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NLT2G_WHEAT
ID   NLT2G_WHEAT             Reviewed;          96 AA.
AC   P82900; Q2PCC8;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Non-specific lipid-transfer protein 2G;
DE            Short=LTP2G;
DE   AltName: Full=7 kDa lipid transfer protein 1;
DE   AltName: Full=Lipid transfer protein 2 isoform 1;
DE            Short=LTP2-1;
DE   Flags: Precursor;
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565 {ECO:0000305};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Leaf;
RX   PubMed=16983534; DOI=10.1007/s00425-006-0397-7;
RA   Boutrot F., Meynard D., Guiderdoni E., Joudrier P., Gautier M.-F.;
RT   "The Triticum aestivum non-specific lipid transfer protein (TaLtp) gene
RT   family: comparative promoter activity of six TaLtp genes in transgenic
RT   rice.";
RL   Planta 225:843-862(2007).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 30-96, FUNCTION, MASS SPECTROMETRY, AND DISULFIDE
RP   BONDS.
RC   TISSUE=Endosperm;
RX   PubMed=11231292; DOI=10.1046/j.1432-1327.2001.02007.x;
RA   Douliez J.-P., Pato C., Rabesona H., Molle D., Marion D.;
RT   "Disulfide bond assignment, lipid transfer activity and secondary structure
RT   of a 7-kDa plant lipid transfer protein, LTP2.";
RL   Eur. J. Biochem. 268:1400-1403(2001).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS) OF 30-96 IN COMPLEX WITH
RP   L-ALPHA-PALMITOYL-PHOSPHATIDYL GLYCEROL, AND DISULFIDE BONDS.
RX   PubMed=15805594; DOI=10.1107/s0907444905000417;
RA   Hoh F., Pons J.L., Gautier M.F., de Lamotte F., Dumas C.;
RT   "Structure of a liganded type 2 non-specific lipid-transfer protein from
RT   wheat and the molecular basis of lipid binding.";
RL   Acta Crystallogr. D 61:397-406(2005).
CC   -!- FUNCTION: Transfer lipids across membranes. May play a role in plant
CC       defense or in the biosynthesis of cuticle layers.
CC       {ECO:0000269|PubMed:11231292, ECO:0000303|PubMed:11231292}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=6971; Mass_error=1; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:11231292};
CC   -!- SIMILARITY: Belongs to the plant LTP family. B11E subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ852549; CAH69200.1; -; Genomic_DNA.
DR   PDB; 1N89; NMR; -; A=30-96.
DR   PDB; 1TUK; X-ray; 1.12 A; A=30-96.
DR   PDBsum; 1N89; -.
DR   PDBsum; 1TUK; -.
DR   AlphaFoldDB; P82900; -.
DR   SMR; P82900; -.
DR   STRING; 4565.Traes_4BL_AB3EBF1FD.2; -.
DR   Allergome; 8724; Tri a 7k-LTP.
DR   PRIDE; P82900; -.
DR   EnsemblPlants; TraesCAD_scaffold_031197_01G000500.1; TraesCAD_scaffold_031197_01G000500.1; TraesCAD_scaffold_031197_01G000500.
DR   EnsemblPlants; TraesCLE_scaffold_005285_01G000700.1; TraesCLE_scaffold_005285_01G000700.1; TraesCLE_scaffold_005285_01G000700.
DR   EnsemblPlants; TraesCS4B02G393300.1; TraesCS4B02G393300.1.cds1; TraesCS4B02G393300.
DR   EnsemblPlants; TraesPAR_scaffold_002158_01G000300.1; TraesPAR_scaffold_002158_01G000300.1; TraesPAR_scaffold_002158_01G000300.
DR   EnsemblPlants; TraesROB_scaffold_004343_01G000700.1; TraesROB_scaffold_004343_01G000700.1; TraesROB_scaffold_004343_01G000700.
DR   EnsemblPlants; TraesWEE_scaffold_028928_01G000300.1; TraesWEE_scaffold_028928_01G000300.1; TraesWEE_scaffold_028928_01G000300.
DR   Gramene; TraesCAD_scaffold_031197_01G000500.1; TraesCAD_scaffold_031197_01G000500.1; TraesCAD_scaffold_031197_01G000500.
DR   Gramene; TraesCLE_scaffold_005285_01G000700.1; TraesCLE_scaffold_005285_01G000700.1; TraesCLE_scaffold_005285_01G000700.
DR   Gramene; TraesCS4B02G393300.1; TraesCS4B02G393300.1.cds1; TraesCS4B02G393300.
DR   Gramene; TraesPAR_scaffold_002158_01G000300.1; TraesPAR_scaffold_002158_01G000300.1; TraesPAR_scaffold_002158_01G000300.
DR   Gramene; TraesROB_scaffold_004343_01G000700.1; TraesROB_scaffold_004343_01G000700.1; TraesROB_scaffold_004343_01G000700.
DR   Gramene; TraesWEE_scaffold_028928_01G000300.1; TraesWEE_scaffold_028928_01G000300.1; TraesWEE_scaffold_028928_01G000300.
DR   eggNOG; ENOG502S3N0; Eukaryota.
DR   HOGENOM; CLU_158223_2_0_1; -.
DR   OMA; TSCAMAI; -.
DR   EvolutionaryTrace; P82900; -.
DR   Proteomes; UP000019116; Unplaced.
DR   Genevisible; P82900; TA.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   CDD; cd01959; nsLTP2; 1.
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; IPR033872; nsLTP2.
DR   PANTHER; PTHR33214; PTHR33214; 1.
DR   Pfam; PF14368; LTP_2; 1.
DR   SUPFAM; SSF47699; SSF47699; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell wall; Cell wall biogenesis/degradation;
KW   Direct protein sequencing; Disulfide bond; Lipid transport; Lipid-binding;
KW   Reference proteome; Secreted; Signal; Transport.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000269|PubMed:11231292"
FT   CHAIN           30..96
FT                   /note="Non-specific lipid-transfer protein 2G"
FT                   /id="PRO_0000153893"
FT   DISULFID        31..63
FT                   /evidence="ECO:0000269|PubMed:11231292,
FT                   ECO:0000269|PubMed:15805594, ECO:0007744|PDB:1TUK"
FT   DISULFID        39..53
FT                   /evidence="ECO:0000269|PubMed:11231292,
FT                   ECO:0000269|PubMed:15805594, ECO:0007744|PDB:1TUK"
FT   DISULFID        54..89
FT                   /evidence="ECO:0000269|PubMed:11231292,
FT                   ECO:0000269|PubMed:15805594, ECO:0007744|PDB:1TUK"
FT   DISULFID        65..96
FT                   /evidence="ECO:0000269|PubMed:11231292,
FT                   ECO:0000269|PubMed:15805594, ECO:0007744|PDB:1TUK"
FT   HELIX           33..39
FT                   /evidence="ECO:0007829|PDB:1TUK"
FT   HELIX           40..45
FT                   /evidence="ECO:0007829|PDB:1TUK"
FT   HELIX           51..60
FT                   /evidence="ECO:0007829|PDB:1TUK"
FT   HELIX           61..63
FT                   /evidence="ECO:0007829|PDB:1TUK"
FT   HELIX           64..67
FT                   /evidence="ECO:0007829|PDB:1TUK"
FT   TURN            71..73
FT                   /evidence="ECO:0007829|PDB:1TUK"
FT   HELIX           74..77
FT                   /evidence="ECO:0007829|PDB:1TUK"
FT   HELIX           80..88
FT                   /evidence="ECO:0007829|PDB:1TUK"
SQ   SEQUENCE   96 AA;  9832 MW;  0016692D11293870 CRC64;
     MAGMMKKQVV TALMLALVVL AAAPGGARAA CQASQLAVCA SAILSGAKPS GECCGNLRAQ
     QGCFCQYAKD PTYGQYIRSP HARDTLTSCG LAVPHC
 
 
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