EPF1_ARATH
ID EPF1_ARATH Reviewed; 104 AA.
AC Q8S8I4;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Protein EPIDERMAL PATTERNING FACTOR 1 {ECO:0000303|PubMed:17639078};
DE Contains:
DE RecName: Full=MEPF1 {ECO:0000303|PubMed:22241782};
DE Flags: Precursor;
GN Name=EPF1 {ECO:0000303|PubMed:17639078};
GN OrderedLocusNames=At2g20875 {ECO:0000312|Araport:AT2G20875};
GN ORFNames=F5H14 {ECO:0000312|EMBL:AAM15214.1};
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 FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17639078; DOI=10.1101/gad.1550707;
RA Hara K., Kajita R., Torii K.U., Bergmann D.C., Kakimoto T.;
RT "The secretory peptide gene EPF1 enforces the stomatal one-cell-spacing
RT rule.";
RL Genes Dev. 21:1720-1725(2007).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, GENE FAMILY, AND
RP 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 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 [6]
RP FUNCTION, AND INTERACTION WITH ERECTA AND ERL1.
RX PubMed=22241782; DOI=10.1101/gad.179895.111;
RA Lee J.S., Kuroha T., Hnilova M., Khatayevich D., Kanaoka M.M., McAbee J.M.,
RA Sarikaya M., Tamerler C., Torii K.U.;
RT "Direct interaction of ligand-receptor pairs specifying stomatal
RT patterning.";
RL Genes Dev. 26:126-136(2012).
RN [7]
RP LACK OF INDUCTION BY CO(2), LACK OF CLEAVAGE BY CRSP, AND FUNCTION.
RX PubMed=25043023; DOI=10.1038/nature13452;
RA Engineer C.B., Ghassemian M., Anderson J.C., Peck S.C., Hu H.,
RA Schroeder J.I.;
RT "Carbonic anhydrases, EPF2 and a novel protease mediate CO2 control of
RT stomatal development.";
RL Nature 513:246-250(2014).
CC -!- FUNCTION: Controls stomatal patterning. Regulates asymmetric cell
CC division during guard cell differentiation. Mediates stomatal
CC development inhibition. Not cleaved by the protease CRSP (AC Q9LNU1)
CC (PubMed:25043023). MEPF1: mobile signal controlling stomatal
CC development in a non-cell-autonomous manner (PubMed:22241782). Uses
CC ERL1 as major receptor (PubMed:22241782). May act by competing with
CC somatogen (AC Q9SV72) for the same receptor, TMM (AC Q9SSD1)
CC (PubMed:22027592). {ECO:0000269|PubMed:17639078,
CC ECO:0000269|PubMed:19435754, ECO:0000269|PubMed:22241782,
CC ECO:0000269|PubMed:25043023, ECO:0000303|PubMed:22027592}.
CC -!- SUBUNIT: Interacts with ERECTA and ERL1, but not with TMM.
CC {ECO:0000269|PubMed:22241782}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in shoots, but not in roots. Mostly
CC localized in developing leaves, specifically in meristemoids, guard
CC mother cells (GMCs), and young guard cells.
CC {ECO:0000269|PubMed:17639078, ECO:0000269|PubMed:19435754}.
CC -!- INDUCTION: Not induced by high CO(2). {ECO:0000269|PubMed:25043023}.
CC -!- DISRUPTION PHENOTYPE: Increased stomatal density and violation of the
CC one-cell-spacing rule (clustering of stomata).
CC {ECO:0000269|PubMed:17639078, ECO:0000269|PubMed:19435754}.
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; AC006234; AAM15214.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07090.1; -; Genomic_DNA.
DR RefSeq; NP_179684.1; NM_127657.4.
DR PDB; 5XJO; X-ray; 2.63 A; E/F=53-104.
DR PDBsum; 5XJO; -.
DR AlphaFoldDB; Q8S8I4; -.
DR SMR; Q8S8I4; -.
DR BioGRID; 1974; 2.
DR STRING; 3702.AT2G20875.1; -.
DR PaxDb; Q8S8I4; -.
DR PRIDE; Q8S8I4; -.
DR EnsemblPlants; AT2G20875.1; AT2G20875.1; AT2G20875.
DR GeneID; 816621; -.
DR Gramene; AT2G20875.1; AT2G20875.1; AT2G20875.
DR KEGG; ath:AT2G20875; -.
DR Araport; AT2G20875; -.
DR TAIR; locus:3436392; AT2G20875.
DR eggNOG; ENOG502S3VT; Eukaryota.
DR HOGENOM; CLU_135272_1_1_1; -.
DR OMA; HHHVGMM; -.
DR OrthoDB; 1424322at2759; -.
DR PhylomeDB; Q8S8I4; -.
DR PRO; PR:Q8S8I4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8S8I4; baseline and differential.
DR Genevisible; Q8S8I4; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0010052; P:guard cell differentiation; IBA:GO_Central.
DR GO; GO:2000122; P:negative regulation of stomatal complex development; IMP:TAIR.
DR GO; GO:0010374; P:stomatal complex development; IGI:TAIR.
DR GO; GO:0010375; P:stomatal complex patterning; IMP:TAIR.
DR InterPro; IPR039455; EPFL.
DR PANTHER; PTHR33109; PTHR33109; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Developmental protein; Disulfide bond; Glycoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..104
FT /note="Protein EPIDERMAL PATTERNING FACTOR 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000392497"
FT CHAIN 53..104
FT /note="MEPF1"
FT /evidence="ECO:0000303|PubMed:22027592"
FT /id="PRO_0000430505"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 60..94
FT /evidence="ECO:0000303|PubMed:22027592"
FT DISULFID 64..70
FT /evidence="ECO:0000303|PubMed:22027592"
FT DISULFID 67..96
FT /evidence="ECO:0000303|PubMed:22027592"
FT DISULFID 79..88
FT /evidence="ECO:0000269|PubMed:22027592"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:5XJO"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:5XJO"
SQ SEQUENCE 104 AA; 11444 MW; 1B7FC910706F78C1 CRC64;
MKSLLLLAFF LSFFFGSLLA RHLPTSSHPS HHHVGMTGAL KRQRRRPDTV QVAGSRLPDC
SHACGSCSPC RLVMVSFVCA SVEEAETCPM AYKCMCNNKS YPVP
