DIRL1_ARATH
ID DIRL1_ARATH Reviewed; 102 AA.
AC Q8W453; Q8LEU7;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Putative lipid-transfer protein DIR1;
DE AltName: Full=Protein DEFECTIVE IN INDUCED RESISTANCE 1;
DE Flags: Precursor;
GN Name=DIR1; OrderedLocusNames=At5g48485; ORFNames=MJE7;
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], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=12353036; DOI=10.1038/nature00962;
RA Maldonado A.M., Doerner P., Dixon R.A., Lamb C.J., Cameron R.K.;
RT "A putative lipid transfer protein involved in systemic resistance
RT signalling in Arabidopsis.";
RL Nature 419:399-403(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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 FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY GLYCEROL-3-PHOSPHATE,
RP SUBCELLULAR LOCATION, INTERACTION WITH AZI1, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=23602565; DOI=10.1016/j.celrep.2013.03.030;
RA Yu K., Soares J.M., Mandal M.K., Wang C., Chanda B., Gifford A.N.,
RA Fowler J.S., Navarre D., Kachroo A., Kachroo P.;
RT "A feedback regulatory loop between G3P and lipid transfer proteins DIR1
RT and AZI1 mediates azelaic-acid-induced systemic immunity.";
RL Cell Rep. 3:1266-1278(2013).
RN [7]
RP LACK OF INTERACTION WITH PDLP1.
RX PubMed=27078071; DOI=10.1016/j.chom.2016.03.006;
RA Lim G.H., Shine M.B., de Lorenzo L., Yu K., Cui W., Navarre D., Hunt A.G.,
RA Lee J.Y., Kachroo A., Kachroo P.;
RT "Plasmodesmata localizing proteins regulate transport and signaling during
RT systemic acquired immunity in plants.";
RL Cell Host Microbe 19:541-549(2016).
RN [8] {ECO:0007744|PDB:2RKN}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 26-102 IN COMPLEX WITH FATTY ACID
RP ANALOG AND ZINC IONS, FUNCTION, AND DISULFIDE BONDS.
RX PubMed=18552128; DOI=10.1110/ps.035972.108;
RA Lascombe M.B., Bakan B., Buhot N., Marion D., Blein J.P., Larue V.,
RA Lamb C., Prange T.;
RT "The structure of 'defective in induced resistance' protein of Arabidopsis
RT thaliana, DIR1, reveals a new type of lipid transfer protein.";
RL Protein Sci. 17:1522-1530(2008).
CC -!- FUNCTION: Putative lipid transfer protein required for systemic
CC acquired resistance (SAR) long distance signaling. May interact with a
CC lipid-derived molecule to promote long distance signaling associated
CC with SAR. Together with AZI1, required for glycerol-3-phosphate- (G3P)
CC and azelaic acid- (AA) induced systemic acquired resistance (SAR).
CC Component of plant systemic immunity involved in priming defenses in a
CC AA-dependent manner, by modulating production and/or translocation of a
CC mobile signal(s) during SAR. Is able to bind with high affinity
CC monoacylated phospholipids, mainly lysophosphatidylcholines
CC (PubMed:18552128). {ECO:0000269|PubMed:12353036,
CC ECO:0000269|PubMed:18552128, ECO:0000269|PubMed:23602565}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- SUBUNIT: Self-interacts and binds to AZI1 (PubMed:23602565). Does not
CC interact with PDLP1 (PubMed:27078071). {ECO:0000269|PubMed:23602565,
CC ECO:0000269|PubMed:27078071}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000305}. Endoplasmic reticulum {ECO:0000269|PubMed:23602565}.
CC Cell junction, plasmodesma {ECO:0000269|PubMed:23602565}.
CC -!- INDUCTION: Induced by glycerol-3-phosphate (G3P).
CC {ECO:0000269|PubMed:23602565}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC condition, but compromised pathogen-induced glycerol-3-phosphate-(G3P)
CC and azelaic acid- (AA) dependent systemic acquired resistance (SAR).
CC {ECO:0000269|PubMed:12353036, ECO:0000269|PubMed:23602565}.
CC -!- SIMILARITY: Belongs to the A9/FIL1 family. {ECO:0000305}.
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DR EMBL; AF342726; AAL76110.1; -; Genomic_DNA.
DR EMBL; AB020745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED95676.1; -; Genomic_DNA.
DR EMBL; AY062857; AAL32935.1; -; mRNA.
DR EMBL; BT006510; AAP21318.1; -; mRNA.
DR EMBL; AY085224; AAM62457.1; -; mRNA.
DR RefSeq; NP_568699.1; NM_124224.3.
DR PDB; 2RKN; X-ray; 1.60 A; A=26-102.
DR PDBsum; 2RKN; -.
DR AlphaFoldDB; Q8W453; -.
DR SMR; Q8W453; -.
DR BioGRID; 20150; 2.
DR STRING; 3702.AT5G48485.1; -.
DR PaxDb; Q8W453; -.
DR PRIDE; Q8W453; -.
DR ProteomicsDB; 224118; -.
DR EnsemblPlants; AT5G48485.1; AT5G48485.1; AT5G48485.
DR GeneID; 834904; -.
DR Gramene; AT5G48485.1; AT5G48485.1; AT5G48485.
DR KEGG; ath:AT5G48485; -.
DR Araport; AT5G48485; -.
DR TAIR; locus:505006681; AT5G48485.
DR eggNOG; ENOG502S7QX; Eukaryota.
DR HOGENOM; CLU_145659_1_0_1; -.
DR InParanoid; Q8W453; -.
DR OMA; SHADINC; -.
DR OrthoDB; 1541738at2759; -.
DR PhylomeDB; Q8W453; -.
DR EvolutionaryTrace; Q8W453; -.
DR PRO; PR:Q8W453; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8W453; differential.
DR Genevisible; Q8W453; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; IDA:UniProtKB.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0005504; F:fatty acid binding; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0009627; P:systemic acquired resistance; IMP:TAIR.
DR GO; GO:0009862; P:systemic acquired resistance, salicylic acid mediated signaling pathway; IMP:UniProtKB.
DR CDD; cd04660; nsLTP_like; 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; IPR039265; DIR1-like.
DR InterPro; IPR044741; NsLTP-like.
DR PANTHER; PTHR33122; PTHR33122; 1.
DR Pfam; PF14368; LTP_2; 1.
DR SMART; SM00499; AAI; 1.
DR SUPFAM; SSF47699; SSF47699; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoplast; Cell junction; Disulfide bond;
KW Endoplasmic reticulum; Lipid transport; Lipid-binding; Metal-binding;
KW Plant defense; Reference proteome; Secreted; Signal; Transport; Zinc.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..102
FT /note="Putative lipid-transfer protein DIR1"
FT /id="PRO_0000401376"
FT BINDING 34
FT /ligand="a 1-acyl-sn-glycero-3-phosphocholine"
FT /ligand_id="ChEBI:CHEBI:58168"
FT /evidence="ECO:0000305|PubMed:18552128,
FT ECO:0007744|PDB:2RKN"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:18552128,
FT ECO:0007744|PDB:2RKN"
FT BINDING 38
FT /ligand="a 1-acyl-sn-glycero-3-phosphocholine"
FT /ligand_id="ChEBI:CHEBI:58168"
FT /evidence="ECO:0000305|PubMed:18552128,
FT ECO:0007744|PDB:2RKN"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:18552128,
FT ECO:0007744|PDB:2RKN"
FT DISULFID 30..67
FT /evidence="ECO:0000269|PubMed:18552128"
FT DISULFID 40..56
FT /evidence="ECO:0000269|PubMed:18552128"
FT DISULFID 57..94
FT /evidence="ECO:0000269|PubMed:18552128"
FT DISULFID 69..102
FT /evidence="ECO:0000269|PubMed:18552128"
FT CONFLICT 9
FT /note="V -> A (in Ref. 5; AAM62457)"
FT /evidence="ECO:0000305"
FT HELIX 34..40
FT /evidence="ECO:0007829|PDB:2RKN"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:2RKN"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:2RKN"
FT HELIX 54..60
FT /evidence="ECO:0007829|PDB:2RKN"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:2RKN"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:2RKN"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:2RKN"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:2RKN"
SQ SEQUENCE 102 AA; 10702 MW; 297614408B34EB32 CRC64;
MASKKAAMVM MAMIVIMAML VDTSVAIDLC GMSQDELNEC KPAVSKENPT SPSQPCCTAL
QHADFACLCG YKNSPWLGSF GVDPELASAL PKQCGLANAP TC
