RLF32_ARATH
ID RLF32_ARATH Reviewed; 117 AA.
AC O23262; Q0WTV4; Q8L9C7;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Protein RALF-like 32;
DE Flags: Precursor;
GN Name=RALFL32; OrderedLocusNames=At4g14010; ORFNames=dl3045c, FCAALL.140;
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 Kim C.J., Chen H., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-117.
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
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}.
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DR EMBL; Z97335; CAB10180.1; -; Genomic_DNA.
DR EMBL; AL161537; CAB78443.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83360.1; -; Genomic_DNA.
DR EMBL; BT024787; ABD59125.1; -; mRNA.
DR EMBL; AY088508; AAM66043.1; -; mRNA.
DR EMBL; AK227441; BAE99444.1; -; mRNA.
DR PIR; B71401; B71401.
DR RefSeq; NP_567418.1; NM_117476.5.
DR AlphaFoldDB; O23262; -.
DR STRING; 3702.AT4G14010.1; -.
DR PaxDb; O23262; -.
DR PRIDE; O23262; -.
DR ProteomicsDB; 228021; -.
DR EnsemblPlants; AT4G14010.1; AT4G14010.1; AT4G14010.
DR GeneID; 827037; -.
DR Gramene; AT4G14010.1; AT4G14010.1; AT4G14010.
DR KEGG; ath:AT4G14010; -.
DR Araport; AT4G14010; -.
DR TAIR; locus:2129341; AT4G14010.
DR eggNOG; ENOG502S5DT; Eukaryota.
DR HOGENOM; CLU_127895_4_0_1; -.
DR InParanoid; O23262; -.
DR OMA; TVIMESW; -.
DR OrthoDB; 1554212at2759; -.
DR PhylomeDB; O23262; -.
DR PRO; PR:O23262; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23262; differential.
DR Genevisible; O23262; 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; Glycoprotein; Hormone; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..64
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000420331"
FT CHAIN 65..117
FT /note="Protein RALF-like 32"
FT /id="PRO_0000420332"
FT REGION 77..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 60..61
FT /note="Required for proteolytic cleavage"
FT /evidence="ECO:0000250"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 82..95
FT /evidence="ECO:0000250"
FT DISULFID 107..113
FT /evidence="ECO:0000250"
FT CONFLICT 113
FT /note="C -> F (in Ref. 5; AAM66043)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 117 AA; 12919 MW; FC95F8204A998E05 CRC64;
MEIKPSRIFS TITIFFLCLL LAHVTSKASS SSLCNGSVAE CSSMVETEEM SVIMESWSSQ
RLTEEQAHKL SYGALRRNQP ACDGGKRGES YSTQCLPPPS NPYSRGCSKH YRCGRDS
