CFL1_ARATH
ID CFL1_ARATH Reviewed; 189 AA.
AC Q5HZ54; O22801; Q84W47;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Protein CURLY FLAG LEAF 1 {ECO:0000303|PubMed:21954461};
DE Short=AtCFL1 {ECO:0000303|PubMed:21954461, ECO:0000303|PubMed:26745719};
GN Name=CFL1 {ECO:0000303|PubMed:21954461};
GN OrderedLocusNames=At2g33510 {ECO:0000312|Araport:AT2G33510};
GN ORFNames=F4P9.28 {ECO:0000312|EMBL:AAB80668.1};
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=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 [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].
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].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INTERACTION WITH HDG1, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=21954461; DOI=10.1105/tpc.111.088625;
RA Wu R., Li S., He S., Wassmann F., Yu C., Qin G., Schreiber L., Qu L.-J.,
RA Gu H.;
RT "CFL1, a WW domain protein, regulates cuticle development by modulating the
RT function of HDG1, a class IV homeodomain transcription factor, in rice and
RT Arabidopsis.";
RL Plant Cell 23:3392-3411(2011).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH BHLH122/CFLAP1 AND
RP BHLH80/CFLAP2.
RC STRAIN=cv. Columbia;
RX PubMed=26745719; DOI=10.1371/journal.pgen.1005744;
RA Li S., Wang X., He S., Li J., Huang Q., Imaizumi T., Qu L., Qin G.,
RA Qu L.-J., Gu H.;
RT "CFLAP1 and CFLAP2 are two bHLH transcription factors participating in
RT synergistic regulation of AtCFL1-mediated cuticle development in
RT Arabidopsis.";
RL PLoS Genet. 12:e1005744-e1005744(2016).
CC -!- FUNCTION: Regulates negatively the cuticle development by interacting
CC with the HD-ZIP IV transcription factor HDG1.
CC {ECO:0000269|PubMed:21954461, ECO:0000269|PubMed:26745719}.
CC -!- SUBUNIT: Interacts with BHLH122/CFLAP1 and BHLH80/CFLAP2
CC (PubMed:26745719). Binds to HDG1 (PubMed:21954461).
CC {ECO:0000269|PubMed:21954461, ECO:0000269|PubMed:26745719}.
CC -!- TISSUE SPECIFICITY: Mostly observed in roots, flowers and siliques
CC (PubMed:21954461). Expressed in cells differentiated from epidermal
CC cells such as trichomes, stigmatic papillar cells and guard cells, as
CC well as in tissues undergoing abscission and dehiscence
CC (PubMed:21954461). {ECO:0000269|PubMed:21954461}.
CC -!- DEVELOPMENTAL STAGE: Expressed in seedlings and all organs of adult
CC plants (PubMed:21954461). In roots, present in endodermis and central
CC cylinder (PubMed:21954461). In flowers, detected in stigmatic papillar
CC cells (PubMed:21954461). When petals and sepals are withering,
CC accumulates in the abscission zone at the bottom of the silique
CC (PubMed:21954461). Later observed along the valve margin-replum
CC boundary, where dehiscence and pod shatter occur (PubMed:21954461).
CC {ECO:0000269|PubMed:21954461}.
CC -!- DISRUPTION PHENOTYPE: Increased cuticle development leading to ectopic
CC cuticle biosynthesis in trichomes. {ECO:0000269|PubMed:26745719}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB80668.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC002332; AAB80668.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC08846.1; -; Genomic_DNA.
DR EMBL; BT004232; AAO42247.1; -; mRNA.
DR EMBL; BT020470; AAW38971.1; -; mRNA.
DR PIR; D84746; D84746.
DR RefSeq; NP_180909.2; NM_128911.3.
DR SMR; Q5HZ54; -.
DR PRIDE; Q5HZ54; -.
DR ProteomicsDB; 185762; -.
DR EnsemblPlants; AT2G33510.1; AT2G33510.1; AT2G33510.
DR GeneID; 817916; -.
DR Gramene; AT2G33510.1; AT2G33510.1; AT2G33510.
DR Araport; AT2G33510; -.
DR OMA; TADVCPK; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q5HZ54; baseline and differential.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR InterPro; IPR012682; Tscrpt_reg_Myc_N.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF01056; Myc_N; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..189
FT /note="Protein CURLY FLAG LEAF 1"
FT /id="PRO_0000456302"
FT DOMAIN 57..91
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT MOTIF 50..55
FT /note="EAR"
FT /evidence="ECO:0000250|UniProtKB:Q9SRN4"
FT CONFLICT 88
FT /note="D -> G (in Ref. 3; AAO42247)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 189 AA; 21568 MW; 2C71E33A2D1DD24D CRC64;
MKAPNMETIT ESLEKSMMNC SLNDRRRRVV GDGFGRSSSN EHMTPISDRT LELNSHLSLP
CHWEQCLDLK TGEIYYINWK NGMRVKEDPR KVMNADPDSG DSYGTVCSEE DSSYYDSEES
SSESSPSSRE NHKEEEEEEE EEEEEEEDVL VVAGCKACFM YFMVPKLVED CPKCAAQLLH
FDRPHSASS
