Wilson disease protein

ATPase, Cu++ transporting, beta polypeptide

PDB rendering based on 2arf.
Identifiers
Symbols ATP7B; PWD; WC1; WD; WND
External IDs OMIM: 606882 MGI: 103297 HomoloGene: 20063 GeneCards: ATP7B Gene
EC number 3.6.3.4
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 540 11979
Ensembl ENSG00000123191 ENSMUSG00000006567
UniProt P35670 Q64446
RefSeq (mRNA) NM_000053.2 NM_007511.2
RefSeq (protein) NP_000044.2 NP_031537.2
Location (UCSC) Chr 13:
52.51 – 52.59 Mb		 Chr 8:
23.1 – 23.17 Mb
PubMed search [1] [2]

Wilson disease protein (also called ATP7B, full name ATPase, Cu++ transporting, beta polypeptide) is an ATPase that transports copper.

This gene is a member of the P-type cation transport ATPase family and encodes a protein with several membrane-spanning domains, an ATPase consensus sequence, a hinge domain, a phosphorylation site, and at least two putative copper-binding sites. This protein functions as a monomer, exporting copper out of the cells, such as the efflux of hepatic copper into the bile. Alternate transcriptional splice variants, encoding different isoforms with distinct cellular localizations, have been characterized. Mutations in this gene have been associated with Wilson's disease.[1]

Contents

Interactions

Wilson disease protein has been shown to interact with ATOX1[2][3] and GLRX.[4]

See also

External links

References

  1. ^ "Entrez Gene: ATP7B ATPase, Cu++ transporting, beta polypeptide". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=540. 
  2. ^ Larin, D; Mekios C, Das K, Ross B, Yang A S, Gilliam T C (Oct. 1999). "Characterization of the interaction between the Wilson and Menkes disease proteins and the cytoplasmic copper chaperone, HAH1p". J. Biol. Chem. (UNITED STATES) 274 (40): 28497–504. doi:10.1074/jbc.274.40.28497. ISSN 0021-9258. PMID 10497213. 
  3. ^ Hamza, I; Schaefer M, Klomp L W, Gitlin J D (Nov. 1999). "Interaction of the copper chaperone HAH1 with the Wilson disease protein is essential for copper homeostasis". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 96 (23): 13363–8. doi:10.1073/pnas.96.23.13363. ISSN 0027-8424. PMC 23953. PMID 10557326. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=23953. 
  4. ^ Lim, Chris M; Cater Michael A, Mercer Julian F B, La Fontaine Sharon (Sep. 2006). "Copper-dependent interaction of glutaredoxin with the N termini of the copper-ATPases (ATP7A and ATP7B) defective in Menkes and Wilson diseases". Bioche Biophys. Res. Commun. (United States) 348 (2): 428–36. doi:10.1016/j.bbrc.2006.07.067. ISSN 0006-291X. PMID 16884690. 

Further reading

3.6.1
3.6.2
3.6.3-4: ATPase
3.6.3
Cu++ (3.6.3.4)
Menkes/ATP7A · Wilson/ATP7B
Ca+ (3.6.3.8)
Na+/K+ (3.6.3.9)
ATP1A1 · ATP1A2 · ATP1A3 · ATP1A4 · ATP1B1 · ATP1B2 · ATP1B3 · ATP1B4
H+/K+ (3.6.3.10)
ATP4A
ATP8B1 · ATP10A · ATP11B · ATP12A · ATP13A2 · ATP13A3 ·
3.6.4
3.6.5: GTPase

Rho family of GTPases: Cdc42 (CDC42, TC10, TCL) • RhoUV (RhoU, RhoV) • Rac (Rac1, 2, 3, RhoG) • RhoBTB (1, 2) • RhoH • Rho (A, B, C) • Rnd (1, 2, 3) • RhoDF (RhoF, RhoD)

other: Ras (HRAS, KRAS, NRAS) · Rab (RAB23, RAB27) · Arf (ARF6, SAR1B, ARL13B, ARL6) · Ran · Rheb · Rap
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
F- and V-type ATPase (3.A.2)
H+ transporting, mitochondrial: ATP5A1, ATP5B, ATP5C1, ATP5C2, ATP5D, ATP5E, ATP5F1, ATP5G1, ATP5G2, ATP5G3, ATP5H, ATP5I, ATP5J, ATP5J2, ATP5L, ATP5L2, ATP5O, ATP5S
P-type ATPase (3.A.3)
  • 3.A.3.1.4: H+/K+ transporting, nongastric: ATP12A
  • 3.A.3.5: Cu++ transporting: ATP7A, ATP7B

Other/ungrouped:

Na+/K+ - H+
see also ATPase disorders
B memb: cead, trns (1A, 1C, 1F, 2A, 3A1, 3A2-3, 3D), othr
Transition metal
Other
ATP7A · ATP7B · Ceruloplasmin · SLC31A1 · ATOX1
TMC6 · TMC8 · SLC30A1 · SLC39A4
Electrolyte

M: NUT

cof, enz, met

noco, nuvi, sysi/epon, met

drug(A8/11/12)