NLTP1_ORYSJ
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 03-AUG-2022, entry version 95.
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; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
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 resistance
RT 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=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
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., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., 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 [6]
RP PROTEIN SEQUENCE OF 26-116.
RC TISSUE=Seed;
RX 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 rice
RT seeds.";
RL Arch. Biochem. Biophys. 265:466-475(1988).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 26-116, AND DISULFIDE BONDS.
RC TISSUE=Seed;
RX 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 in
RT 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 a
CC 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. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be an inhibitor of alpha-amylase or
CC of a protease and was known as PAPI: probable alpha-amylase/protease
CC inhibitor. {ECO:0000305}.
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DR EMBL; DP000011; ABA96284.1; -; Genomic_DNA.
DR EMBL; AP008218; BAF29006.1; -; Genomic_DNA.
DR EMBL; AP014968; BAT15595.1; -; Genomic_DNA.
DR EMBL; CM000149; EAZ19435.1; -; Genomic_DNA.
DR RefSeq; XP_015620385.1; XM_015764899.1.
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 AlphaFoldDB; Q0IQK9; -.
DR SMR; Q0IQK9; -.
DR STRING; 4530.OS12T0115100-00; -.
DR Allergome; 2788; Ory s 14.
DR PaxDb; Q0IQK9; -.
DR PRIDE; Q0IQK9; -.
DR EnsemblPlants; Os12t0115100-00; Os12t0115100-00; Os12g0115100.
DR GeneID; 4351318; -.
DR Gramene; Os12t0115100-00; Os12t0115100-00; Os12g0115100.
DR KEGG; osa:4351318; -.
DR eggNOG; ENOG502S4CI; Eukaryota.
DR HOGENOM; CLU_128423_0_0_1; -.
DR InParanoid; Q0IQK9; -.
DR OMA; CLVLMCM; -.
DR OrthoDB; 1546493at2759; -.
DR EvolutionaryTrace; Q0IQK9; -.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000007752; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 12.
DR ExpressionAtlas; Q0IQK9; baseline and differential.
DR Genevisible; Q0IQK9; OS.
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 3D-structure; Direct protein sequencing; Disulfide bond; Lipid-binding;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:2458699"
FT CHAIN 26..116
FT /note="Non-specific lipid-transfer protein 1"
FT /id="PRO_0000018391"
FT DISULFID 28..75
FT /evidence="ECO:0000269|PubMed:9512714,
FT ECO:0007744|PDB:1RZL"
FT DISULFID 38..52
FT /evidence="ECO:0000269|PubMed:9512714,
FT ECO:0007744|PDB:1RZL"
FT DISULFID 53..98
FT /evidence="ECO:0000269|PubMed:9512714,
FT ECO:0007744|PDB:1RZL"
FT DISULFID 73..112
FT /evidence="ECO:0000269|PubMed:9512714,
FT ECO:0007744|PDB:1RZL"
FT HELIX 28..35
FT /evidence="ECO:0007829|PDB:1RZL"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1RZL"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:1RZL"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:1UVC"
FT HELIX 50..62
FT /evidence="ECO:0007829|PDB:1RZL"
FT HELIX 66..81
FT /evidence="ECO:0007829|PDB:1RZL"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:1RZL"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:1RZL"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:1UVA"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1RZL"
SQ SEQUENCE 116 AA; 11345 MW; 54612FE0D79F9D5D CRC64;
MARAQLVLVA LVAALLLAAP HAAVAITCGQ VNSAVGPCLT YARGGAGPSA ACCSGVRSLK
AAASTTADRR TACNCLKNAA RGIKGLNAGN AASIPSKCGV SVPYTISASI DCSRVS
