CRABP2

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Cellular retinoic acid binding protein 2
Protein CRABP2 PDB 1blr.png
PDB rendering based on 1blr.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols CRABP2 ; CRABP-II; RBP6
External IDs OMIM180231 MGI88491 HomoloGene1415 ChEMBL: 2692 GeneCards: CRABP2 Gene
RNA expression pattern
PBB GE CRABP2 202575 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 1382 12904
Ensembl ENSG00000143320 ENSMUSG00000004885
UniProt P29373 P22935
RefSeq (mRNA) NM_001199723 NM_007759
RefSeq (protein) NP_001186652 NP_031785
Location (UCSC) Chr 1:
156.67 – 156.68 Mb
Chr 3:
87.95 – 87.95 Mb
PubMed search [1] [2]

Cellular retinoic acid-binding protein 2 is a protein that in humans is encoded by the CRABP2 gene.[1][2]

A number of specific carrier proteins for members of the vitamin A family have been discovered. Cellular retinoic acid binding proteins (CRABP) are low molecular weight proteins whose precise function remains unknown. The inducibility of the CRABP2 gene suggests that this isoform is important in retinoic acid-mediated regulation of human skin growth and differentiation. It has been postulated that the CRABP2 gene is transcriptionally regulated by a newly synthesized regulatory protein.[2]

Interactions[edit]

CRABP2 has been shown to interact with Cyclin D3.[3]

References[edit]

  1. ^ Astrom A, Tavakkol A, Pettersson U, Cromie M, Elder JT, Voorhees JJ (Oct 1991). "Molecular cloning of two human cellular retinoic acid-binding proteins (CRABP). Retinoic acid-induced expression of CRABP-II but not CRABP-I in adult human skin in vivo and in skin fibroblasts in vitro". J Biol Chem 266 (26): 17662–6. PMID 1654334. 
  2. ^ a b "Entrez Gene: CRABP2 cellular retinoic acid binding protein 2". 
  3. ^ Despouy, Gilles; Bastie Jean-Nöel, Deshaies Sylvie, Balitrand Nicole, Mazharian Alexandra, Rochette-Egly Cécile, Chomienne Christine, Delva Laurent (Feb 2003). "Cyclin D3 is a cofactor of retinoic acid receptors, modulating their activity in the presence of cellular retinoic acid-binding protein II". J. Biol. Chem. (United States) 278 (8): 6355–62. doi:10.1074/jbc.M210697200. ISSN 0021-9258. PMID 12482873. 

Further reading[edit]

  • Eller MS, Oleksiak MF, McQuaid TJ, et al. (1992). "The molecular cloning and expression of two CRABP cDNAs from human skin". Exp. Cell Res. 198 (2): 328–36. doi:10.1016/0014-4827(92)90387-N. PMID 1309505. 
  • Elder JT, Aström A, Pettersson U, et al. (1992). "Assignment of the human CRABP-II gene to chromosome 1q21 by nonisotopic in situ hybridization". Hum. Genet. 89 (5): 487–90. doi:10.1007/BF00219171. PMID 1321791. 
  • Aström A, Pettersson U, Voorhees JJ (1993). "Structure of the human cellular retinoic acid-binding protein II gene. Early transcriptional regulation by retinoic acid". J. Biol. Chem. 267 (35): 25251–5. PMID 1334086. 
  • Thompson JR, Bratt JM, Banaszak LJ (1995). "Crystal structure of cellular retinoic acid binding protein I shows increased access to the binding cavity due to formation of an intermolecular beta-sheet". J. Mol. Biol. 252 (4): 433–46. doi:10.1006/jmbi.1995.0509. PMID 7563063. 
  • Kleywegt GJ, Bergfors T, Senn H, et al. (1995). "Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid". Structure 2 (12): 1241–58. doi:10.1016/S0969-2126(94)00125-1. PMID 7704533. 
  • Stephanou A, Sarlis NJ, Richards R, Handwerger S (1994). "Expression of retinoic acid receptor subtypes and cellular retinoic acid binding protein-II mRNAs during differentiation of human trophoblast cells". Biochem. Biophys. Res. Commun. 202 (2): 772–80. doi:10.1006/bbrc.1994.1997. PMID 8048948. 
  • Sanquer S, Eller MS, Gilchrest BA (1993). "Retinoids and state of differentiation modulate CRABP II gene expression in a skin equivalent". J. Invest. Dermatol. 100 (2): 148–53. doi:10.1111/1523-1747.ep12462785. PMID 8381448. 
  • Wang L, Li Y, Yan H (1997). "Structure-function relationships of cellular retinoic acid-binding proteins. Quantitative analysis of the ligand binding properties of the wild-type proteins and site-directed mutants". J. Biol. Chem. 272 (3): 1541–7. doi:10.1074/jbc.272.3.1541. PMID 8999826. 
  • Flagiello D, Apiou F, Gibaud A, et al. (1997). "Assignment of the genes for cellular retinoic acid binding protein 1 (CRABP1) and 2 (CRABP2) to human chromosome band 15q24 and 1q21.3, respectively, by in situ hybridization". Cytogenet. Cell Genet. 76 (1–2): 17–8. doi:10.1159/000134502. PMID 9154115. 
  • Brar AK, Kessler CA, Meyer AJ, et al. (1997). "Retinoic acid suppresses in-vitro decidualization of human endometrial stromal cells". Mol. Hum. Reprod. 2 (3): 185–93. doi:10.1093/molehr/2.3.185. PMID 9238678. 
  • Chen X, Tordova M, Gilliland GL, et al. (1998). "Crystal structure of apo-cellular retinoic acid-binding protein type II (R111M) suggests a mechanism of ligand entry". J. Mol. Biol. 278 (3): 641–53. doi:10.1006/jmbi.1998.1734. PMID 9600845. 
  • Wang L, Li Y, Abildgaard F, et al. (1998). "NMR solution structure of type II human cellular retinoic acid binding protein: implications for ligand binding". Biochemistry 37 (37): 12727–36. doi:10.1021/bi9808924. PMID 9737849. 
  • Wang L, Yan H (1998). "NMR study suggests a major role for Arg111 in maintaining the structure and dynamical properties of type II human cellular retinoic acid binding protein". Biochemistry 37 (37): 13021–32. doi:10.1021/bi981021x. PMID 9737883. 
  • Chaudhuri BN, Kleywegt GJ, Broutin-L'Hermite I, et al. (2000). "Structures of cellular retinoic acid binding proteins I and II in complex with synthetic retinoids". Acta Crystallogr. D Biol. Crystallogr. 55 (Pt 11): 1850–7. doi:10.1107/S0907444999011026. PMID 10531482. 
  • Budhu AS, Noy N (2002). "Direct Channeling of Retinoic Acid between Cellular Retinoic Acid-Binding Protein II and Retinoic Acid Receptor Sensitizes Mammary Carcinoma Cells to Retinoic Acid-Induced Growth Arrest". Mol. Cell. Biol. 22 (8): 2632–41. doi:10.1128/MCB.22.8.2632-2641.2002. PMC 133717. PMID 11909957. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. 
  • Despouy G, Bastie JN, Deshaies S, et al. (2003). "Cyclin D3 is a cofactor of retinoic acid receptors, modulating their activity in the presence of cellular retinoic acid-binding protein II". J. Biol. Chem. 278 (8): 6355–62. doi:10.1074/jbc.M210697200. PMID 12482873. 
  • Behrens GM, Genschel J, Schmidt RE, Schmidt HH (2004). "Lack of mutations in LMNA, its promoter region, and the cellular retinoic acid binding protein II (CRABP II) in HIV associated lipodystrophy". Eur. J. Med. Res. 8 (5): 221–5. PMID 12844477. 
  • Van den Bogaerdt AJ, El Ghalbzouri A, Hensbergen PJ, et al. (2004). "Differential expression of CRABP-II in fibroblasts derived from dermis and subcutaneous fat". Biochem. Biophys. Res. Commun. 315 (2): 428–33. doi:10.1016/j.bbrc.2004.01.069. PMID 14766225.