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NLTPD_BRAOT
ID   NLTPD_BRAOT             Reviewed;         118 AA.
AC   Q43304;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Non-specific lipid-transfer protein D;
DE            Short=LTP D;
DE   AltName: Full=Wax-associated protein 9D;
DE   Flags: Precursor;
GN   Name=WAX9D;
OS   Brassica oleracea var. italica (Broccoli).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=36774;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=8203911; DOI=10.1006/abbi.1994.1263;
RA   Pyee J., Yu H., Kolattukudy P.E.;
RT   "Identification of a lipid transfer protein as the major protein in the
RT   surface wax of broccoli (Brassica oleracea) leaves.";
RL   Arch. Biochem. Biophys. 311:460-468(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Green sprouting; TISSUE=Leaf;
RX   PubMed=7894511; DOI=10.1046/j.1365-313x.1995.07010049.x;
RA   Pyee J., Kolattukudy P.E.;
RT   "The gene for the major cuticular wax-associated protein and three
RT   homologous genes from broccoli (Brassica oleracea) and their expression
RT   patterns.";
RL   Plant J. 7:49-59(1995).
CC   -!- FUNCTION: Plant non-specific lipid-transfer proteins transfer
CC       phospholipids as well as galactolipids across membranes. May play a
CC       role in wax or cutin deposition in the cell walls of expanding
CC       epidermal cells and certain secretory tissues.
CC   -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
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DR   EMBL; L29767; AAA32995.1; -; mRNA.
DR   EMBL; L33907; AAA73948.1; -; Genomic_DNA.
DR   PIR; S45680; S45680.
DR   AlphaFoldDB; Q43304; -.
DR   SMR; Q43304; -.
DR   PRIDE; Q43304; -.
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   3: Inferred from homology;
KW   Disulfide bond; Lipid-binding; Signal; Transport.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..118
FT                   /note="Non-specific lipid-transfer protein D"
FT                   /id="PRO_0000018373"
FT   DISULFID        29..77
FT                   /evidence="ECO:0000255"
FT   DISULFID        39..54
FT                   /evidence="ECO:0000255"
FT   DISULFID        55..100
FT                   /evidence="ECO:0000255"
FT   DISULFID        75..114
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   118 AA;  11937 MW;  53214BCDC4491DFC CRC64;
     MAGLMKLACL IFACMIVAGP ITSNAALSCG TVSGYVAPCI GYLAQNAPAV PTACCSGVTS
     LNNMARTTPD RQQACRCLVG AANALPTINV ARAAGLPKAC GVNIPYKISK TTNCNSVK
 
 
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