GenomeNet

Database: UniProt
Entry: A0A2H5P3T5_CITUN
LinkDB: A0A2H5P3T5_CITUN
Original site: A0A2H5P3T5_CITUN 
ID   A0A2H5P3T5_CITUN        Unreviewed;       117 AA.
AC   A0A2H5P3T5;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Non-specific lipid-transfer protein {ECO:0000256|RuleBase:RU000628};
GN   ORFNames=CUMW_100820 {ECO:0000313|EMBL:GAY46941.1};
OS   Citrus unshiu (Satsuma mandarin) (Citrus nobilis var. unshiu).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=55188 {ECO:0000313|EMBL:GAY46941.1};
RN   [1] {ECO:0000313|EMBL:GAY46941.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=29259619; DOI=10.3389/fgene.2017.00180;
RA   Shimizu T., Tanizawa Y., Mochizuki T., Nagasaki H., Yoshioka T., Toyoda A.,
RA   Fujiyama A., Kaminuma E., Nakamura Y.;
RT   "Draft sequencing of the heterozygous diploid genome of Satsuma (Citrus
RT   unshiu Marc.) using a hybrid assembly approach.";
RL   Front. Genet. 8:180-180(2017).
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       {ECO:0000256|RuleBase:RU000628}.
CC   -!- SIMILARITY: Belongs to the plant LTP family.
CC       {ECO:0000256|ARBA:ARBA00009748, ECO:0000256|RuleBase:RU000628}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAY46941.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BDQV01000036; GAY46941.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H5P3T5; -.
DR   STRING; 55188.A0A2H5P3T5; -.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:InterPro.
DR   CDD; cd01960; nsLTP1; 1.
DR   Gene3D; 1.10.110.10; Plant lipid-transfer and hydrophobic proteins; 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:SF53; NODULE CYSTEINE-RICH (NCR) SECRETED PEPTIDE; 1.
DR   PANTHER; PTHR33076; NON-SPECIFIC LIPID-TRANSFER PROTEIN 2-RELATED; 1.
DR   Pfam; PF00234; Tryp_alpha_amyl; 1.
DR   PRINTS; PR00382; LIPIDTRNSFER.
DR   SMART; SM00499; AAI; 1.
DR   SUPFAM; SSF47699; Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin; 1.
PE   3: Inferred from homology;
KW   Lipid-binding {ECO:0000256|RuleBase:RU000628};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transport {ECO:0000256|RuleBase:RU000628}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..117
FT                   /note="Non-specific lipid-transfer protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014131591"
FT   DOMAIN          31..115
FT                   /note="Bifunctional inhibitor/plant lipid transfer
FT                   protein/seed storage helical"
FT                   /evidence="ECO:0000259|SMART:SM00499"
SQ   SEQUENCE   117 AA;  11855 MW;  C0A23E3E1E2211F0 CRC64;
     MKKGGAVISM LVVFAMVQLL AAKPGEAAIT CGQEDSSLAS CIPYLMGGGN PAAACCDGLK
     NLKAITPTTA DRRAACDCVK AAAARNPNIK ENAASSLPSK CGVQIDIPIS KTTNCAK
//
DBGET integrated database retrieval system