1OIP

The Molecular Basis of Vitamin E Retention: Structure of Human Alpha-Tocopherol Transfer Protein

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1oipa1	All alpha proteins	RuvA C-terminal domain-like	CRAL/TRIO N-terminal domain	CRAL/TRIO N-terminal domain	Alpha-tocopherol transfer protein	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d1oipa2	Alpha and beta proteins (a/b)	SpoIIaa-like	CRAL/TRIO domain	CRAL/TRIO domain	Alpha-tocopherol transfer protein	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	CRAL/TRIO domain	8040349	3001058	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	CRAL/TRIO N-terminal domain	8040363	3001241	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	CRAL_TRIO_N	e1oipA1	A: alpha arrays	X: RuvA-C	H: RuvA-C, UBA, CRAL/TRIO-N, HBS1 (From Topology)	T: RuvA-C, UBA, CRAL/TRIO-N, HBS1	F: CRAL_TRIO_N	ECOD (1.6)
A	CRAL_TRIO	e1oipA2	A: a/b three-layered sandwiches	X: SpoIIaa-like (From Topology)	H: SpoIIaa-like (From Topology)	T: SpoIIaa-like	F: CRAL_TRIO	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.8.20	Mainly Alpha	Orthogonal Bundle	Helicase, Ruva Protein	domain 3	CATH (4.3.0)
A	1.20.5.1200	Mainly Alpha	Up-down Bundle	Single alpha-helices involved in coiled-coils or other helix-helix interfaces	Alpha-tocopherol transfer	CATH (4.3.0)
A	3.40.525.10	Alpha Beta	3-Layer(aba) Sandwich	Phosphatidylinositol Transfer Protein Sec14p	CRAL-TRIO lipid binding domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00650	CRAL/TRIO domain (CRAL_TRIO)	CRAL/TRIO domain	-	Domain
A	PF03765	CRAL/TRIO, N-terminal domain (CRAL_TRIO_N)	CRAL/TRIO, N-terminal domain	This all-alpha domain is found to the N-terminus of Pfam:PF00650.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	ALPHA-TOCOPHEROL TRANSFER PROTEIN	binding ion binding phosphatidylinositol-4,5-bisphosphate binding anion binding phosphatidylinositol bisphosphate binding phospholipid binding lipid binding phosphatidylinositol phosphate binding phosphatidylinositol binding small molecule binding phosphatidylinositol-3,4-bisphosphate binding vitamin binding organic cyclic compound binding heterocyclic compound binding binding ion binding phosphatidylinositol-4,5-bisphosphate binding anion binding phosphatidylinositol bisphosphate binding phospholipid binding lipid binding phosphatidylinositol phosphate binding phosphatidylinositol binding small molecule binding phosphatidylinositol-3,4-bisphosphate binding vitamin binding organic cyclic compound binding heterocyclic compound binding vitamin E binding lipid transporter activity lipid transfer activity transporter activity	localization transport vitamin transport establishment of localization vitamin E metabolic process fat-soluble vitamin metabolic process organic hydroxy compound metabolic process metabolic process cellular process small molecule metabolic process vitamin metabolic process membrane organization intermembrane lipid transfer lipid localization localization transport vitamin transport establishment of localization vitamin E metabolic process fat-soluble vitamin metabolic process organic hydroxy compound metabolic process metabolic process cellular process small molecule metabolic process vitamin metabolic process membrane organization intermembrane lipid transfer lipid localization lipid transport cellular component organization macromolecule localization cellular component organization or biogenesis multicellular organismal process regulation of biological process biological regulation positive regulation of biological process positive regulation of amyloid-beta clearance positive regulation of multicellular organismal process regulation of multicellular organismal process amyloid-beta clearance regulation of amyloid-beta clearance primary metabolic process lipid metabolic process developmental process placenta development chordate embryonic development animal organ development embryo development in utero embryonic development multicellular organism development embryonic placenta development embryo development ending in birth or egg hatching anatomical structure development embryonic organ development regulation of cellular process regulation of developmental process cellular developmental process regulation of establishment of blood-brain barrier negative regulation of biological process cell development regulation of cell differentiation regulation of cell development cell differentiation negative regulation of cellular process negative regulation of cell differentiation system development establishment of blood-brain barrier negative regulation of developmental process nervous system development negative regulation of cell development central nervous system development negative regulation of establishment of blood-brain barrier response to stimulus response to chemical response to toxic substance	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol membrane-bounded organelle endosome intracellular vesicle intracellular membrane-bounded organelle endomembrane system intracellular organelle cytoplasmic vesicle organelle late endosome vesicle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR001251	CRAL-TRIO lipid binding domain	Domain
A	IPR036865	CRAL-TRIO lipid binding domain superfamily	Homologous Superfamily
A	IPR011074	CRAL/TRIO, N-terminal domain	Domain
A	IPR036273	CRAL/TRIO, N-terminal domain superfamily	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A	Pharos: P49638	familial isolated deficiency of vitamin E retinitis pigmentosa muscular atrophy nervous system disorder speech disorder atherosclerosis Vitamin E Deficiency hearing disorder hyperreflexia retinal disease vision disorder lung cancer arteriosclerosis disorder cone-rod dystrophy pancreatic ductal adenocarcinoma familial isolated deficiency of vitamin E retinitis pigmentosa muscular atrophy nervous system disorder speech disorder atherosclerosis Vitamin E Deficiency hearing disorder hyperreflexia retinal disease vision disorder lung cancer arteriosclerosis disorder cone-rod dystrophy pancreatic ductal adenocarcinoma Charcot-Marie-Tooth disease intellectual disability malignant colon neoplasm

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.