ID   STIG1_SOLLC             Reviewed;         143 AA.
AC   Q6EEH1;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Protein STIG1 {ECO:0000303|PubMed:15255864};
DE            Short=LeSTIG1 {ECO:0000303|PubMed:15255864};
DE   AltName: Full=Stigma-specific protein STIG1 {ECO:0000303|PubMed:15255864};
DE   Flags: Precursor;
GN   Name=STIG1 {ECO:0000303|PubMed:15255864}; OrderedLocusNames=Solyc03g120960;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH PRK1 AND PRK2.
RC   STRAIN=cv. VF36; TISSUE=Stigma;
RX   PubMed=15255864; DOI=10.1111/j.1365-313x.2004.02139.x;
RA   Tang W., Kelley D., Ezcurra I., Cotter R., McCormick S.;
RT   "LeSTIG1, an extracellular binding partner for the pollen receptor kinases
RT   LePRK1 and LePRK2, promotes pollen tube growth in vitro.";
RL   Plant J. 39:343-353(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Heinz 1706;
RX   PubMed=22660326; DOI=10.1038/nature11119;
RG   Tomato Genome Consortium;
RT   "The tomato genome sequence provides insights into fleshy fruit
RT   evolution.";
RL   Nature 485:635-641(2012).
RN   [3]
RP   FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING,
RP   AND MUTAGENESIS OF 80-PHE--PHE-83.
RC   STRAIN=cv. VF36;
RX   PubMed=24938288; DOI=10.1105/tpc.114.123281;
RA   Huang W.J., Liu H.K., McCormick S., Tang W.H.;
RT   "Tomato pistil factor STIG1 promotes in vivo pollen tube growth by binding
RT   to phosphatidylinositol 3-phosphate and the extracellular domain of the
RT   pollen receptor kinase LePRK2.";
RL   Plant Cell 26:2505-2523(2014).
CC   -!- FUNCTION: Promotes pollen tube growth (PubMed:15255864,
CC       PubMed:24938288). A C-terminal peptide is cleaved from the propeptide
CC       in the stigmatic exudate and represent the major form of STIG1
CC       (PubMed:24938288). Binds phosphoinositol lipids (PubMed:24938288). The
CC       binding of external phosphatidylinositol 3-phosphate (PI(3)P) and PRK2
CC       by STIG1 induces a rapid intracellular reactive oxygen species
CC       elevation (PubMed:24938288). {ECO:0000269|PubMed:15255864,
CC       ECO:0000269|PubMed:24938288}.
CC   -!- SUBUNIT: Interacts with PRK1 and PRK2 (via extracellular domain).
CC       {ECO:0000269|PubMed:15255864}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000269|PubMed:24938288}.
CC   -!- TISSUE SPECIFICITY: Expressed in the stigma and the upper section of
CC       the style. {ECO:0000269|PubMed:24938288}.
CC   -!- SIMILARITY: Belongs to the STIG1 family. {ECO:0000305}.
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DR   EMBL; AY376851; AAR27430.1; -; mRNA.
DR   RefSeq; NP_001234442.1; NM_001247513.1.
DR   AlphaFoldDB; Q6EEH1; -.
DR   STRING; 4081.Solyc03g120960.1.1; -.
DR   PaxDb; Q6EEH1; -.
DR   PRIDE; Q6EEH1; -.
DR   GeneID; 543904; -.
DR   KEGG; sly:543904; -.
DR   eggNOG; ENOG502R7YC; Eukaryota.
DR   HOGENOM; CLU_111795_1_0_1; -.
DR   OrthoDB; 1564231at2759; -.
DR   PhylomeDB; Q6EEH1; -.
DR   Proteomes; UP000004994; Unplaced.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   InterPro; IPR006969; Stig1.
DR   PANTHER; PTHR33227; PTHR33227; 1.
DR   Pfam; PF04885; Stig1; 1.
PE   1: Evidence at protein level;
KW   Apoplast; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..143
FT                   /note="Protein STIG1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000431929"
FT   REGION          76..87
FT                   /note="Sufficient for PI(4)P binding"
FT                   /evidence="ECO:0000269|PubMed:24938288"
FT   REGION          80..83
FT                   /note="Sufficient for binding to the extracellular domain
FT                   of PRK2"
FT                   /evidence="ECO:0000269|PubMed:24938288"
FT   REGION          88..115
FT                   /note="Sufficient for PI(3)P binding"
FT                   /evidence="ECO:0000269|PubMed:24938288"
FT   MUTAGEN         80
FT                   /note="F->A: No effect on the interaction with PRK2."
FT                   /evidence="ECO:0000269|PubMed:24938288"
FT   MUTAGEN         81
FT                   /note="N->A: Strongly decreased interaction with PRK2 and
FT                   loss of growth-promoting activity."
FT                   /evidence="ECO:0000269|PubMed:24938288"
FT   MUTAGEN         82..83
FT                   /note="YF->AA: Increased interaction with PRK2."
FT                   /evidence="ECO:0000269|PubMed:24938288"
SQ   SEQUENCE   143 AA;  15412 MW;  DFFBB5F510173CDE CRC64;
     MDFIILLIAI LALSSTPITI ISGSVTNHTY STTNSYTNVA LSARKVVFPP PRQLGKDNSD
     DDDLICKTCK RLSEHRTCCF NYFCVDLFTN RFNCGSCGLV CIVGTRCCGG ICVDIKKDNG
     NCGKCNNVCS PGQNCSFGLC VSA