RLF4_ARATH
ID RLF4_ARATH Reviewed; 110 AA.
AC Q9FZA0;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Protein RALF-like 4;
DE Flags: Precursor;
GN Name=RALFL4; OrderedLocusNames=At1g28270; ORFNames=F3H9.8;
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 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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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).
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; AC021044; AAF98428.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30939.1; -; Genomic_DNA.
DR EMBL; BT005747; AAO64155.1; -; mRNA.
DR EMBL; AK228573; BAF00491.1; -; mRNA.
DR PIR; H86408; H86408.
DR RefSeq; NP_174148.1; NM_102592.3.
DR PDB; 6QWN; X-ray; 3.89 A; F/G/H/I/J=54-107.
DR PDB; 6QXP; X-ray; 3.20 A; I/J/K/L/M/N/O/P=54-107.
DR PDB; 6TME; X-ray; 2.33 A; C/D=58-107.
DR PDBsum; 6QWN; -.
DR PDBsum; 6QXP; -.
DR PDBsum; 6TME; -.
DR AlphaFoldDB; Q9FZA0; -.
DR SMR; Q9FZA0; -.
DR STRING; 3702.AT1G28270.1; -.
DR PaxDb; Q9FZA0; -.
DR PRIDE; Q9FZA0; -.
DR ProteomicsDB; 228083; -.
DR EnsemblPlants; AT1G28270.1; AT1G28270.1; AT1G28270.
DR GeneID; 839721; -.
DR Gramene; AT1G28270.1; AT1G28270.1; AT1G28270.
DR KEGG; ath:AT1G28270; -.
DR Araport; AT1G28270; -.
DR TAIR; locus:2032195; AT1G28270.
DR eggNOG; ENOG502S8YN; Eukaryota.
DR HOGENOM; CLU_127895_0_1_1; -.
DR InParanoid; Q9FZA0; -.
DR OMA; RCPFTIM; -.
DR OrthoDB; 1592895at2759; -.
DR PhylomeDB; Q9FZA0; -.
DR PRO; PR:Q9FZA0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZA0; baseline and differential.
DR Genevisible; Q9FZA0; 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 GO; GO:0080092; P:regulation of pollen tube growth; IGI:TAIR.
DR InterPro; IPR008801; RALF.
DR Pfam; PF05498; RALF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Hormone; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..58
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000420294"
FT CHAIN 59..110
FT /note="Protein RALF-like 4"
FT /evidence="ECO:0000250"
FT /id="PRO_0000420295"
FT SITE 54..55
FT /note="Required for proteolytic cleavage"
FT /evidence="ECO:0000250"
FT DISULFID 76..86
FT /evidence="ECO:0000250"
FT DISULFID 99..105
FT /evidence="ECO:0000250"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:6TME"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:6QXP"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:6QXP"
FT HELIX 102..106
FT /evidence="ECO:0007829|PDB:6TME"
SQ SEQUENCE 110 AA; 12662 MW; 5F27C7C0457956B9 CRC64;
MGVKMLLIFG LLILAMVAKS VNATYPLTKS CINGQGCIGE DDELESLMDS ETNRRQLARG
RRYIGYDALK KNNVPCSRRG RSYYDCKKRR RNNPYRRGCS AITHCYRYAR
