HSY1_SOLLC
ID HSY1_SOLLC Reviewed; 146 AA.
AC Q7XAD0;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Hydroxyproline-rich systemin;
DE AltName: Full=Defense-signaling glycopeptide hormone;
DE Contains:
DE RecName: Full=HypSys I;
DE AltName: Full=TomHypSys I;
DE Contains:
DE RecName: Full=HypSys II;
DE AltName: Full=TomHypSys II;
DE Contains:
DE RecName: Full=HypSys III;
DE AltName: Full=TomHypSys III;
DE Flags: Precursor;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000312|EMBL:AAQ19087.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 49-66; 71-85 AND 111-125,
RP FUNCTION, TISSUE SPECIFICITY, MASS SPECTROMETRY, HYDROXYLATION AT PRO-51;
RP PRO-55; PRO-56; PRO-57; PRO-58; PRO-63; PRO-79; PRO-80; PRO-82; PRO-119;
RP PRO-120; PRO-121 AND PRO-122, AND GLYCOSYLATION.
RC STRAIN=cv. Castlemart {ECO:0000312|EMBL:AAQ19087.1};
RX PubMed=12748180; DOI=10.1074/jbc.m304159200;
RA Pearce G., Ryan C.A.;
RT "Systemic signaling in tomato plants for defense against herbivores:
RT isolation and characterization of three novel defense-signaling
RT glycopeptide hormones coded in a single precursor gene.";
RL J. Biol. Chem. 278:30044-30050(2003).
RN [2] {ECO:0000305}
RP REVIEW ON FUNCTION.
RX PubMed=12949264; DOI=10.1073/pnas.1934788100;
RA Ryan C.A., Pearce G.;
RT "Systemins: a functionally defined family of peptide signals that regulate
RT defensive genes in Solanaceae species.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:14577-14580(2003).
CC -!- FUNCTION: Activates a lipid-based signal transduction pathway in which
CC linolenic acid is converted to jasmonic acid, a potent activator of
CC defense gene transcription. Induces synthesis of proteinase inhibitors
CC I and II in leaves when supplied through cut stems.
CC {ECO:0000269|PubMed:12748180}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Leaves. {ECO:0000269|PubMed:12748180}.
CC -!- INDUCTION: By wounding and methyl jasmonate in leaves.
CC {ECO:0000269|PubMed:12748180}.
CC -!- PTM: O-glycosylated; contains pentose side chains.
CC {ECO:0000269|PubMed:12748180}.
CC -!- MASS SPECTROMETRY: [HypSys I]: Mass=4191; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12748180};
CC -!- MASS SPECTROMETRY: [HypSys I]: Mass=3531; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12748180};
CC -!- MASS SPECTROMETRY: [HypSys III]: Mass=2954; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12748180};
CC -!- MASS SPECTROMETRY: [HypSys II]: Mass=4513; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12748180, ECO:0000303|PubMed:12748180};
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DR EMBL; AY292201; AAQ19087.1; -; mRNA.
DR RefSeq; NP_001234375.1; NM_001247446.2.
DR AlphaFoldDB; Q7XAD0; -.
DR SMR; Q7XAD0; -.
DR PaxDb; Q7XAD0; -.
DR EnsemblPlants; Solyc06g068520.3.1; Solyc06g068520.3.1; Solyc06g068520.3.
DR GeneID; 543883; -.
DR Gramene; Solyc06g068520.3.1; Solyc06g068520.3.1; Solyc06g068520.3.
DR KEGG; sly:543883; -.
DR eggNOG; ENOG502R5P7; Eukaryota.
DR HOGENOM; CLU_1985565_0_0_1; -.
DR InParanoid; Q7XAD0; -.
DR OMA; KHEPIIG; -.
DR OrthoDB; 1565068at2759; -.
DR Proteomes; UP000004994; Chromosome 6.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Hormone; Hydroxylation;
KW Plant defense; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..48
FT /evidence="ECO:0000255, ECO:0000269|PubMed:12748180"
FT /id="PRO_0000021449"
FT PEPTIDE 49..66
FT /note="HypSys I"
FT /evidence="ECO:0000269|PubMed:12748180"
FT /id="PRO_0000021450"
FT PROPEP 67..70
FT /evidence="ECO:0000269|PubMed:12748180"
FT /id="PRO_0000021451"
FT PEPTIDE 71..85
FT /note="HypSys III"
FT /evidence="ECO:0000269|PubMed:12748180"
FT /id="PRO_0000021452"
FT PROPEP 86..110
FT /evidence="ECO:0000269|PubMed:12748180"
FT /id="PRO_0000021453"
FT PEPTIDE 111..130
FT /note="HypSys II"
FT /evidence="ECO:0000269|PubMed:12748180,
FT ECO:0000303|PubMed:12748180"
FT /id="PRO_0000021454"
FT PROPEP 131..146
FT /evidence="ECO:0000303|PubMed:12748180"
FT /id="PRO_0000021455"
FT REGION 47..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:12748180"
FT MOD_RES 55
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:12748180"
FT MOD_RES 56
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:12748180"
FT MOD_RES 57
FT /note="4-hydroxyproline"
FT MOD_RES 58
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:12748180"
FT MOD_RES 63
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:12748180"
FT MOD_RES 79
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:12748180"
FT MOD_RES 80
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:12748180"
FT MOD_RES 82
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:12748180"
FT MOD_RES 119
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:12748180"
FT MOD_RES 120
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:12748180"
FT MOD_RES 121
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:12748180"
FT MOD_RES 122
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:12748180"
FT CARBOHYD 51
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000255"
FT CARBOHYD 55
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000255"
SQ SEQUENCE 146 AA; 16012 MW; 115E92B146A31973 CRC64;
MISFFRAFFL IIIISFLIFV GAQARTLLGN YHDDEMLIEL KLESGNYGRT PYKTPPPPTS
SSPTHQEIVN GRHDSVLPPP SPKTDPIIGQ LTTITTTPHH DDTVAAPPVG GRHDYVASPP
PPKPQDEQRQ IIITSSSSTL PLQASY
