ID   RALF_TOBAC              Reviewed;         115 AA.
AC   Q945T0;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Rapid alkalinization factor;
DE            Short=NtRALF;
DE   Flags: Precursor;
GN   Name=RALF;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 67-83, FUNCTION, MASS
RP   SPECTROMETRY, AND DISULFIDE BONDS.
RX   PubMed=11675511; DOI=10.1073/pnas.201416998;
RA   Pearce G., Moura D.S., Stratmann J., Ryan C.A. Jr.;
RT   "RALF, a 5-kDa ubiquitous polypeptide in plants, arrests root growth and
RT   development.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12843-12847(2001).
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       Prevents root growth and seedling development in heterologous system.
CC       {ECO:0000269|PubMed:11675511}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- PTM: Proteolytically cleaved, probably by S1P, a subtilisin-like serine
CC       protease (subtilase). {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=5332.7; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11675511};
CC   -!- SIMILARITY: Belongs to the plant rapid alkalinization factor (RALF)
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF407278; AAL26478.1; -; mRNA.
DR   RefSeq; XP_016491711.1; XM_016636225.1.
DR   AlphaFoldDB; Q945T0; -.
DR   PRIDE; Q945T0; -.
DR   GeneID; 107811318; -.
DR   KEGG; nta:107811318; -.
DR   OMA; WMVPARS; -.
DR   OrthoDB; 1601238at2759; -.
DR   PhylomeDB; Q945T0; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IDA:UniProtKB.
DR   GO; GO:0048018; F:receptor ligand activity; IDA:UniProtKB.
DR   GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR   GO; GO:0010469; P:regulation of signaling receptor activity; IDA:UniProtKB.
DR   InterPro; IPR008801; RALF.
DR   Pfam; PF05498; RALF; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hormone; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..66
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000269|PubMed:11675511"
FT                   /id="PRO_0000420289"
FT   PEPTIDE         67..115
FT                   /note="Rapid alkalinization factor"
FT                   /id="PRO_5000061289"
FT   SITE            63..64
FT                   /note="Required for proteolytic cleavage"
FT                   /evidence="ECO:0000250"
FT   DISULFID        84..94
FT                   /evidence="ECO:0000269|PubMed:11675511"
FT   DISULFID        107..113
FT                   /evidence="ECO:0000269|PubMed:11675511"
SQ   SEQUENCE   115 AA;  12203 MW;  7089DDF3EC1CE346 CRC64;
     MGVPSGLILC VLIGAFFISM AAAGDSGAYD WVMPARSGGG CKGSIGECIA EEEEFELDSE
     SNRRILATKK YISYGALQKN SVPCSRRGAS YYNCKPGAQA NPYSRGCSAI TRCRS