EPFL5_ARATH
ID EPFL5_ARATH Reviewed; 107 AA.
AC Q9LUH9;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=EPIDERMAL PATTERNING FACTOR-like protein 5 {ECO:0000303|PubMed:19435754};
DE Short=EPF-like protein 5;
DE Contains:
DE RecName: Full=CHALLAH-LIKE1 {ECO:0000303|PubMed:21862708};
DE Flags: Precursor;
GN Name=EPFL5 {ECO:0000303|PubMed:19435754};
GN Synonyms=CLL1 {ECO:0000303|PubMed:21862708};
GN OrderedLocusNames=At3g22820 {ECO:0000312|Araport:AT3G22820};
GN ORFNames=MWI23.19;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [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, TISSUE SPECIFICITY, AND INTERACTION WITH ERECTA.
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 FUNCTION, AND TISSUE SPECIFICITY.
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 [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DISULFIDE BOND.
RC STRAIN=cv. Columbia;
RX PubMed=23748792; DOI=10.1271/bbb.130145;
RA Niwa T., Kondo T., Nishizawa M., Kajita R., Kakimoto T., Ishiguro S.;
RT "EPIDERMAL PATTERNING FACTOR LIKE5 peptide represses stomatal development
RT by inhibiting meristemoid maintenance in Arabidopsis thaliana.";
RL Biosci. Biotechnol. Biochem. 77:1287-1295(2013).
CC -!- FUNCTION: Controls stomatal patterning. Mediates differentiation of
CC stomatal lineage cells to pavement cells and stomatal development
CC inhibition (PubMed:23748792). TMM (AC Q9SSD1) functions to dampen or
CC block CLL1 signaling. Acts as growth-regulatory ligand for ERECTA
CC family receptors. Promotes fruit growth and fertility
CC (PubMed:22474391). {ECO:0000269|PubMed:19435754,
CC ECO:0000269|PubMed:21862708, ECO:0000269|PubMed:22474391,
CC ECO:0000269|PubMed:23748792}.
CC -!- SUBUNIT: Interacts with ERECTA. {ECO:0000269|PubMed:21862708}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed asymetically in the hypocotyl, on the
CC side proximal to the folded cotyledons at germination. Detected in
CC developing flowers, the chalazal region of ovules and near the root
CC apex, but not in inflorescence stems. Expressed in cotyledons, flowers,
CC adult leaves and fruits (PubMed:23748792).
CC {ECO:0000269|PubMed:21862708, ECO:0000269|PubMed:22474391,
CC ECO:0000269|PubMed:23748792}.
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; AB022223; BAB01257.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76680.1; -; Genomic_DNA.
DR EMBL; BT012590; AAT06409.1; -; mRNA.
DR EMBL; BT014813; AAT41796.1; -; mRNA.
DR RefSeq; NP_188921.1; NM_113181.4.
DR AlphaFoldDB; Q9LUH9; -.
DR STRING; 3702.AT3G22820.1; -.
DR PaxDb; Q9LUH9; -.
DR PRIDE; Q9LUH9; -.
DR EnsemblPlants; AT3G22820.1; AT3G22820.1; AT3G22820.
DR GeneID; 821853; -.
DR Gramene; AT3G22820.1; AT3G22820.1; AT3G22820.
DR KEGG; ath:AT3G22820; -.
DR Araport; AT3G22820; -.
DR TAIR; locus:2094424; AT3G22820.
DR eggNOG; ENOG502S3SX; Eukaryota.
DR HOGENOM; CLU_135272_3_3_1; -.
DR InParanoid; Q9LUH9; -.
DR OrthoDB; 1489306at2759; -.
DR PhylomeDB; Q9LUH9; -.
DR PRO; PR:Q9LUH9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LUH9; 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 Developmental protein; Disulfide bond; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..107
FT /note="EPIDERMAL PATTERNING FACTOR-like protein 5"
FT /id="PRO_0000392503"
FT CHAIN 57..107
FT /note="CHALLAH-LIKE1"
FT /evidence="ECO:0000303|PubMed:22027592"
FT /id="PRO_0000430511"
FT DISULFID 64..98
FT /evidence="ECO:0000269|PubMed:23748792"
FT DISULFID 68..74
FT /evidence="ECO:0000269|PubMed:23748792"
FT DISULFID 71..100
FT /evidence="ECO:0000269|PubMed:23748792"
SQ SEQUENCE 107 AA; 11505 MW; C5F5E71358745F3A CRC64;
MGVVLPTLIV YAFLLFFSSS SAASLQRPSG GLGQGKKEIA RSGLPGQIVD QKRLGGPGSV
PPMCRLKCGK CEPCKAVHVP IQPGLIMPLE YYPEAWRCKC GNKLFMP
