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NLTP2_ARATH
ID   NLTP2_ARATH             Reviewed;         118 AA.
AC   Q9S7I3; Q3C1C6; Q41935; Q43277; Q43280;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Non-specific lipid-transfer protein 2;
DE            Short=LTP 2;
DE   AltName: Full=Protein CELL GROWTH DEFECT FACTOR 3;
DE   Flags: Precursor;
GN   Name=LTP2; Synonyms=CDF3; OrderedLocusNames=At2g38530; ORFNames=T6A23.27;
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 [GENOMIC DNA].
RC   STRAIN=cv. Wassilewskija;
RX   PubMed=10189704; DOI=10.1093/oxfordjournals.pcp.a029476;
RA   Clark A.M., Bohnert H.J.;
RT   "Cell-specific expression of genes of the lipid transfer protein family
RT   from Arabidopsis thaliana.";
RL   Plant Cell Physiol. 40:69-76(1999).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=18050905;
RA   Kim K.-M., Jun D.-Y., Kim S.-K., Kim C.-K., Kim B.O., Kim Y.-H., Park W.,
RA   Sohn J.-K., Hirata A., Kawai-Yamada M., Uchimiya H., Kim D.-H., Sul I.-W.;
RT   "Identification of novel mitochondrial membrane protein (Cdf 3) from
RT   Arabidopsis thaliana and its functional analysis in a yeast system.";
RL   J. Microbiol. Biotechnol. 17:891-896(2007).
RN   [4]
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   [5]
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   [6]
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   [7]
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-79; 51-118 AND 69-118.
RC   STRAIN=cv. Columbia; TISSUE=Green siliques;
RX   PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA   Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA   Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA   Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA   Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA   Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT   "An inventory of 1152 expressed sequence tags obtained by partial
RT   sequencing of cDNAs from Arabidopsis thaliana.";
RL   Plant J. 4:1051-1061(1993).
RN   [9]
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}.
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DR   EMBL; AF057357; AAC24829.1; -; Genomic_DNA.
DR   EMBL; AF159799; AAF76928.1; -; mRNA.
DR   EMBL; AB238795; BAE46870.1; -; mRNA.
DR   EMBL; AC005499; AAC67365.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09546.1; -; Genomic_DNA.
DR   EMBL; AY059927; AAL24409.1; -; mRNA.
DR   EMBL; AY081562; AAM10124.1; -; mRNA.
DR   EMBL; AY085800; AAM63016.1; -; mRNA.
DR   EMBL; Z17770; CAA79060.1; -; mRNA.
DR   EMBL; Z17787; CAA79068.1; -; mRNA.
DR   EMBL; Z18168; CAA79122.1; -; mRNA.
DR   PIR; B84806; B84806.
DR   RefSeq; NP_181387.1; NM_129410.5.
DR   AlphaFoldDB; Q9S7I3; -.
DR   SMR; Q9S7I3; -.
DR   BioGRID; 3777; 2.
DR   STRING; 3702.AT2G38530.1; -.
DR   Allergome; 1085; Ara t 3.
DR   PaxDb; Q9S7I3; -.
DR   PRIDE; Q9S7I3; -.
DR   ProteomicsDB; 250537; -.
DR   EnsemblPlants; AT2G38530.1; AT2G38530.1; AT2G38530.
DR   GeneID; 818435; -.
DR   Gramene; AT2G38530.1; AT2G38530.1; AT2G38530.
DR   KEGG; ath:AT2G38530; -.
DR   Araport; AT2G38530; -.
DR   TAIR; locus:2064107; AT2G38530.
DR   eggNOG; ENOG502S4CI; Eukaryota.
DR   HOGENOM; CLU_128423_0_0_1; -.
DR   InParanoid; Q9S7I3; -.
DR   OMA; ETLPAKC; -.
DR   OrthoDB; 1546493at2759; -.
DR   PhylomeDB; Q9S7I3; -.
DR   PRO; PR:Q9S7I3; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9S7I3; baseline and differential.
DR   Genevisible; Q9S7I3; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0005768; C:endosome; HDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0042335; P:cuticle development; IMP:TAIR.
DR   GO; GO:0006649; P:phospholipid transfer to membrane; NAS:TAIR.
DR   GO; GO:0090627; P:plant epidermal cell differentiation; IMP:TAIR.
DR   GO; GO:1901957; P:regulation of cutin biosynthetic process; IMP: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..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..118
FT                   /note="Non-specific lipid-transfer protein 2"
FT                   /id="PRO_0000018362"
FT   DISULFID        29..76
FT                   /evidence="ECO:0000255"
FT   DISULFID        39..53
FT                   /evidence="ECO:0000255"
FT   DISULFID        54..100
FT                   /evidence="ECO:0000255"
FT   DISULFID        74..114
FT                   /evidence="ECO:0000255"
FT   CONFLICT        69
FT                   /note="D -> N (in Ref. 8; CAA79122)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   118 AA;  11938 MW;  88490E003188B6AC CRC64;
     MAGVMKLACM VLACMIVAGP ITANALMSCG TVNGNLAGCI AYLTRGAPLT QGCCNGVTNL
     KNMASTTPDR QQACRCLQSA AKAVGPGLNT ARAAGLPSAC KVNIPYKISA STNCNTVR
 
 
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