RLF34_ARATH
ID RLF34_ARATH Reviewed; 129 AA.
AC Q9FHA6; Q8L9S6;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Protein RALF-like 34;
DE Flags: Precursor;
GN Name=RALFL34; OrderedLocusNames=At5g67070; ORFNames=K21H1.3;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
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 [5]
RP TISSUE SPECIFICITY, INDUCTION BY SENESCENCE, 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 -!- TISSUE SPECIFICITY: Expressed in roots, stems and leaves.
CC {ECO:0000269|PubMed:12611624}.
CC -!- INDUCTION: Accumulates during senescence.
CC {ECO:0000269|PubMed:12611624}.
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; AB020742; BAB10941.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98297.1; -; Genomic_DNA.
DR EMBL; AF370212; AAK44027.1; -; mRNA.
DR EMBL; AY133871; AAM91805.1; -; mRNA.
DR EMBL; AY088253; AAM65793.1; -; mRNA.
DR RefSeq; NP_201508.1; NM_126107.4.
DR AlphaFoldDB; Q9FHA6; -.
DR STRING; 3702.AT5G67070.1; -.
DR PaxDb; Q9FHA6; -.
DR PRIDE; Q9FHA6; -.
DR ProteomicsDB; 228182; -.
DR EnsemblPlants; AT5G67070.1; AT5G67070.1; AT5G67070.
DR GeneID; 836842; -.
DR Gramene; AT5G67070.1; AT5G67070.1; AT5G67070.
DR KEGG; ath:AT5G67070; -.
DR Araport; AT5G67070; -.
DR TAIR; locus:2155553; AT5G67070.
DR eggNOG; ENOG502S4T2; Eukaryota.
DR HOGENOM; CLU_127895_2_0_1; -.
DR InParanoid; Q9FHA6; -.
DR OMA; THNCFGA; -.
DR OrthoDB; 1600000at2759; -.
DR PhylomeDB; Q9FHA6; -.
DR PRO; PR:Q9FHA6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHA6; baseline and differential.
DR Genevisible; Q9FHA6; 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 2: Evidence at transcript level;
KW Disulfide bond; Hormone; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..76
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000420335"
FT CHAIN 77..129
FT /note="Protein RALF-like 34"
FT /id="PRO_0000420336"
FT SITE 70..71
FT /note="Required for proteolytic cleavage"
FT /evidence="ECO:0000250"
FT DISULFID 94..107
FT /evidence="ECO:0000250"
FT DISULFID 121..127
FT /evidence="ECO:0000250"
FT CONFLICT 119
FT /note="R -> L (in Ref. 4; AAM65793)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 129 AA; 14729 MW; 2D37905589A035EA CRC64;
MAASSLNLLL ILSLLTFISL QRSESLSDNP SLTLLPDGFD WPISHSDEFD IIDGEESFEV
TEEDDGVTDR RSLYWRRTKY YISYGALSAN RVPCPPRSGR SYYTHNCFRA RGPVHPYSRG
CSSITRCRR
