2CBR

CELLULAR RETINOIC ACID BINDING PROTEIN I IN COMPLEX WITH A RETINOBENZOIC ACID (AM80)

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2cbra_	All beta proteins	Lipocalins	Lipocalins	Fatty acid binding protein-like	Cellular retinoic-acid-binding protein (CRABP)	cattle (Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Fatty acid binding protein-like	8030286	4002547	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Lipocalins	8042665	3001332	SCOP2 (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	Lipocalin_7	e2cbrA1	A: beta barrels	X: Lipocalins/Streptavidin	H: Lipocalins (From Topology)	T: Lipocalins	F: Lipocalin_7	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.40.128.20	Mainly Beta	Beta Barrel	Lipocalin	Calycin beta-barrel core domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00061	Lipocalin / cytosolic fatty-acid binding protein family (Lipocalin)	Lipocalin / cytosolic fatty-acid binding protein family	Lipocalins are transporters for small hydrophobic molecules, such as lipids, steroid hormones, bilins, and retinoids. The family also encompasses the enzyme prostaglandin D synthase (EC:5.3.99.2). Alignment subsumes both the lipocalin and fatty acid ...	Lipocalins are transporters for small hydrophobic molecules, such as lipids, steroid hormones, bilins, and retinoids. The family also encompasses the enzyme prostaglandin D synthase (EC:5.3.99.2). Alignment subsumes both the lipocalin and fatty acid binding protein signatures from PROSITE. This is supported on structural and functional grounds. The structure is an eight-stranded beta barrel.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	PROTEIN (CRABP-I)	vitamin binding binding retinal binding isoprenoid binding retinoid binding lipid binding small molecule binding fatty acid binding organic acid binding ion binding anion binding carboxylic acid binding monocarboxylic acid binding alcohol binding vitamin binding binding retinal binding isoprenoid binding retinoid binding lipid binding small molecule binding fatty acid binding organic acid binding ion binding anion binding carboxylic acid binding monocarboxylic acid binding alcohol binding retinol binding retinoic acid binding identical protein binding protein binding	organic anion transport carboxylic acid transport transport lipid localization lipid transport establishment of localization organic acid transport localization monocarboxylic acid transport fatty acid transport macromolecule localization	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol protein-containing complex membrane-bounded organelle intracellular organelle organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR000463	Cytosolic fatty-acid binding	Domain
A	IPR012674	Calycin	Homologous Superfamily
A	IPR031259	Intracellular lipid binding protein	Family
A	IPR000566	Lipocalin/cytosolic fatty-acid binding domain	Domain

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.