SCA_LILLO
ID SCA_LILLO Reviewed; 113 AA.
AC Q9SW93;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Stigma/stylar cysteine-rich adhesin;
DE AltName: Full=Lipid transfer protein;
DE Flags: Precursor;
GN Name=SCA; Synonyms=LTP;
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 23-57, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Nellie white;
RX PubMed=10634914; DOI=10.2307/3871036;
RA Park S.Y., Jauh G.Y., Mollet J.-C., Eckard K.J., Nothnagel E.A.,
RA Walling L.L., Lord E.M.;
RT "A lipid transfer-like protein is necessary for lily pollen tube adhesion
RT to an in vitro stylar matrix.";
RL Plant Cell 12:151-164(2000).
RN [2]
RP PECTIN BINDING.
RX PubMed=11006344; DOI=10.2307/3871186;
RA Mollet J.-C., Park S.Y., Nothnagel E.A., Lord E.M.;
RT "A lily stylar pectin is necessary for pollen tube adhesion to an in vitro
RT stylar matrix.";
RL Plant Cell 12:1737-1750(2000).
RN [3]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12602877; DOI=10.1023/a:1021139502947;
RA Park S.Y., Lord E.M.;
RT "Expression studies of SCA in lily and confirmation of its role in pollen
RT tube adhesion.";
RL Plant Mol. Biol. 51:183-189(2003).
CC -!- FUNCTION: Acts as an adhesive agent between the pollen tube wall and
CC the stylar transmitting tract epidermis. Binds a stylar pectin in a pH-
CC dependent manner. Enhances activity of chemocyanin, a diffusible
CC chemotropic factor.
CC -!- TISSUE SPECIFICITY: Highly expressed in style and stigma, abundant in
CC young leaves and petals, and low expression in young anthers at pollen
CC mother cell stage with an active tapetum. Not expressed in mature
CC leaves or in pollen grains or tubes. Found in the stylar transmitting
CC tract epidermis and in the stylar extracellular matrix.
CC {ECO:0000269|PubMed:10634914, ECO:0000269|PubMed:12602877}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development of the stigma and
CC style, and then decreases at 6 days after anthesis.
CC {ECO:0000269|PubMed:12602877}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
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DR EMBL; AF171094; AAD46683.1; -; mRNA.
DR AlphaFoldDB; Q9SW93; -.
DR SMR; Q9SW93; -.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:InterPro.
DR Gene3D; 1.10.110.10; -; 1.
DR InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR InterPro; IPR000528; Plant_nsLTP.
DR PANTHER; PTHR33076; PTHR33076; 1.
DR Pfam; PF00234; Tryp_alpha_amyl; 1.
DR PRINTS; PR00382; LIPIDTRNSFER.
DR SMART; SM00499; AAI; 1.
DR SUPFAM; SSF47699; SSF47699; 1.
DR PROSITE; PS00597; PLANT_LTP; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Lipid-binding; Signal;
KW Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:10634914"
FT CHAIN 23..113
FT /note="Stigma/stylar cysteine-rich adhesin"
FT /id="PRO_0000018417"
FT DISULFID 25..72
FT /evidence="ECO:0000250"
FT DISULFID 35..49
FT /evidence="ECO:0000250"
FT DISULFID 50..95
FT /evidence="ECO:0000250"
FT DISULFID 70..109
FT /evidence="ECO:0000250"
SQ SEQUENCE 113 AA; 11686 MW; F2E3D9725EFBE83A CRC64;
MARSSAVCFL LLLAFLIGTA SAITCGQVDS DLTSCLGYAR KGGVIPPGCC AGVRTLNNLA
KTTPDRQTAC NCLKSLVNPS LGLNAAIVAG IPGKCGVNIP YPIRMQTDCN KVR