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SB0135 : Retinoid X receptor [alpha]

[ CaMP Format ]

* Basic Information

OrganismHomo sapiens (human)
Protein Namesretinoic acid receptor RXR-alpha isoform a [Homo sapiens]; retinoic acid receptor RXR-alpha isoform a; retinoic acid receptor RXR-alpha; retinoid X nuclear receptor alpha; nuclear receptor subfamily 2 group B member 1; Retinoic acid receptor RXR-alpha; Nuclear receptor subfamily 2 group B member 1; Retinoid X receptor alpha
Gene NamesRXRA; NR2B1; retinoid X receptor, alpha
Gene Locus9q34.3; chromosome 9
GO FunctionNot available
Entrez Protein Entrez Nucleotide Entrez Gene UniProt OMIM HGNC HPRD KEGG
NP_002948 NM_002957 6256 P19793 180245 HGNC:10477 01577 hsa:6256

* Information From OMIM

Function: Zhou et al. (1995) used an in vitro model system of cardiac muscle cell hypertrophy to identify a retinoic acid-mediated pathway that suppresses the acquisition of specific features of the hypertrophic phenotype after exposure to the alpha-adrenergic receptor agonist phenylephrine. They found that retinoic acid at physiologic concentrations suppressed the increase in cell size and induction of a genetic marker for hypertrophy, namely the atrial natriuretic factor gene (ANF; OMIM:108780). Retinoic acid also suppressed endothelin-1 (EDN1; OMIM:131240) pathways for cardiac muscle cell hypertrophy. These and results of further studies suggested the possibility that a pathway for suppression of hypertrophy may exist in vivo, which may have potential therapeutic value.

* Structure Information

1. Primary Information

Length: 462 aa

Average Mass: 50.811 kDa

Monoisotopic Mass: 50.778 kDa

2. Domain Information

Annotated Domains: interpro / pfam / smart / prosite

Computationally Assigned Domains (Pfam+HMMER):

domain namebeginendscoree-value
Nuclear/hormone receptor activator site AF-1 1. 171271.021.5
--- cleavage 90 (inside Nuclear/hormone receptor activator site AF-1 17..127) ---
--- cleavage 118 (inside Nuclear/hormone receptor activator site AF-1 17..127) ---
Zinc finger, C4 type (two domains) 1. 1342022.016.3
Ligand-binding domain of nuclear hormone receptor 1. 26544013.00.0

3. Sequence Information

Fasta Sequence: SB0135.fasta

Amino Acid Sequence and Secondary Structures (PsiPred):

4. 3D Information

Known Structures in PDB: 1BY4 (X-ray; 210 A; A/B/C/D=129-209), 1DSZ (X-ray; 170 A; B=129-212), 1FBY (X-ray; 225 A; A/B=224-462), 1FM6 (X-ray; 210 A; A/U=225-462), 1FM9 (X-ray; 210 A; A=225-462), 1G1U (X-ray; 250 A; A/B/C/D=225-462), 1G5Y (X-ray; 200 A; A/B/C/D=225-462), 1K74 (X-ray; 230 A; A=225-462), 1LBD (X-ray; 270 A; A=201-460), 1MV9 (X-ray; 190 A; A=223-462), 1MVC (X-ray; 190 A; A=223-462), 1MZN (X-ray; 190 A; A/C/E/G=223-462), 1R0N (X-ray; 260 A; A=130-206), 1RDT (X-ray; 240 A; A=225-462), 1RXR (NMR; -; A=130-212), 1XLS (X-ray; 296 A; A/B/C/D=227-458), 1XV9 (X-ray; 270 A; A/C=227-462), 1XVP (X-ray; 260 A; A/C=227-462), 1YNW (X-ray; 300 A; B=130-228), 2ACL (X-ray; 280 A; A/C/E/G=225-462), 2NLL (X-ray; 190 A; A=135-200), 2P1T (X-ray; 180 A; A=223-462), 2P1U (X-ray; 220 A; A=223-462), 2P1V (X-ray; 220 A; A=223-462), 2ZXZ (X-ray; 300 A; A=223-462), 2ZY0 (X-ray; 290 A; A/C=223-462), 3DZU (X-ray; 320 A; A=11-462), 3DZY (X-ray; 310 A; A=11-462), 3E00 (X-ray; 310 A; A=11-462), 3E94 (X-ray; 190 A; A=223-462), 3FAL (X-ray; 236 A; A/C=225-462), 3FC6 (X-ray; 206 A; A/C=225-462), 3FUG (X-ray; 200 A; A=223-462), 3H0A (X-ray; 210 A; A=228-455), 3KWY (X-ray; 230 A; A=223-462), 3NSP (X-ray; 290 A; A/B=223-462), 3NSQ (X-ray; 260 A; A/B=223-462), 3OAP (X-ray; 205 A; A=228-458), 3OZJ (X-ray; 210 A; A/C=225-462), 3PCU (X-ray; 200 A; A=229-458), 3R29 (X-ray; 290 A; A/B=223-462), 3R2A (X-ray; 300 A; A/B/C/D=223-462), 3R5M (X-ray; 280 A; A/C=223-462), 3UVV (X-ray; 295 A; B=225-462), 4CN2 (X-ray; 207 A; C/D=130-212), 4CN3 (X-ray; 235 A; A/B/C=130-212, D=130-173, D=175-212), 4CN5 (X-ray; 200 A; A/B=130-212), 4CN7 (X-ray; 234 A; A/B/E/F=130-212), 4J5W (X-ray; 280 A; C/D=227-462), 4J5X (X-ray; 280 A; C/D=227-462), 4K4J (X-ray; 200 A; A=228-458), 4K6I (X-ray; 210 A; A=228-458), 4M8E (X-ray; 240 A; A=228-458), 4M8H (X-ray; 220 A; A=228-458), 4N5G (X-ray; 211 A; A/B/C/D=223-462), 4N8R (X-ray; 203 A; A/B/C/D=223-462), 4NQA (X-ray; 310 A; A/H=98-462), 4OC7 (X-ray; 250 A; A=223-462), 4POH (X-ray; 230 A; A=228-458), 4POJ (X-ray; 200 A; A=228-458), 4PP3 (X-ray; 200 A; A=228-458), 4PP5 (X-ray; 200 A; A=228-458)

* Cleavage Information

2 [sites] cleaved by Calpain 2

Source Reference: [PubMed ID: 23389291] Gao W, Liu J, Hu M, Huang M, Cai S, Zeng Z, Lin B, Cao X, Chen J, Zeng JZ, Zhou H, Zhang XK, Regulation of proteolytic cleavage of retinoid X receptor-alpha by GSK-3beta. Carcinogenesis. 2013 Jun;34(6):1208-15. doi: 10.1093/carcin/bgt043. Epub 2013 Feb

Cleavage sites (±10aa)


Gly90 Ser

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'

Sequence conservation (by blast)


Lys118 Val

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'

Sequence conservation (by blast)

* References

[PubMed ID: 24513686] Zhang J, Ma X, Wang H, Ma D, Huang G, Elevated methylation of the RXRA promoter region may be responsible for its downregulated expression in the myocardium of patients with TOF. Pediatr Res. 2014 May;75(5):588-94. doi: 10.1038/pr.2014.17. Epub 2014 Feb 10.

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