EPFL6_ARATH
ID EPFL6_ARATH Reviewed; 156 AA.
AC Q1PEY6; O22933;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=EPIDERMAL PATTERNING FACTOR-like protein 6 {ECO:0000303|PubMed:19435754};
DE Short=EPF-like protein 6;
DE Contains:
DE RecName: Full=CHALLAH {ECO:0000303|PubMed:22027592};
DE Flags: Precursor;
GN Name=EPFL6 {ECO:0000303|PubMed:19435754};
GN Synonyms=CHAL {ECO:0000303|PubMed:20056678};
GN OrderedLocusNames=At2g30370 {ECO:0000312|Araport:AT2G30370};
GN ORFNames=T9D9.18;
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] (ISOFORM 1).
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 [4]
RP 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 [5]
RP FUNCTION, MUTAGENESIS OF PRO-122, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=20056678; DOI=10.1242/dev.040931;
RA Abrash E.B., Bergmann D.C.;
RT "Regional specification of stomatal production by the putative ligand
RT CHALLAH.";
RL Development 137:447-455(2010).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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 [7]
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 [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 EPFL4 in
CC procambial development regulation. Acts also as tissue-specific
CC regulator of epidermal pattern. Controls stomatal patterning by
CC repressing stomatal production. TMM (AC Q9SSD1) functions to dampen or
CC block CHAL signaling. Not processed by SDD1 (AC O64495). Acts as
CC growth-regulatory ligand for ERECTA family receptors.
CC {ECO:0000269|PubMed:20056678, ECO:0000269|PubMed:21862708,
CC ECO:0000269|PubMed:22474391, ECO:0000269|PubMed:23881395}.
CC -!- SUBUNIT: Interacts with ERECTA. {ECO:0000269|PubMed:22474391}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q1PEY6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q1PEY6-2; Sequence=VSP_038808;
CC -!- TISSUE SPECIFICITY: Expressed in the internal layers of the root,
CC hypocotyl and stems, and in the midrib of developing rosette leaves.
CC Detected in a ring of cells surrounding the vascular elements.
CC Expressed in developing stems soon after bolting, in inflorescence
CC stems, near the root apex and in the chalazal region of ovules. Not
CC found in cotyledons or in stomatal precursors or stomata.
CC {ECO:0000269|PubMed:20056678, ECO:0000269|PubMed:21862708,
CC ECO:0000269|PubMed:22027592}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype in wild-type background, but
CC restores stomata to hypocotyls in a tmm background. Chal and cll2
CC double mutants are defective in growth, with a short stature, shortened
CC pedicells and compact inflorescence. {ECO:0000269|PubMed:20056678,
CC ECO:0000269|PubMed:21862708, 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; AC002338; AAC16939.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08377.1; -; Genomic_DNA.
DR EMBL; DQ446581; ABE65875.1; -; mRNA.
DR PIR; F84707; F84707.
DR RefSeq; NP_001189638.1; NM_001202709.2. [Q1PEY6-1]
DR AlphaFoldDB; Q1PEY6; -.
DR BioGRID; 2936; 4.
DR IntAct; Q1PEY6; 1.
DR PaxDb; Q1PEY6; -.
DR EnsemblPlants; AT2G30370.2; AT2G30370.2; AT2G30370. [Q1PEY6-1]
DR GeneID; 817587; -.
DR Gramene; AT2G30370.2; AT2G30370.2; AT2G30370. [Q1PEY6-1]
DR KEGG; ath:AT2G30370; -.
DR Araport; AT2G30370; -.
DR eggNOG; ENOG502S3PD; Eukaryota.
DR HOGENOM; CLU_135272_3_1_1; -.
DR InParanoid; Q1PEY6; -.
DR PRO; PR:Q1PEY6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q1PEY6; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0010052; P:guard cell differentiation; ISS:UniProtKB.
DR GO; GO:0010374; P:stomatal complex development; ISS:UniProtKB.
DR InterPro; IPR039455; EPFL.
DR PANTHER; PTHR33109; PTHR33109; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Disulfide bond;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..47
FT /evidence="ECO:0000255"
FT CHAIN 48..156
FT /note="EPIDERMAL PATTERNING FACTOR-like protein 6"
FT /id="PRO_0000392504"
FT CHAIN 106..156
FT /note="CHALLAH"
FT /evidence="ECO:0000303|PubMed:22027592"
FT /id="PRO_0000430512"
FT DISULFID 113..147
FT /evidence="ECO:0000303|PubMed:22027592"
FT DISULFID 117..123
FT /evidence="ECO:0000303|PubMed:22027592"
FT DISULFID 120..149
FT /evidence="ECO:0000303|PubMed:22027592"
FT VAR_SEQ 60..156
FT /note="YNRNSNSGTLGNFYAKEEGKSTVVIKKTRKIGDRSKEAELRRILRGLGSSPP
FT RCSSKCGRCTPCKPVHVPVPPGTPVTAEYYPEAWRCKCGNKLYMP -> FSDCDGMSRL
FT TGHAEMPCTPKEILSRRIGFSAHEDKDSTQLLVRSPLVGPCLAYDLDRVVILAPTVHVN
FT V (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038808"
FT MUTAGEN 122
FT /note="P->S: In chal-1; derepress stomatal production in a
FT specific subset of tissues."
FT /evidence="ECO:0000269|PubMed:20056678"
SQ SEQUENCE 156 AA; 17180 MW; FFDD8704837BDCEB CRC64;
MGFERTSSSL SLLSSSLPSS LQPSENTRAK FSLFYLLLLF FVLCVIATFT ITPTSTSSPY
NRNSNSGTLG NFYAKEEGKS TVVIKKTRKI GDRSKEAELR RILRGLGSSP PRCSSKCGRC
TPCKPVHVPV PPGTPVTAEY YPEAWRCKCG NKLYMP
