NLTP7_ARATH
ID NLTP7_ARATH Reviewed; 123 AA.
AC Q9ZUK6; B3H547; Q680R4;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Non-specific lipid-transfer protein 7;
DE Short=LTP 7;
DE Flags: Precursor;
GN Name=LTP7; OrderedLocusNames=At2g15050; ORFNames=T15J14.9;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9ZUK6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ZUK6-2; Sequence=VSP_035945, VSP_035946;
CC Name=3;
CC IsoId=Q9ZUK6-3; Sequence=VSP_035947;
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
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DR EMBL; AC005957; AAD03362.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06364.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06365.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06366.1; -; Genomic_DNA.
DR EMBL; AF325066; AAK17134.1; -; mRNA.
DR EMBL; AK175803; BAD43566.1; -; mRNA.
DR EMBL; AK220655; BAD95164.1; -; mRNA.
DR EMBL; BT024565; ABD38904.1; -; mRNA.
DR PIR; D84524; D84524.
DR RefSeq; NP_001118321.1; NM_001124849.2. [Q9ZUK6-3]
DR RefSeq; NP_001318227.1; NM_001335447.1. [Q9ZUK6-1]
DR RefSeq; NP_973466.1; NM_201737.3. [Q9ZUK6-2]
DR AlphaFoldDB; Q9ZUK6; -.
DR SMR; Q9ZUK6; -.
DR STRING; 3702.AT2G15050.1; -.
DR PaxDb; Q9ZUK6; -.
DR PRIDE; Q9ZUK6; -.
DR ProteomicsDB; 249121; -. [Q9ZUK6-1]
DR EnsemblPlants; AT2G15050.1; AT2G15050.1; AT2G15050. [Q9ZUK6-1]
DR EnsemblPlants; AT2G15050.2; AT2G15050.2; AT2G15050. [Q9ZUK6-2]
DR EnsemblPlants; AT2G15050.3; AT2G15050.3; AT2G15050. [Q9ZUK6-3]
DR GeneID; 815994; -.
DR Gramene; AT2G15050.1; AT2G15050.1; AT2G15050. [Q9ZUK6-1]
DR Gramene; AT2G15050.2; AT2G15050.2; AT2G15050. [Q9ZUK6-2]
DR Gramene; AT2G15050.3; AT2G15050.3; AT2G15050. [Q9ZUK6-3]
DR KEGG; ath:AT2G15050; -.
DR Araport; AT2G15050; -.
DR TAIR; locus:2055828; AT2G15050.
DR InParanoid; Q9ZUK6; -.
DR OMA; CASYLWR; -.
DR PhylomeDB; Q9ZUK6; -.
DR PRO; PR:Q9ZUK6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZUK6; baseline and differential.
DR Genevisible; Q9ZUK6; AT.
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; PF14368; LTP_2; 1.
DR PRINTS; PR00382; LIPIDTRNSFER.
DR SMART; SM00499; AAI; 1.
DR SUPFAM; SSF47699; SSF47699; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Lipid-binding; Reference proteome;
KW Signal; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..123
FT /note="Non-specific lipid-transfer protein 7"
FT /id="PRO_0000355616"
FT DISULFID 29..78
FT /evidence="ECO:0000255"
FT DISULFID 39..55
FT /evidence="ECO:0000255"
FT DISULFID 56..102
FT /evidence="ECO:0000255"
FT DISULFID 76..118
FT /evidence="ECO:0000255"
FT VAR_SEQ 113..115
FT /note="RFN -> SVR (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_035945"
FT VAR_SEQ 116..123
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_035946"
FT VAR_SEQ 121..123
FT /note="YIC -> VR (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_035947"
SQ SEQUENCE 123 AA; 12995 MW; 9CE09B76A9E22015 CRC64;
MAGLMKLGCL VFVFVIAAGP ITAKAALSCG EVNSNLKPCT GYLTNGGITS PGPQCCNGVR
KLNGMVLTTL DRRQACRCIK NAARNVGPGL NADRAAGIPR RCGIKIPYST QIRFNTKCNT
YIC
