NLTP1_ACTCC
ID NLTP1_ACTCC Reviewed; 114 AA.
AC P85204; A0A2R6PA47;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2019, sequence version 2.
DT 25-MAY-2022, entry version 15.
DE RecName: Full=Non-specific lipid-transfer protein 1 {ECO:0000303|PubMed:22114713};
DE Short=LTP1 {ECO:0000303|PubMed:22114713};
DE AltName: Allergen=Act c 10 {ECO:0000303|PubMed:22114713};
DE Flags: Precursor;
GN Name=NLTP1 {ECO:0000305};
GN ORFNames=CEY00_Acc30713 {ECO:0000312|EMBL:PSR87667.1};
OS Actinidia chinensis var. chinensis (Chinese soft-hair kiwi).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Ericales; Actinidiaceae; Actinidia.
OX NCBI_TaxID=1590841;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Red5;
RX PubMed=29661190; DOI=10.1186/s12864-018-4656-3;
RA Pilkington S.M., Crowhurst R., Hilario E., Nardozza S., Fraser L., Peng Y.,
RA Gunaseelan K., Simpson R., Tahir J., Deroles S.C., Templeton K., Luo Z.,
RA Davy M., Cheng C., McNeilage M., Scaglione D., Liu Y., Zhang Q., Datson P.,
RA De Silva N., Gardiner S.E., Bassett H., Chagne D., McCallum J.,
RA Dzierzon H., Deng C., Wang Y.Y., Barron L., Manako K., Bowen J.,
RA Foster T.M., Erridge Z.A., Tiffin H., Waite C.N., Davies K.M.,
RA Grierson E.P., Laing W.A., Kirk R., Chen X., Wood M., Montefiori M.,
RA Brummell D.A., Schwinn K.E., Catanach A., Fullerton C., Li D.,
RA Meiyalaghan S., Nieuwenhuizen N., Read N., Prakash R., Hunter D., Zhang H.,
RA McKenzie M., Knabel M., Harris A., Allan A.C., Gleave A., Chen A.,
RA Janssen B.J., Plunkett B., Ampomah-Dwamena C., Voogd C., Leif D.,
RA Lafferty D., Souleyre E.J.F., Varkonyi-Gasic E., Gambi F., Hanley J.,
RA Yao J.L., Cheung J., David K.M., Warren B., Marsh K., Snowden K.C.,
RA Lin-Wang K., Brian L., Martinez-Sanchez M., Wang M., Ileperuma N.,
RA Macnee N., Campin R., McAtee P., Drummond R.S.M., Espley R.V.,
RA Ireland H.S., Wu R., Atkinson R.G., Karunairetnam S., Bulley S.,
RA Chunkath S., Hanley Z., Storey R., Thrimawithana A.H., Thomson S.,
RA David C., Testolin R., Huang H., Hellens R.P., Schaffer R.J.;
RT "A manually annotated Actinidia chinensis var. chinensis (kiwifruit) genome
RT highlights the challenges associated with draft genomes and gene prediction
RT in plants.";
RL BMC Genomics 19:257-257(2018).
RN [2]
RP PROTEIN SEQUENCE OF 26-40, TISSUE SPECIFICITY, AND ALLERGENICITY.
RC TISSUE=Seed {ECO:0000269|PubMed:22114713};
RX PubMed=22114713; DOI=10.1371/journal.pone.0027856;
RA Bernardi M.L., Giangrieco I., Camardella L., Ferrara R., Palazzo P.,
RA Panico M.R., Crescenzo R., Carratore V., Zennaro D., Liso M., Santoro M.,
RA Zuzzi S., Tamburrini M., Ciardiello M.A., Mari A.;
RT "Allergenic lipid transfer proteins from plant-derived foods do not
RT immunologically and clinically behave homogeneously: the kiwifruit LTP as a
RT model.";
RL PLoS ONE 6:E27856-E27856(2011).
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|UniProtKB:Q42952}.
CC -!- TISSUE SPECIFICITY: Expressed in seeds and, at very low levels, in pulp
CC of fruit (at protein level). {ECO:0000269|PubMed:22114713}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC {ECO:0000269|PubMed:22114713}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
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DR EMBL; NKQK01000027; PSR87667.1; -; Genomic_DNA.
DR PDB; 7KSB; X-ray; 1.95 A; A/B=26-114.
DR PDBsum; 7KSB; -.
DR AlphaFoldDB; P85204; -.
DR SMR; P85204; -.
DR Allergome; 5735; Act c 10.
DR Allergome; 5736; Act c 10.0101.
DR EnsemblPlants; PSR87667; PSR87667; CEY00_Acc30713.
DR Gramene; PSR87667; PSR87667; CEY00_Acc30713.
DR OMA; SSTIACC; -.
DR Proteomes; UP000241394; Chromosome lg27.
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 1: Evidence at protein level;
KW 3D-structure; Allergen; Direct protein sequencing; Disulfide bond;
KW Lipid-binding; Reference proteome; Signal; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:22114713"
FT CHAIN 26..114
FT /note="Non-specific lipid-transfer protein 1"
FT /id="PRO_0000415602"
FT DISULFID 29..76
FT /evidence="ECO:0000250|UniProtKB:Q42952"
FT DISULFID 39..53
FT /evidence="ECO:0000250|UniProtKB:Q42952"
FT DISULFID 54..99
FT /evidence="ECO:0000250|UniProtKB:Q42952"
FT DISULFID 74..113
FT /evidence="ECO:0000250|UniProtKB:Q42952"
FT CONFLICT 35
FT /note="S -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 29..35
FT /evidence="ECO:0007829|PDB:7KSB"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:7KSB"
FT HELIX 40..45
FT /evidence="ECO:0007829|PDB:7KSB"
FT HELIX 51..63
FT /evidence="ECO:0007829|PDB:7KSB"
FT HELIX 67..83
FT /evidence="ECO:0007829|PDB:7KSB"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:7KSB"
SQ SEQUENCE 114 AA; 11664 MW; 1AB9706364E30393 CRC64;
MIKGLAITVV AVLAVVQLLA RPSDAAVSCG QVDTSLTPCL TYLTKGGTPS TQCCSGVRSL
KSMTGTKADR QAACNCLKQA AARYQGIKDA AAAALSQKCG VQLSVPISRK TDCS
