2RKN | pdb_00002rkn

X-ray structure of the self-defense and signaling protein DIR1 from Arabidopsis taliana

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Tryp_alpha_amyl_1	e2rknA1	A: alpha superhelices	X: Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin-like	H: Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin/Protein HNS-dependent expression A HdeA	T: Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin	F: Tryp_alpha_amyl_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.110.10	Mainly Alpha	Orthogonal Bundle	Hydrophobic Seed Protein	Plant lipid-transfer and hydrophobic proteins	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF14368	Probable lipid transfer (LTP_2)	Probable lipid transfer	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	DIR1 protein	fatty acid binding organic acid binding binding ion binding anion binding lipid binding carboxylic acid binding monocarboxylic acid binding small molecule binding cation binding transition metal ion binding zinc ion binding metal ion binding	localization transport macromolecule localization lipid localization lipid transport establishment of localization cellular response to stimulus biological process involved in interspecies interaction between organisms regulation of cellular process response to stimulus signaling response to biotic stimulus response to salicylic acid cell communication localization transport macromolecule localization lipid localization lipid transport establishment of localization cellular response to stimulus biological process involved in interspecies interaction between organisms regulation of cellular process response to stimulus signaling response to biotic stimulus response to salicylic acid cell communication response to stress response to external biotic stimulus signal transduction salicylic acid mediated signaling pathway cellular response to salicylic acid stimulus systemic acquired resistance regulation of biological process response to other organism defense response biological regulation response to oxygen-containing compound defense response to symbiont response to external stimulus systemic acquired resistance, salicylic acid mediated signaling pathway cellular response to oxygen-containing compound cellular response to chemical stimulus defense response to other organism response to chemical cellular process	membrane-bounded organelle intracellular anatomical structure intracellular vesicle intracellular membrane-bounded organelle intracellular organelle cellular anatomical structure cytoplasmic vesicle organelle secretory vesicle cytoplasm vesicle cell-cell junction symplast anchoring junction membrane-bounded organelle intracellular anatomical structure intracellular vesicle intracellular membrane-bounded organelle intracellular organelle cellular anatomical structure cytoplasmic vesicle organelle secretory vesicle cytoplasm vesicle cell-cell junction symplast anchoring junction cell junction plasmodesma extracellular region apoplast endoplasmic reticulum endomembrane system

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR036312	Bifunctional inhibitor/plant lipid transfer protein/seed storage helical domain superfamily	Homologous Superfamily
A	IPR016140	Bifunctional inhibitor/plant lipid transfer protein/seed storage helical domain	Domain
A	IPR044741	Non-specific lipid-transfer protein-like	Domain
A	IPR039265	Putative lipid-transfer protein DIR1-like	Family

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.