EPFL9_ARATH
ID EPFL9_ARATH Reviewed; 102 AA.
AC Q9SV72;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=EPIDERMAL PATTERNING FACTOR-like protein 9 {ECO:0000303|PubMed:19435754};
DE Short=EPF-like protein 9;
DE Contains:
DE RecName: Full=Stomagen {ECO:0000303|PubMed:20010603};
DE Flags: Precursor;
GN Name=EPFL9 {ECO:0000303|PubMed:19435754};
GN Synonyms=STOMAGEN {ECO:0000303|PubMed:20010603};
GN OrderedLocusNames=At4g12970 {ECO:0000312|Araport:AT4G12970};
GN ORFNames=F25G13.60;
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=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 [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 Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
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, PROTEIN SEQUENCE OF 58-67, PROCESSING, DISRUPTION PHENOTYPE, AND
RP TISSUE SPECIFICITY.
RX PubMed=20010603; DOI=10.1038/nature08682;
RA Sugano S.S., Shimada T., Imai Y., Okawa K., Tamai A., Mori M.,
RA Hara-Nishimura I.;
RT "Stomagen positively regulates stomatal density in Arabidopsis.";
RL Nature 463:241-244(2010).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, DISULFIDE BOND, AND SUBCELLULAR LOCATION.
RX PubMed=20007289; DOI=10.1093/pcp/pcp180;
RA Kondo T., Kajita R., Miyazaki A., Hokoyama M., Nakamura-Miura T.,
RA Mizuno S., Masuda Y., Irie K., Tanaka Y., Takada S., Kakimoto T.,
RA Sakagami Y.;
RT "Stomatal density is controlled by a mesophyll-derived signaling
RT molecule.";
RL Plant Cell Physiol. 51:1-8(2010).
RN [7]
RP FUNCTION, STRUCTURE BY NMR OF 58-102, DISULFIDE BOND, MUTAGENESIS OF
RP CYS-65; CYS-70; CYS-73; CYS-77; GLU-85; ASP-88; CYS-98 AND CYS-100, AND
RP 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 [8]
RP LACK OF CLEAVAGE.
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).
RN [9]
RP FUNCTION, AND INTERACTION WITH ERECTA AND TMM.
RX PubMed=26083750; DOI=10.1038/nature14561;
RA Lee J.S., Hnilova M., Maes M., Lin Y.C., Putarjunan A., Han S.K., Avila J.,
RA Torii K.U.;
RT "Competitive binding of antagonistic peptides fine-tunes stomatal
RT patterning.";
RL Nature 522:439-443(2015).
CC -!- FUNCTION: [Stomagen]: Positively regulates stomatal density and
CC patterning. Acts by competing with EPF2 (AC Q8LC53) for the same
CC receptors, ERECTA (AC Q42371) and TMM (AC Q9SSD1). Not cleaved by the
CC protease CRSP (AC Q9LNU1) (PubMed:25043023).
CC {ECO:0000269|PubMed:20007289, ECO:0000269|PubMed:20010603,
CC ECO:0000269|PubMed:22027592, ECO:0000269|PubMed:25043023,
CC ECO:0000269|PubMed:26083750}.
CC -!- SUBUNIT: Interacts with ERECTA and TMM. {ECO:0000269|PubMed:26083750}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:20007289, ECO:0000269|PubMed:20010603}. Secreted
CC {ECO:0000269|PubMed:20007289, ECO:0000269|PubMed:20010603}.
CC -!- TISSUE SPECIFICITY: Expressed in immature organs, including leaves,
CC stems and flower buds, but not in roots, shoot apical meristem and
CC petals. Detected in the mesophyll tissues but not in the epidermal
CC tissues where stomata develop. {ECO:0000269|PubMed:20007289,
CC ECO:0000269|PubMed:20010603}.
CC -!- DOMAIN: The loop (82-95) connecting the two anti-parallel beta-strands
CC (76-81 and 96-101) confers the function to the peptide.
CC {ECO:0000269|PubMed:22027592}.
CC -!- DISRUPTION PHENOTYPE: Reduced stomatal densities in various organs.
CC {ECO:0000269|PubMed:20010603}.
CC -!- SIMILARITY: Belongs to the plant cysteine rich small secretory peptide
CC family. Epidermal patterning factor subfamily.
CC {ECO:0000303|PubMed:19435754}.
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DR EMBL; AL079349; CAB45496.1; -; Genomic_DNA.
DR EMBL; AL161535; CAB78339.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83209.1; -; Genomic_DNA.
DR EMBL; AK175876; BAD43639.1; -; mRNA.
DR PIR; T10199; T10199.
DR RefSeq; NP_193033.1; NM_117366.4.
DR PDB; 2LIY; NMR; -; A=58-102.
DR PDBsum; 2LIY; -.
DR AlphaFoldDB; Q9SV72; -.
DR BMRB; Q9SV72; -.
DR SMR; Q9SV72; -.
DR STRING; 3702.AT4G12970.1; -.
DR PaxDb; Q9SV72; -.
DR PRIDE; Q9SV72; -.
DR ProteomicsDB; 220665; -.
DR DNASU; 826909; -.
DR EnsemblPlants; AT4G12970.1; AT4G12970.1; AT4G12970.
DR GeneID; 826909; -.
DR Gramene; AT4G12970.1; AT4G12970.1; AT4G12970.
DR KEGG; ath:AT4G12970; -.
DR Araport; AT4G12970; -.
DR TAIR; locus:2123261; AT4G12970.
DR eggNOG; ENOG502S4I2; Eukaryota.
DR HOGENOM; CLU_164346_0_0_1; -.
DR InParanoid; Q9SV72; -.
DR OMA; RCITIFF; -.
DR OrthoDB; 1582565at2759; -.
DR PhylomeDB; Q9SV72; -.
DR PRO; PR:Q9SV72; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SV72; baseline and differential.
DR Genevisible; Q9SV72; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0019901; F:protein kinase binding; IPI:TAIR.
DR GO; GO:0033612; F:receptor serine/threonine kinase binding; IPI:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; NAS:TAIR.
DR GO; GO:0010052; P:guard cell differentiation; ISS:UniProtKB.
DR GO; GO:2000123; P:positive regulation of stomatal complex development; IDA:TAIR.
DR GO; GO:2000038; P:regulation of stomatal complex development; IMP:TAIR.
DR GO; GO:0010374; P:stomatal complex development; ISS:UniProtKB.
DR GO; GO:0010375; P:stomatal complex patterning; IDA:TAIR.
DR Gene3D; 2.20.25.390; -; 1.
DR InterPro; IPR031753; Stomagen.
DR InterPro; IPR044858; Stomagen_C.
DR InterPro; IPR038572; Stomagen_C_sf.
DR PANTHER; PTHR37239; PTHR37239; 1.
DR Pfam; PF16851; Stomagen; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoplast; Developmental protein; Direct protein sequencing;
KW Disulfide bond; Reference proteome; Secreted; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..102
FT /note="EPIDERMAL PATTERNING FACTOR-like protein 9"
FT /id="PRO_0000392507"
FT CHAIN 58..102
FT /note="Stomagen"
FT /evidence="ECO:0000269|PubMed:20010603,
FT ECO:0000269|PubMed:22027592"
FT /id="PRO_0000430515"
FT DISULFID 65..98
FT /evidence="ECO:0000269|PubMed:20007289,
FT ECO:0000269|PubMed:22027592"
FT DISULFID 70..77
FT /evidence="ECO:0000269|PubMed:20007289,
FT ECO:0000269|PubMed:22027592"
FT DISULFID 73..100
FT /evidence="ECO:0000269|PubMed:20007289,
FT ECO:0000269|PubMed:22027592"
FT MUTAGEN 65
FT /note="C->S: Incorrect disulfide bonds formation and loss
FT of activity; when associated with S-98. Unstructured
FT protein and loss of activity; when associated with S-70; S-
FT 73; S-77; S-98 and S-100."
FT /evidence="ECO:0000269|PubMed:22027592"
FT MUTAGEN 70
FT /note="C->S: Incorrect disulfide bonds formation and loss
FT of activity; when associated with S-77. Unstructured
FT protein and loss of activity; when associated with S-65; S-
FT 73; S-77; S-98 and S-100."
FT /evidence="ECO:0000269|PubMed:22027592"
FT MUTAGEN 73
FT /note="C->S: Incorrect disulfide bonds formation and loss
FT of activity; when associated with S-100. Unstructured
FT protein and loss of activity; when associated with S-65; S-
FT 70; S-77; S-98 and S-100."
FT /evidence="ECO:0000269|PubMed:22027592"
FT MUTAGEN 77
FT /note="C->S: Incorrect disulfide bonds formation and loss
FT of activity; when associated with S-70. Unstructured
FT protein and loss of activity; when associated with S-65; S-
FT 70; S-73; S-98 and S-100."
FT /evidence="ECO:0000269|PubMed:22027592"
FT MUTAGEN 85
FT /note="E->A: No effect on conformation, but decreased
FT activity."
FT /evidence="ECO:0000269|PubMed:22027592"
FT MUTAGEN 88
FT /note="D->A: No effect on conformation or activity."
FT /evidence="ECO:0000269|PubMed:22027592"
FT MUTAGEN 98
FT /note="C->S: Incorrect disulfide bonds formation and loss
FT of activity; when associated with S-65. Unstructured
FT protein and loss of activity; when associated with S-65; S-
FT 70; S-73; S-77 and S-100."
FT /evidence="ECO:0000269|PubMed:22027592"
FT MUTAGEN 100
FT /note="C->S: Incorrect disulfide bonds formation and loss
FT of activity; when associated with S-73. Unstructured
FT protein and loss of activity; when associated with S-65; S-
FT 70; S-73; S-77 and S-98."
FT /evidence="ECO:0000269|PubMed:22027592"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:2LIY"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:2LIY"
FT STRAND 75..85
FT /evidence="ECO:0007829|PDB:2LIY"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:2LIY"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:2LIY"
SQ SEQUENCE 102 AA; 11840 MW; B0918A267783A6DA CRC64;
MKHEMMNIKP RCITIFFLLF ALLLGNYVVQ ASRPRSIENT VSLLPQVHLL NSRRRHMIGS
TAPTCTYNEC RGCRYKCRAE QVPVEGNDPI NSAYHYRCVC HR
