RLF1_ARATH
ID RLF1_ARATH Reviewed; 120 AA.
AC Q9SRY3;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Protein RALF-like 1;
DE AltName: Full=Rapid alkalinization factor 1;
DE Short=AtRALF1;
DE Flags: Precursor;
GN Name=RALF1; Synonyms=RALFL1; OrderedLocusNames=At1g02900;
GN ORFNames=F22D16.10;
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=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 [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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP PROTEIN SEQUENCE OF 76-84, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION BY OXIDATION.
RC STRAIN=cv. Wassilewskija;
RX PubMed=18494498; DOI=10.1021/bi8001488;
RA Haruta M., Monshausen G., Gilroy S., Sussman M.R.;
RT "A cytoplasmic Ca2+ functional assay for identifying and purifying
RT endogenous cell signaling peptides in Arabidopsis seedlings: identification
RT of AtRALF1 peptide.";
RL Biochemistry 47:6311-6321(2008).
RN [5]
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).
RN [6]
RP FUNCTION, MUTAGENESIS OF ARG-69, AND CLEAVAGE BY KEXIN-LIKE CONVERTASE.
RC STRAIN=cv. Columbia;
RX PubMed=18775699; DOI=10.1016/j.febslet.2008.08.025;
RA Matos J.L., Fiori C.S., Silva-Filho M.C., Moura D.S.;
RT "A conserved dibasic site is essential for correct processing of the
RT peptide hormone AtRALF1 in Arabidopsis thaliana.";
RL FEBS Lett. 582:3343-3347(2008).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH FER, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=cv. Columbia;
RX PubMed=24458638; DOI=10.1126/science.1244454;
RA Haruta M., Sabat G., Stecker K., Minkoff B.B., Sussman M.R.;
RT "A peptide hormone and its receptor protein kinase regulate plant cell
RT expansion.";
RL Science 343:408-411(2014).
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.
CC Mostly active in roots. Prevents plant growth (e.g. root and leaf
CC length). Suppresses cell elongation of the primary root by activating
CC the cell surface receptor FER and triggering phosphorylation of AHA2
CC and subsequent extracellular alkalinization.
CC {ECO:0000269|PubMed:18494498, ECO:0000269|PubMed:18775699,
CC ECO:0000269|PubMed:24458638}.
CC -!- SUBUNIT: Interacts with FER and promotes its phosphorylation and
CC subsequent activation. {ECO:0000269|PubMed:24458638}.
CC -!- INTERACTION:
CC Q9SRY3; Q9SCZ4: FER; NbExp=3; IntAct=EBI-16091545, EBI-15880405;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and stems.
CC {ECO:0000269|PubMed:18494498}.
CC -!- DEVELOPMENTAL STAGE: First detected in the root hair zone of seedlings,
CC mostly in the vascular bundles, cortex, and endodermis. Later observed
CC in hypocotyls and veins of cotyledons. {ECO:0000269|PubMed:18494498}.
CC -!- INDUCTION: More efficient to mediate cytoplasmic Ca(2+) accumulation
CC when oxidized, but inactive when reduced.
CC {ECO:0000269|PubMed:18494498}.
CC -!- PTM: Proteolytically cleaved, probably by S1P, a subtilisin-like serine
CC protease (subtilase). {ECO:0000269|PubMed:18775699}.
CC -!- DISRUPTION PHENOTYPE: Longer roots. {ECO:0000269|PubMed:24458638}.
CC -!- SIMILARITY: Belongs to the plant rapid alkalinization factor (RALF)
CC family. {ECO:0000305}.
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DR EMBL; AC009525; AAF02876.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27494.1; -; Genomic_DNA.
DR EMBL; BT010174; AAQ22643.1; -; mRNA.
DR PIR; D86159; D86159.
DR RefSeq; NP_171789.1; NM_100171.3.
DR AlphaFoldDB; Q9SRY3; -.
DR BioGRID; 24624; 1.
DR DIP; DIP-61428N; -.
DR IntAct; Q9SRY3; 1.
DR STRING; 3702.AT1G02900.1; -.
DR PaxDb; Q9SRY3; -.
DR PRIDE; Q9SRY3; -.
DR ProteomicsDB; 228004; -.
DR EnsemblPlants; AT1G02900.1; AT1G02900.1; AT1G02900.
DR GeneID; 839389; -.
DR Gramene; AT1G02900.1; AT1G02900.1; AT1G02900.
DR KEGG; ath:AT1G02900; -.
DR Araport; AT1G02900; -.
DR TAIR; locus:2024730; AT1G02900.
DR eggNOG; ENOG502S1TF; Eukaryota.
DR HOGENOM; CLU_127895_1_2_1; -.
DR InParanoid; Q9SRY3; -.
DR OMA; WMVPARS; -.
DR OrthoDB; 1601238at2759; -.
DR PhylomeDB; Q9SRY3; -.
DR PRO; PR:Q9SRY3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SRY3; baseline and differential.
DR Genevisible; Q9SRY3; 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; IDA:TAIR.
DR GO; GO:0007267; P:cell-cell signaling; ISS:TAIR.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0048364; P:root development; IMP:UniProtKB.
DR InterPro; IPR008801; RALF.
DR Pfam; PF05498; RALF; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hormone;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..71
FT /note="Removed in mature form"
FT /id="PRO_0000420290"
FT CHAIN 72..120
FT /note="Protein RALF-like 1"
FT /id="PRO_0000420291"
FT SITE 68..69
FT /note="Required for proteolytic cleavage"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 89..99
FT /evidence="ECO:0000250"
FT DISULFID 112..118
FT /evidence="ECO:0000250"
FT MUTAGEN 69
FT /note="R->A: Loss of propeptide cleavage by kexin-like
FT convertase leading to an impaired activity."
FT /evidence="ECO:0000269|PubMed:18775699"
SQ SEQUENCE 120 AA; 12967 MW; E3D2FA2C1DA0EDAD CRC64;
MDKSFTLFLT LTILVVFIIS SPPVQAGFAN DLGGVAWATT GDNGSGCHGS IAECIGAEEE
EMDSEINRRI LATTKYISYQ SLKRNSVPCS RRGASYYNCQ NGAQANPYSR GCSKIARCRS
