6IQF"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:6IQF"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:6IQF"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:6IQF"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:6IQF"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:6IQF"
FT STRAND 135..143
FT /evidence="ECO:0007829|PDB:6IQF"
FT HELIX 149..165
FT /evidence="ECO:0007829|PDB:6IQF"
SQ SEQUENCE 168 AA; 18282 MW; 8A41CC1627842A54 CRC64;
MPLPHTHSLV VSTLSLEHSD KPQRRSRAKV KKKKKTNMSW QTYVDDHLMC DVAGNRLTAA
AILGQDGSVW AQSNNFPQVK PEEIQGIKDD FTTPGTLAPT GLFLGGNKYM VIQGEPNAVI
RGKKGAGGVT IKKTTLALVF GIYDEPMTPG QCNMVVENLG EYLIESGL
