EPF2_ARATH
ID EPF2_ARATH Reviewed; 120 AA.
AC Q8LC53;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Protein EPIDERMAL PATTERNING FACTOR 2 {ECO:0000303|PubMed:19435754};
DE Contains:
DE RecName: Full=MEPF2 {ECO:0000303|PubMed:22241782};
DE Flags: Precursor;
GN Name=EPF2 {ECO:0000303|PubMed:19435754};
GN OrderedLocusNames=At1g34245 {ECO:0000312|Araport:AT1G34245};
GN ORFNames=F23M19;
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, DISRUPTION
RP PHENOTYPE, 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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;
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19398336; DOI=10.1016/j.cub.2009.03.069;
RA Hunt L., Gray J.E.;
RT "The signaling peptide EPF2 controls asymmetric cell divisions during
RT stomatal development.";
RL Curr. Biol. 19:864-869(2009).
RN [6]
RP FUNCTION, 3D-STRUCTURE MODELING, DISULFIDE BOND, AND DOMAIN.
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, AND INTERACTION WITH ERECTA; ERL1 AND TMM.
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 [8]
RP INDUCTION BY CO(2), CLEAVAGE BY CRSP, MUTAGENESIS OF 69-THR--CYS-80, AND
RP DISRUPTION PHENOTYPE.
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 the number of cells
CC that enter, and remain in, the stomatal lineage by inhibiting
CC protodermal cells from adopting the meristemoid mother cell (MMC) fate
CC in a non-cell-autonomous manner. Mediates stomatal development
CC inhibition. MEPF2: mobile signal controlling stomatal development in a
CC non-cell-autonomous manner (PubMed:22241782). Uses ERECTA as major
CC receptor (PubMed:22241782). Inactivated by cleavage by CRSP (AC Q9LNU1)
CC (PubMed:25043023). May act by competing with somatogen (AC Q9SV72) for
CC the same receptor, TMM (AC Q9SSD1) (PubMed:22027592).
CC {ECO:0000269|PubMed:19398336, ECO:0000269|PubMed:19435754,
CC ECO:0000269|PubMed:22241782, ECO:0000269|PubMed:25043023,
CC ECO:0000303|PubMed:22027592}.
CC -!- SUBUNIT: Interacts with ERECTA, ERL1 and TMM.
CC {ECO:0000269|PubMed:22241782}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, especially by the MMCs and
CC their early descendants cells (stomatal lineage cells) including guard
CC mother cells (GMCs). {ECO:0000269|PubMed:19398336,
CC ECO:0000269|PubMed:19435754}.
CC -!- INDUCTION: Induced by high CO(2). {ECO:0000269|PubMed:25043023}.
CC -!- DOMAIN: The loop (92-105) connecting the two anti-parallel beta-strands
CC (85-91 and 106-112) confers the function to the peptide.
CC {ECO:0000269|PubMed:22027592}.
CC -!- DISRUPTION PHENOTYPE: Increased small pavement cell (non-stomatal) and
CC stomatal cell density. Inversion in CO(2) control of stomatal
CC development resulting in an increased number of stomata at elevated
CC CO(2) concentration. {ECO:0000269|PubMed:19398336,
CC ECO:0000269|PubMed:19435754, ECO:0000269|PubMed:25043023}.
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; AB499311; BAH58781.1; -; mRNA.
DR EMBL; AC007454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE31689.1; -; Genomic_DNA.
DR EMBL; AY086790; AAM63840.1; -; mRNA.
DR RefSeq; NP_564442.1; NM_103147.3.
DR PDB; 5XKJ; X-ray; 3.48 A; E/F=69-120.
DR PDBsum; 5XKJ; -.
DR AlphaFoldDB; Q8LC53; -.
DR SMR; Q8LC53; -.
DR BioGRID; 25556; 3.
DR STRING; 3702.AT1G34245.1; -.
DR PaxDb; Q8LC53; -.
DR PRIDE; Q8LC53; -.
DR EnsemblPlants; AT1G34245.1; AT1G34245.1; AT1G34245.
DR GeneID; 840324; -.
DR Gramene; AT1G34245.1; AT1G34245.1; AT1G34245.
DR KEGG; ath:AT1G34245; -.
DR Araport; AT1G34245; -.
DR TAIR; locus:505006168; AT1G34245.
DR eggNOG; ENOG502S55W; Eukaryota.
DR HOGENOM; CLU_135272_1_0_1; -.
DR InParanoid; Q8LC53; -.
DR OMA; VIYRCTC; -.
DR OrthoDB; 1615631at2759; -.
DR PhylomeDB; Q8LC53; -.
DR PRO; PR:Q8LC53; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LC53; baseline and differential.
DR Genevisible; Q8LC53; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0019901; F:protein kinase binding; IPI:TAIR.
DR GO; GO:0010052; P:guard cell differentiation; IMP:TAIR.
DR GO; GO:2000122; P:negative regulation of stomatal complex development; IMP:TAIR.
DR GO; GO:0090626; P:plant epidermis morphogenesis; IMP:TAIR.
DR GO; GO:0010374; P:stomatal complex development; IMP:TAIR.
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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..120
FT /note="Protein EPIDERMAL PATTERNING FACTOR 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000392498"
FT CHAIN 69..120
FT /note="MEPF2"
FT /evidence="ECO:0000303|PubMed:22027592"
FT /id="PRO_0000430506"
FT DISULFID 76..107
FT /evidence="ECO:0000303|PubMed:22027592"
FT DISULFID 80..86
FT /evidence="ECO:0000303|PubMed:22027592"
FT DISULFID 83..109
FT /evidence="ECO:0000303|PubMed:22027592"
FT DISULFID 95..101
FT /evidence="ECO:0000269|PubMed:22027592"
FT MUTAGEN 69..80
FT /note="TGSSLPDCSYAC->IGSTAPTCTYNE: Loss of cleavage by
FT CRSP."
FT /evidence="ECO:0000269|PubMed:25043023"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:5XKJ"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:5XKJ"
FT STRAND 103..113
FT /evidence="ECO:0007829|PDB:5XKJ"
SQ SEQUENCE 120 AA; 13317 MW; BDA520F3DC3BECCE CRC64;
MTKFVRKYMF CLVLVFAACS LVVNSIRTPP LKNTVNGGEK KNADIEQAQT HHKKEISKNG
GVEMEMYPTG SSLPDCSYAC GACSPCKRVM ISFECSVAES CSVIYRCTCR GRYYHVPSRA
