RLF31_ARATH
ID RLF31_ARATH Reviewed; 113 AA.
AC Q2HIM9; O23256; Q8LDV7;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Protein RALF-like 31;
DE Flags: Precursor;
GN Name=RALFL31; OrderedLocusNames=At4g13950; ORFNames=dl3015c, FCAALL.121;
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
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 [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 Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12611624;
RA Olsen A.N., Mundy J., Skriver K.;
RT "Peptomics, identification of novel cationic Arabidopsis peptides with
RT conserved sequence motifs.";
RL In Silico Biol. 2:441-451(2002).
CC -!- FUNCTION: Cell signaling peptide that may regulate plant stress,
CC growth, and development. Mediates a rapid alkalinization of
CC extracellular space by mediating a transient increase in the
CC cytoplasmic Ca(2+) concentration leading to a calcium-dependent
CC signaling events through a cell surface receptor and a concomitant
CC activation of some intracellular mitogen-activated protein kinases (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- PTM: Proteolytically cleaved, probably by S1P, a subtilisin-like serine
CC protease (subtilase). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the plant rapid alkalinization factor (RALF)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10174.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78437.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z97335; CAB10174.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161537; CAB78437.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83349.1; -; Genomic_DNA.
DR EMBL; BT024552; ABD38891.1; -; mRNA.
DR EMBL; AY085773; AAM62990.1; -; mRNA.
DR PIR; D71400; D71400.
DR RefSeq; NP_567413.1; NM_117469.2.
DR AlphaFoldDB; Q2HIM9; -.
DR SMR; Q2HIM9; -.
DR PaxDb; Q2HIM9; -.
DR PRIDE; Q2HIM9; -.
DR ProteomicsDB; 228160; -.
DR EnsemblPlants; AT4G13950.1; AT4G13950.1; AT4G13950.
DR GeneID; 827029; -.
DR Gramene; AT4G13950.1; AT4G13950.1; AT4G13950.
DR KEGG; ath:AT4G13950; -.
DR Araport; AT4G13950; -.
DR TAIR; locus:2129261; AT4G13950.
DR eggNOG; ENOG502S4CN; Eukaryota.
DR HOGENOM; CLU_127895_0_0_1; -.
DR InParanoid; Q2HIM9; -.
DR OMA; DTITRCA; -.
DR OrthoDB; 1601238at2759; -.
DR PhylomeDB; Q2HIM9; -.
DR PRO; PR:Q2HIM9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q2HIM9; baseline and differential.
DR Genevisible; Q2HIM9; AT.
DR GO; GO:0048046; C:apoplast; ISS:TAIR.
DR GO; GO:0005179; F:hormone activity; ISS:UniProtKB.
DR GO; GO:0019722; P:calcium-mediated signaling; ISS:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; ISS:TAIR.
DR InterPro; IPR008801; RALF.
DR Pfam; PF05498; RALF; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Hormone; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..58
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000420329"
FT CHAIN 59..113
FT /note="Protein RALF-like 31"
FT /id="PRO_0000420330"
FT SITE 54..55
FT /note="Required for proteolytic cleavage"
FT /evidence="ECO:0000250"
FT DISULFID 76..86
FT /evidence="ECO:0000250"
FT DISULFID 98..104
FT /evidence="ECO:0000250"
FT CONFLICT 16
FT /note="L -> S (in Ref. 5; AAM62990)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="A -> V (in Ref. 5; AAM62990)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 113 AA; 12676 MW; 6C1BFC2AFDD9DDB1 CRC64;
MFNSTALVIF AILFLLISAD AFPIPSPNGE IDAMLIRNSI IGEDEDLMPT EISRRVLMAQ
KRYIGYETLR RDMVPCQKPG ASYYDCRSGQ ANSYSRGCDT ITRCARDTND INT
