ID NLTP1_ORYSJ Reviewed; 116 AA. AC Q0IQK9; O22484; P23096; P93434; Q2QYL1; DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 24. DE RecName: Full=Non-specific lipid-transfer protein 1; DE Short=LTP 1; DE Short=PAPI; DE Flags: Precursor; GN Name=LTP; OrderedLocusNames=Os12g0115100, LOC_Os12g02320; GN ORFNames=OsJ_033644; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=39947; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16188032; DOI=10.1186/1741-7007-3-20; RG The rice chromosomes 11 and 12 sequencing consortia; RT "The sequence of rice chromosomes 11 and 12, rich in disease RT resistance genes and recent gene duplications."; RL BMC Biol. 3:20-20(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16100779; DOI=10.1038/nature03895; RG International rice genome sequencing project (IRGSP); RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=17210932; DOI=10.1101/gr.5509507; RG The rice annotation project (RAP); RT "Curated genome annotation of Oryza sativa ssp. japonica and RT comparative genome analysis with Arabidopsis thaliana."; RL Genome Res. 17:175-183(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038; RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., RA Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., RA Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., RA Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., RA Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., RA Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., RA Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., RA Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., RA Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., RA Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., RA Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., RA Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., RA Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., RA Samudrala R., Wang J., Wong G.K.-S., Yang H.; RT "The genomes of Oryza sativa: a history of duplications."; RL PLoS Biol. 3:266-281(2005). RN [5] RP PROTEIN SEQUENCE OF 26-116. RC TISSUE=Seed; RX MEDLINE=88339366; PubMed=2458699; DOI=10.1016/0003-9861(88)90151-8; RA Yu Y.G., Chung C.H., Fowler A., Suh S.W.; RT "Amino acid sequence of a probable amylase/protease inhibitor from RT rice seeds."; RL Arch. Biochem. Biophys. 265:466-475(1988). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). RC TISSUE=Seed; RX MEDLINE=98173870; PubMed=9512714; DOI=10.1006/jmbi.1997.1550; RA Lee J.Y., Min K., Cha H., Shin D.H., Hwang K.Y., Suh S.W.; RT "Rice non-specific lipid transfer protein: the 1.6-A crystal structure RT in the unliganded state reveals a small hydrophobic cavity."; RL J. Mol. Biol. 276:437-448(1998). 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 -!- TISSUE SPECIFICITY: Aleurone (external part) of the seeds. CC -!- SIMILARITY: Belongs to the plant LTP family. CC -!- CAUTION: Was originally thought to be an inhibitor of alpha- CC amylase or of a protease and was known as PAPI: probable alpha- CC amylase/protease inhibitor. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DP000011; ABA96284.1; -; Genomic_DNA. DR EMBL; AP008218; BAF29006.1; -; Genomic_DNA. DR EMBL; CM000149; EAZ19435.1; -; Genomic_DNA. DR RefSeq; NP_001065987.1; -. DR UniGene; Os.8629; -. DR PDB; 1BV2; NMR; -; A=26-116. DR PDB; 1RZL; X-ray; 1.60 A; A=26-116. DR PDB; 1UVA; X-ray; 2.50 A; A=26-116. DR PDB; 1UVB; X-ray; 2.10 A; A=26-116. DR PDB; 1UVC; X-ray; 2.00 A; A/B=26-116. DR PDBsum; 1BV2; -. DR PDBsum; 1RZL; -. DR PDBsum; 1UVA; -. DR PDBsum; 1UVB; -. DR PDBsum; 1UVC; -. DR GeneID; 4351318; -. DR KEGG; osa:4351318; -. DR Gramene; P23096; -. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0006869; P:lipid transport; IEA:InterPro. DR InterPro; IPR013770; LPT_helical. DR InterPro; IPR003612; LTP/seed_store/tryp_amyl_inhib. DR InterPro; IPR000528; Plant_LTP. DR Gene3D; G3DSA:1.10.110.10; LPT_helical; 1. DR Pfam; PF00234; Tryp_alpha_amyl; 1. DR PRINTS; PR00382; LIPIDTRNSFER. DR SMART; SM00499; AAI; 1. DR PROSITE; PS00597; PLANT_LTP; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; KW Lipid-binding; Signal; Transport. FT SIGNAL 1 25 FT CHAIN 26 116 Non-specific lipid-transfer protein 1. FT /FTId=PRO_0000018391. FT DISULFID 28 75 FT DISULFID 38 52 FT DISULFID 53 98 FT DISULFID 73 112 FT HELIX 28 35 FT HELIX 36 38 FT HELIX 39 42 FT HELIX 50 62 FT HELIX 66 81 FT HELIX 88 92 FT HELIX 94 98 FT HELIX 112 114 SQ SEQUENCE 116 AA; 11345 MW; 54612FE0D79F9D5D CRC64; MARAQLVLVA LVAALLLAAP HAAVAITCGQ VNSAVGPCLT YARGGAGPSA ACCSGVRSLK AAASTTADRR TACNCLKNAA RGIKGLNAGN AASIPSKCGV SVPYTISASI DCSRVS //