EPFL4_ARATH
ID EPFL4_ARATH Reviewed; 109 AA.
AC Q2V3I3;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=EPIDERMAL PATTERNING FACTOR-like protein 4 {ECO:0000303|PubMed:19435754};
DE Short=EPF-like protein 4;
DE Contains:
DE RecName: Full=CHALLAH-LIKE2 {ECO:0000303|PubMed:21862708};
DE Flags: Precursor;
GN Name=EPFL4 {ECO:0000303|PubMed:19435754};
GN Synonyms=CLL2 {ECO:0000303|PubMed:21862708};
GN OrderedLocusNames=At4g14723 {ECO:0000312|Araport:AT4G14723};
GN ORFNames=FCAALL;
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [5]
RP FUNCTION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19435754; DOI=10.1093/pcp/pcp068;
RA Hara K., Yokoo T., Kajita R., Onishi T., Yahata S., Peterson K.M.,
RA Torii K.U., Kakimoto T.;
RT "Epidermal cell density is autoregulated via a secretory peptide, EPIDERMAL
RT PATTERNING FACTOR 2 in Arabidopsis leaves.";
RL Plant Cell Physiol. 50:1019-1031(2009).
RN [6]
RP 3D-STRUCTURE MODELING, AND DISULFIDE BOND.
RX PubMed=22027592; DOI=10.1038/ncomms1520;
RA Ohki S., Takeuchi M., Mori M.;
RT "The NMR structure of stomagen reveals the basis of stomatal density
RT regulation by plant peptide hormones.";
RL Nat. Commun. 2:512-512(2011).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=21862708; DOI=10.1105/tpc.111.086637;
RA Abrash E.B., Davies K.A., Bergmann D.C.;
RT "Generation of signaling specificity in Arabidopsis by spatially restricted
RT buffering of ligand-receptor interactions.";
RL Plant Cell 23:2864-2879(2011).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP ERECTA.
RX PubMed=22474391; DOI=10.1073/pnas.1117537109;
RA Uchida N., Lee J.S., Horst R.J., Lai H.H., Kajita R., Kakimoto T.,
RA Tasaka M., Torii K.U.;
RT "Regulation of inflorescence architecture by intertissue layer ligand-
RT receptor communication between endodermis and phloem.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:6337-6342(2012).
RN [9]
RP FUNCTION.
RX PubMed=23881395; DOI=10.1093/jxb/ert196;
RA Uchida N., Tasaka M.;
RT "Regulation of plant vascular stem cells by endodermis-derived EPFL-family
RT peptide hormones and phloem-expressed ERECTA-family receptor kinases.";
RL J. Exp. Bot. 64:5335-5343(2013).
CC -!- FUNCTION: Acts primarily as positive regulator of inflorescence growth.
CC Endodermal expression is sufficient for proper inflorescence
CC architecture (PubMed:22474391). Redundantly involved with EPFL6 in
CC procambial development regulation. Controls stomatal patterning.
CC Mediates stomatal development inhibition. TMM (AC Q9SSD1) functions to
CC dampen or block CLL2 signaling. Acts as growth-regulatory ligand for
CC ERECTA family receptors. {ECO:0000269|PubMed:19435754,
CC ECO:0000269|PubMed:21862708, ECO:0000269|PubMed:22474391,
CC ECO:0000269|PubMed:23881395}.
CC -!- SUBUNIT: Interacts with ERECTA. {ECO:0000269|PubMed:22474391}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed at the base of the apical meristem at 3
CC days after germination. Not detected in the hypocotyl. Expressed in
CC developing stems soon after bolting, in inflorescence stems and in
CC young siliques. {ECO:0000269|PubMed:21862708,
CC ECO:0000269|PubMed:22474391}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Chal and cll2 double
CC mutants are defective in growth, with a short stature, shortened
CC pedicells and compact inflorescence. {ECO:0000269|PubMed:21862708,
CC ECO:0000269|PubMed:22474391}.
CC -!- SIMILARITY: Belongs to the plant cysteine rich small secretory peptide
CC family. Epidermal patterning factor subfamily. {ECO:0000305}.
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DR EMBL; Z97336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z97337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002687; AEE83488.1; -; Genomic_DNA.
DR EMBL; DQ487600; ABF59246.1; -; mRNA.
DR RefSeq; NP_001031641.1; NM_001036564.4.
DR PDB; 5XKN; X-ray; 3.65 A; E/F=59-109.
DR PDBsum; 5XKN; -.
DR AlphaFoldDB; Q2V3I3; -.
DR SMR; Q2V3I3; -.
DR STRING; 3702.AT4G14723.1; -.
DR PaxDb; Q2V3I3; -.
DR PRIDE; Q2V3I3; -.
DR EnsemblPlants; AT4G14723.1; AT4G14723.1; AT4G14723.
DR GeneID; 3769880; -.
DR Gramene; AT4G14723.1; AT4G14723.1; AT4G14723.
DR KEGG; ath:AT4G14723; -.
DR Araport; AT4G14723; -.
DR TAIR; locus:1009023326; AT4G14723.
DR eggNOG; ENOG502S3SX; Eukaryota.
DR HOGENOM; CLU_135272_3_3_1; -.
DR OMA; WIGQRTG; -.
DR OrthoDB; 1489306at2759; -.
DR PhylomeDB; Q2V3I3; -.
DR PRO; PR:Q2V3I3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q2V3I3; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0010052; P:guard cell differentiation; IMP:UniProtKB.
DR GO; GO:0010374; P:stomatal complex development; IMP:UniProtKB.
DR InterPro; IPR039455; EPFL.
DR PANTHER; PTHR33109; PTHR33109; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Developmental protein; Disulfide bond; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..109
FT /note="EPIDERMAL PATTERNING FACTOR-like protein 4"
FT /id="PRO_0000392502"
FT CHAIN 59..109
FT /note="CHALLAH-LIKE2"
FT /evidence="ECO:0000303|PubMed:22027592"
FT /id="PRO_0000430510"
FT DISULFID 66..100
FT /evidence="ECO:0000303|PubMed:22027592"
FT DISULFID 70..76
FT /evidence="ECO:0000303|PubMed:22027592"
FT DISULFID 73..102
FT /evidence="ECO:0000303|PubMed:22027592"
SQ SEQUENCE 109 AA; 12057 MW; 89DE4EA3DFB8EE97 CRC64;
MGTFRRRRRF LLAALVTFAL LHLFSASSIV SADGRWIGQR TGSDLPGGFI RSNKRFGGPG
SSPPTCRSKC GKCQPCKPVH VPIQPGLSMP LEYYPEAWRC KCGNKLFMP
