ID   BABL_LILLO              Reviewed;         126 AA.
AC   P60496;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Chemocyanin;
DE   AltName: Full=Basic blue protein;
DE   AltName: Full=Plantacyanin;
DE   Flags: Precursor;
OS   Lilium longiflorum (Trumpet lily).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Liliales; Liliaceae; Lilium.
OX   NCBI_TaxID=4690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-52 AND 56-80, TISSUE
RP   SPECIFICITY, AND MASS SPECTROMETRY.
RC   STRAIN=cv. Nellie white; TISSUE=Stigma;
RX   PubMed=14671326; DOI=10.1073/pnas.2533800100;
RA   Kim S., Mollet J.-C., Dong J., Zhang K., Park S.-Y., Lord E.M.;
RT   "Chemocyanin, a small basic protein from the lily stigma, induces pollen
RT   tube chemotropism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:16125-16130(2003).
CC   -!- FUNCTION: Diffusible chemotropic factor that induces pollen tube
CC       chemotropism.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in stigma and style and to a
CC       lesser extent in leaves, ovary and petals. Not detected in pollen
CC       tubes, mature anthers or roots. {ECO:0000269|PubMed:14671326}.
CC   -!- INDUCTION: Activity enhanced in the presence of stigma/stylar Cys-rich
CC       adhesin (SCA).
CC   -!- MASS SPECTROMETRY: Mass=9898.0; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:14671326};
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DR   EMBL; AY425323; AAR84219.1; -; mRNA.
DR   AlphaFoldDB; P60496; -.
DR   SMR; P60496; -.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd11013; Plantacyanin; 1.
DR   Gene3D; 2.60.40.420; -; 1.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR039391; Phytocyanin.
DR   InterPro; IPR003245; Phytocyanin_dom.
DR   InterPro; IPR041844; Plantacyanin.
DR   PANTHER; PTHR33021; PTHR33021; 1.
DR   Pfam; PF02298; Cu_bind_like; 1.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   PROSITE; PS51485; PHYTOCYANIN; 1.
PE   1: Evidence at protein level;
KW   Copper; Direct protein sequencing; Disulfide bond; Metal-binding; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..126
FT                   /note="Chemocyanin"
FT                   /id="PRO_0000002865"
FT   DOMAIN          31..126
FT                   /note="Phytocyanin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT   BINDING         69
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT   BINDING         109
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT   BINDING         114
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT   DISULFID        82..115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
SQ   SEQUENCE   126 AA;  12979 MW;  813D63D696280874 CRC64;
     MAQGSGSAER ALVLGVVLVF LVFNCEVAES VVYTVGDGGG WTFGTSGWPA GKTFRAGDVL
     VFKYNPAVHN VVSVPAGGYK SCTASPGSRV FKSGDDRITL SRGTNYFICS VPGHCQGGLK
     IAVTAA