PRF1_ARATH
ID PRF1_ARATH Reviewed; 131 AA.
AC Q42449;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=Profilin-1 {ECO:0000303|PubMed:8685262};
DE AltName: Full=AtPROF1 {ECO:0000305};
DE AltName: Full=AthPRF1 {ECO:0000303|PubMed:8685262};
DE AltName: Allergen=Ara t 8 {ECO:0000305};
GN Name=PRF1 {ECO:0000303|PubMed:8685262};
GN Synonyms=PFN1 {ECO:0000303|PubMed:8771785}, PRO1 {ECO:0000305};
GN OrderedLocusNames=At2g19760 {ECO:0000312|Araport:AT2G19760};
GN ORFNames=F6F22.21 {ECO:0000312|EMBL:AAC62140.1};
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 [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
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=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 [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 INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11340190; DOI=10.2307/3871372;
RA McKinney E.C., Kandasamy M.K., Meagher R.B.;
RT "Small changes in the regulation of one Arabidopsis profilin isovariant,
RT PRF1, alter seedling development.";
RL Plant Cell 13:1179-1191(2001).
RN [7]
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 [8]
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 [9]
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 [10]
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 [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26574597; DOI=10.1104/pp.15.01321;
RA Cao L., Henty-Ridilla J.L., Blanchoin L., Staiger C.J.;
RT "Profilin-dependent nucleation and assembly of actin filaments controls
RT cell elongation in Arabidopsis.";
RL Plant Physiol. 170:220-233(2016).
RN [12]
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 [13]
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).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS).
RX PubMed=9016723; DOI=10.1016/s0969-2126(97)00163-9;
RA Thorn K.S., Christensen H.E.M., Shigeta R. Jr., Hudler D. Jr., Shalaby L.,
RA Lindnerg U., Chua N.-H., Schutt C.E.;
RT "The crystal structure of a major allergen from plants.";
RL Structure 5:19-32(1997).
CC -!- FUNCTION: Binds to actin monomers and regulates the organization of the
CC actin cytoskeleton (PubMed:26574597). 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). Binds ACT1, ACT7 and ACT11 and
CC inhibits actin polymerization (PubMed:26578694). Coordinates the
CC stochastic dynamic properties of actin filaments by modulating formin-
CC mediated actin nucleation and assembly during axial cell expansion
CC (PubMed:26574597). Binds G-actin and poly-L-proline in vitro
CC (PubMed:19200149). Inhibits cell growth of various pathogenic fungal
CC strains (PubMed:30056100). May play a role as antifungal proteins in
CC the defense system against fungal pathogen attacks (PubMed:30056100).
CC {ECO:0000269|PubMed:19200149, ECO:0000269|PubMed:26574597,
CC ECO:0000269|PubMed:26578694, 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}. Cytoplasm
CC {ECO:0000269|PubMed:17933902, ECO:0000269|PubMed:19200149}.
CC Note=Probably associated with cytoplasmic actin filaments.
CC {ECO:0000269|PubMed:19200149}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels roots, leaves, stems,
CC flowers and siliques (PubMed:8771785, PubMed:8685262). Expressed in
CC leaf epidermal cells, trichomes and stem epidermal cells
CC (PubMed:19200149). Detected in phloem exudates (at protein level)
CC (PubMed:30056100). {ECO:0000269|PubMed:19200149,
CC ECO:0000269|PubMed:30056100, ECO:0000269|PubMed:8685262,
CC ECO:0000269|PubMed:8771785}.
CC -!- INDUCTION: Down-regulated by light. {ECO:0000269|PubMed:11340190}.
CC -!- DISRUPTION PHENOTYPE: Delayed germination (PubMed:11340190). In young
CC seedlings, excessive numbers of root hairs, abnormal raised cotyledons,
CC elongated hypocotyls, and elongated cells in the hypocotyl
CC (PubMed:11340190, PubMed:26574597). Defects in rosette leaf and
CC inflorescence development (PubMed:26160044).
CC {ECO:0000269|PubMed:11340190, ECO:0000269|PubMed:26160044,
CC ECO:0000269|PubMed:26574597}.
CC -!- ALLERGEN: Causes an allergic reaction in human. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the profilin family. {ECO:0000305}.
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DR EMBL; U43325; AAB39480.1; -; mRNA.
DR EMBL; U43322; AAB39476.1; -; Genomic_DNA.
DR EMBL; U43593; AAG10090.1; -; Genomic_DNA.
DR EMBL; U43590; AAB46750.1; -; mRNA.
DR EMBL; AC005169; AAC62140.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06923.1; -; Genomic_DNA.
DR EMBL; AY072427; AAL62419.1; -; mRNA.
DR EMBL; BT000264; AAN15583.1; -; mRNA.
DR PIR; G84580; G84580.
DR RefSeq; NP_179566.1; NM_127534.3.
DR PDB; 1A0K; X-ray; 2.20 A; A=1-131.
DR PDB; 3NUL; X-ray; 1.60 A; A=2-131.
DR PDBsum; 1A0K; -.
DR PDBsum; 3NUL; -.
DR AlphaFoldDB; Q42449; -.
DR SMR; Q42449; -.
DR BioGRID; 1850; 1.
DR IntAct; Q42449; 1.
DR STRING; 3702.AT2G19760.1; -.
DR PaxDb; Q42449; -.
DR PRIDE; Q42449; -.
DR ProteomicsDB; 226504; -.
DR EnsemblPlants; AT2G19760.1; AT2G19760.1; AT2G19760.
DR GeneID; 816495; -.
DR Gramene; AT2G19760.1; AT2G19760.1; AT2G19760.
DR KEGG; ath:AT2G19760; -.
DR Araport; AT2G19760; -.
DR TAIR; locus:2051965; AT2G19760.
DR eggNOG; KOG1755; Eukaryota.
DR HOGENOM; CLU_120772_0_1_1; -.
DR InParanoid; Q42449; -.
DR OMA; NETMSWQ; -.
DR OrthoDB; 1428600at2759; -.
DR PhylomeDB; Q42449; -.
DR EvolutionaryTrace; Q42449; -.
DR PRO; PR:Q42449; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q42449; baseline and differential.
DR Genevisible; Q42449; AT.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005819; C:spindle; 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 GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
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; Allergen; Cytoplasm; Cytoskeleton;
KW Plant defense; Reference proteome.
FT CHAIN 1..131
FT /note="Profilin-1"
FT /id="PRO_0000199615"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:3NUL"
FT STRAND 21..27
FT /evidence="ECO:0007829|PDB:3NUL"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:3NUL"
FT HELIX 44..55
FT /evidence="ECO:0007829|PDB:3NUL"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:3NUL"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:3NUL"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:3NUL"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:3NUL"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:3NUL"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:3NUL"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:3NUL"
FT HELIX 112..128
FT /evidence="ECO:0007829|PDB:3NUL"
SQ SEQUENCE 131 AA; 14266 MW; 84212D4681F83F51 CRC64;
MSWQSYVDDH LMCDVEGNHL TAAAILGQDG SVWAQSAKFP QLKPQEIDGI KKDFEEPGFL
APTGLFLGGE KYMVIQGEQG AVIRGKKGPG GVTIKKTNQA LVFGFYDEPM TGGQCNLVVE
RLGDYLIESE L
