NLTP4_ARATH
ID NLTP4_ARATH Reviewed; 112 AA.
AC Q9LLR6; Q9FIE7;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Non-specific lipid-transfer protein 4;
DE Short=LTP 4;
DE Flags: Precursor;
GN Name=LTP4; OrderedLocusNames=At5g59310; ORFNames=MNC17.22;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=10940464; DOI=10.1016/s0168-9452(00)00232-6;
RA Arondel V.A., Vergnolle C., Cantrel C., Kader J.-C.;
RT "Lipid transfer proteins are encoded by a small multigene family in
RT Arabidopsis thaliana.";
RL Plant Sci. 157:1-12(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18674922; DOI=10.1016/j.plaphy.2008.06.011;
RA Sels J., Mathys J., De Coninck B.M.A., Cammue B.P.A., De Bolle M.F.C.;
RT "Plant pathogenesis-related (PR) proteins: a focus on PR peptides.";
RL Plant Physiol. Biochem. 46:941-950(2008).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09776.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF159801; AAF76930.1; -; mRNA.
DR EMBL; AB016890; BAB09776.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97170.1; -; Genomic_DNA.
DR EMBL; AY058233; AAL15407.1; -; mRNA.
DR EMBL; AY035015; AAK59520.1; -; mRNA.
DR EMBL; AY045644; AAK74002.1; -; mRNA.
DR EMBL; AY059081; AAL15187.1; -; mRNA.
DR EMBL; BT002397; AAO00757.1; -; mRNA.
DR EMBL; BT006514; AAP21322.1; -; mRNA.
DR EMBL; AY088209; AAM65751.1; -; mRNA.
DR RefSeq; NP_568904.1; NM_125322.3.
DR AlphaFoldDB; Q9LLR6; -.
DR SMR; Q9LLR6; -.
DR BioGRID; 21294; 2.
DR STRING; 3702.AT5G59310.1; -.
DR PaxDb; Q9LLR6; -.
DR ProteomicsDB; 251180; -.
DR EnsemblPlants; AT5G59310.1; AT5G59310.1; AT5G59310.
DR GeneID; 836050; -.
DR Gramene; AT5G59310.1; AT5G59310.1; AT5G59310.
DR KEGG; ath:AT5G59310; -.
DR Araport; AT5G59310; -.
DR TAIR; locus:2168459; AT5G59310.
DR eggNOG; ENOG502SAKZ; Eukaryota.
DR HOGENOM; CLU_128423_2_1_1; -.
DR InParanoid; Q9LLR6; -.
DR OMA; CLVLMCM; -.
DR OrthoDB; 1546493at2759; -.
DR PhylomeDB; Q9LLR6; -.
DR PRO; PR:Q9LLR6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LLR6; baseline and differential.
DR Genevisible; Q9LLR6; AT.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; TAS:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
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; Reference proteome; Signal; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..112
FT /note="Non-specific lipid-transfer protein 4"
FT /id="PRO_0000018364"
FT DISULFID 27..74
FT /evidence="ECO:0000255"
FT DISULFID 37..51
FT /evidence="ECO:0000255"
FT DISULFID 52..94
FT /evidence="ECO:0000255"
FT DISULFID 72..108
FT /evidence="ECO:0000255"
SQ SEQUENCE 112 AA; 11405 MW; 7B9ED24A794CEA01 CRC64;
MAFALRFFTC FVLTVFIVAS VDAAITCGTV ASSLSPCLGY LSKGGVVPPP CCAGVKKLNG
MAQTTPDRQQ ACRCLQSAAK GVNPSLASGL PGKCGVSIPY PISTSTNCAT IK
