ID A0A2P1HA25_ARTAN Unreviewed; 117 AA. AC A0A2P1HA25; DT 23-MAY-2018, integrated into UniProtKB/TrEMBL. DT 23-MAY-2018, sequence version 1. DT 10-APR-2019, entry version 4. DE RecName: Full=Non-specific lipid-transfer protein {ECO:0000256|RuleBase:RU000628}; GN Name=LTP1 {ECO:0000313|EMBL:AVN68375.1}; OS Artemisia annua (Sweet wormwood). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; campanulids; Asterales; Asteraceae; OC Asteroideae; Anthemideae; Artemisiinae; Artemisia. OX NCBI_TaxID=35608 {ECO:0000313|EMBL:AVN68375.1}; RN [1] {ECO:0000313|EMBL:AVN68375.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Leaf {ECO:0000313|EMBL:AVN68375.1}; RX PubMed=27421621; DOI=10.1016/j.ymben.2016.07.004; RA Wang B., Kashkooli A.B., Sallets A., Ting H.M., de Ruijter N.C., RA Olofsson L., Brodelius P., Pottier M., Boutry M., Bouwmeester H., RA van der Krol A.R.; RT "Transient production of artemisinin in Nicotiana benthamiana is RT boosted by a specific lipid transfer protein from A. annua."; RL Metab. Eng. 38:159-169(2016). RN [2] {ECO:0000313|EMBL:AVN68375.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Leaf {ECO:0000313|EMBL:AVN68375.1}; RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I., RA Dimitrov K.M., Suarez D.L., Swayne D.E.; RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Plant non-specific lipid-transfer proteins transfer CC phospholipids as well as galactolipids across membranes. May play CC a 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|RuleBase:RU000628, ECO:0000256|SAAS:SAAS00593559}. 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; KY860528; AVN68375.1; -; mRNA. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0006869; P:lipid transport; IEA:InterPro. DR InterPro; IPR036312; Bifun_inhib/LTP/seed_sf. DR InterPro; IPR016140; Bifunc_inhib/LTP/seed_store. DR InterPro; IPR000528; Plant_LTP. 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 2: Evidence at transcript level; KW Disulfide bond {ECO:0000256|SAAS:SAAS00486961}; KW Lipid-binding {ECO:0000256|RuleBase:RU000628}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transport {ECO:0000256|RuleBase:RU000628}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 117 Non-specific lipid-transfer protein. FT {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015166400. FT DOMAIN 28 113 AAI. {ECO:0000259|SMART:SM00499}. SQ SEQUENCE 117 AA; 12149 MW; 5D4DCFF49458A5D0 CRC64; MVGKVVLVVA IYFLVVAGLH AVEGEVTCDQ VVSNMTPCVT YLTSSGDSVP SDCCSGVNSL NNAATTTADK QAACKCLEQS ASQLSDIDLE KARSLPGKCG VNLPYEISPT TDCSTIQ //