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. Author manuscript; available in PMC: 2021 May 28.
Published in final edited form as: Crit Rev Biochem Mol Biol. 2020 May 28;55(2):197–218. doi: 10.1080/10409238.2020.1768207

Table 1.

Retinoid-binding proteins found in mammals.a,b

Original nomenclature Genetic nomenclature Ligands Tissue distribution
Retinol-binding protein (RBP) RBP4 Retinol Serum/plasma
Cellular retinol-binding protein I (CRBPI) RBP1 Retinol and retinaldehyde Most tissues
Cellular retinol-binding protein II (CRBPII) RBP2 Retinol and retinaldehyde Small intestine
Cellular retinol-binding protein IV (CRBPIV) RBP5 Retinol and retinaldehyde Liver, kidney, spleen
Cellular retinol-binding protein III (CRBPIII) RBP7 Retinol& retinaldehyde Adipose and muscle
Interphotoreceptor retinol-binding protein (IRBP) RBP3 Retinol and retinaldehyde and other lipids Eye, retina retinal pigmented epithelium (RPE)
Cellular retinaldehyde-Binding protein (CRALBP) RLBP1 11-cis-retinol and 11-cis-retinaldehyde Retina, RPE
Cellular retinoic acid-binding protein I (CRABPI) CRABP1 Retinoic acid Many tissues
Cellular retinoic acid-binding protein II (CRABPII) CRABP2 Retinoic acid Skin, adipose, others
Fatty acid-binding protein 5 (FABP5) FABP5 Fatty acids and retinoic acid Adipose, liver, others
a

A listing of retinoid-binding proteins that are canonically accepted to be importantly involved in facilitating retinoid metabolism and/or actions.

b

RBP1, RBP2, RBP5, RBP7, CRABP1, CRABP2, and FABP5 are all fatty acid-binding proteins. These along with RBP4 are member of the lipocalin superfamily.