ATP2C1: Difference between revisions

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{{Infobox_gene}}
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'''Calcium-transporting ATPase type 2C member 1''' is an [[enzyme]] that in humans is encoded by the ''ATP2C1'' [[gene]].<ref name="pmid10615129">{{cite journal | vauthors = Hu Z, Bonifas JM, Beech J, Bench G, Shigihara T, Ogawa H, Ikeda S, Mauro T, ((Epstein EH Jr)) | title = Mutations in ATP2C1, encoding a calcium pump, cause Hailey-Hailey disease | journal = Nat Genet | volume = 24 | issue = 1 | pages = 61–5 |date=Feb 2000 | pmid = 10615129 | pmc =  | doi = 10.1038/71701 }}</ref><ref name="pmid10767338">{{cite journal | vauthors = Sudbrak R, Brown J, Dobson-Stone C, Carter S, Ramser J, White J, Healy E, Dissanayake M, Larregue M, Perrussel M, Lehrach H, Munro CS, Strachan T, Burge S, Hovnanian A, Monaco AP | title = Hailey-Hailey disease is caused by mutations in ATP2C1 encoding a novel Ca(2+) pump | journal = Hum Mol Genet | volume = 9 | issue = 7 | pages = 1131–40 |date=Jun 2000 | pmid = 10767338 | pmc =  | doi =10.1093/hmg/9.7.1131 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ATP2C1 ATPase, Ca++ transporting, type 2C, member 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27032| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source = 
| PDB =
| Name = ATPase, Ca++ transporting, type 2C, member 1
| HGNCid = 13211
| Symbol = ATP2C1
| AltSymbols =; ATP2C1A; BCPM; HHD; KIAA1347; PMR1; SPCA1; hSPCA1
| OMIM = 604384
| ECnumber =
| Homologene = 56672
| MGIid = 1889008
| GeneAtlas_image1 = PBB_GE_ATP2C1_209934_s_at_tn.png
  | GeneAtlas_image2 = PBB_GE_ATP2C1_209935_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005388 |text = calcium-transporting ATPase activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0016820 |text = hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances}}
| Component = {{GNF_GO|id=GO:0000139 |text = Golgi membrane}} {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}} {{GNF_GO|id=GO:0005802 |text = trans-Golgi network}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
  | Process = {{GNF_GO|id=GO:0006812 |text = cation transport}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0008544 |text = epidermis development}} {{GNF_GO|id=GO:0016339 |text = calcium-dependent cell-cell adhesion}} {{GNF_GO|id=GO:0031532 |text = actin cytoskeleton reorganization}} {{GNF_GO|id=GO:0032468 |text = Golgi calcium ion homeostasis}} {{GNF_GO|id=GO:0032472 |text = Golgi calcium ion transport}} {{GNF_GO|id=GO:0043123 |text = positive regulation of I-kappaB kinase/NF-kappaB cascade}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 27032
    | Hs_Ensembl = ENSG00000017260
    | Hs_RefseqProtein = NP_001001485
    | Hs_RefseqmRNA = NM_001001485
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 3
    | Hs_GenLoc_start = 132095712
    | Hs_GenLoc_end = 132218243
    | Hs_Uniprot = P98194
    | Mm_EntrezGene = 235574
    | Mm_Ensembl = ENSMUSG00000032570
    | Mm_RefseqmRNA = XM_981296
    | Mm_RefseqProtein = XP_986390
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 105269458
    | Mm_GenLoc_end = 105379247
    | Mm_Uniprot = Q3UWW0
  }}
}}
'''ATPase, Ca++ transporting, type 2C, member 1''', also known as '''ATP2C1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ATP2C1 ATPase, Ca++ transporting, type 2C, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27032| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = The protein encoded by this gene belongs to the family of P-type cation transport ATPases. This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of the calcium. Defects in this gene cause Hailey-Hailey disease, an autosomal dominant disorder. Alternatively spliced transcript variants encoding different isoforms have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: ATP2C1 ATPase, Ca++ transporting, type 2C, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27032| accessdate = }}</ref>
| summary_text = This gene encodes one of the [[Secretory Pathway Ca²⁺ ATPase|SPCA]] proteins, a Ca<sup>2+</sup> ion-transporting P-type ATPase. This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of the calcium. Defects in this gene cause [[Hailey-Hailey disease]], an autosomal dominant disorder. Alternatively spliced transcript variants encoding different isoforms have been identified.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|ATP2C1}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Missiaen L, Raeymaekers L, Dode L, ''et al.'' |title=SPCA1 pumps and Hailey-Hailey disease. |journal=Biochem. Biophys. Res. Commun. |volume=322 |issue= 4 |pages= 1204-13 |year= 2004 |pmid= 15336968 |doi= 10.1016/j.bbrc.2004.07.128 }}
*{{cite journal  | vauthors=Missiaen L, Raeymaekers L, Dode L |title=SPCA1 pumps and Hailey-Hailey disease. |journal=Biochem. Biophys. Res. Commun. |volume=322 |issue= 4 |pages= 1204–13 |year= 2004 |pmid= 15336968 |doi= 10.1016/j.bbrc.2004.07.128 |display-authors=etal}}
*{{cite journal  | author=Ikeda S, Welsh EA, Peluso AM, ''et al.'' |title=Localization of the gene whose mutations underlie Hailey-Hailey disease to chromosome 3q. |journal=Hum. Mol. Genet. |volume=3 |issue= 7 |pages= 1147-50 |year= 1995 |pmid= 7981684 |doi=  }}
*{{cite journal  | vauthors=Ikeda S, Welsh EA, Peluso AM |title=Localization of the gene whose mutations underlie Hailey-Hailey disease to chromosome 3q. |journal=Hum. Mol. Genet. |volume=3 |issue= 7 |pages= 1147–50 |year= 1995 |pmid= 7981684 |doi=10.1093/hmg/3.7.1147 |display-authors=etal}}
*{{cite journal  | author=Hu Z, Bonifas JM, Beech J, ''et al.'' |title=Mutations in ATP2C1, encoding a calcium pump, cause Hailey-Hailey disease. |journal=Nat. Genet. |volume=24 |issue= 1 |pages= 61-5 |year= 2000 |pmid= 10615129 |doi= 10.1038/71701 }}
*{{cite journal  | vauthors=Nagase T, Kikuno R, Ishikawa KI |title=Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=7 |issue= 1 |pages= 65–73 |year= 2000 |pmid= 10718198 |doi=10.1093/dnares/7.1.65  |display-authors=etal}}
*{{cite journal  | author=Nagase T, Kikuno R, Ishikawa KI, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=7 |issue= 1 |pages= 65-73 |year= 2000 |pmid= 10718198 |doi= }}
*{{cite journal  | vauthors=Stanchi F, Bertocco E, Toppo S |title=Characterization of 16 novel human genes showing high similarity to yeast sequences. |journal=Yeast |volume=18 |issue= 1 |pages= 69–80 |year= 2001 |pmid= 11124703 |doi= 10.1002/1097-0061(200101)18:1<69::AID-YEA647>3.0.CO;2-H |display-authors=etal}}
*{{cite journal  | author=Sudbrak R, Brown J, Dobson-Stone C, ''et al.'' |title=Hailey-Hailey disease is caused by mutations in ATP2C1 encoding a novel Ca(2+) pump. |journal=Hum. Mol. Genet. |volume=9 |issue= 7 |pages= 1131-40 |year= 2000 |pmid= 10767338 |doi= }}
*{{cite journal  | vauthors=Ton VK, Mandal D, Vahadji C, Rao R |title=Functional expression in yeast of the human secretory pathway Ca(2+), Mn(2+)-ATPase defective in Hailey-Hailey disease. |journal=J. Biol. Chem. |volume=277 |issue= 8 |pages= 6422–7 |year= 2002 |pmid= 11741891 |doi= 10.1074/jbc.M110612200 }}
*{{cite journal  | author=Stanchi F, Bertocco E, Toppo S, ''et al.'' |title=Characterization of 16 novel human genes showing high similarity to yeast sequences. |journal=Yeast |volume=18 |issue= 1 |pages= 69-80 |year= 2001 |pmid= 11124703 |doi= 10.1002/1097-0061(200101)18:1<69::AID-YEA647>3.0.CO;2-H }}
*{{cite journal  | vauthors=Dobson-Stone C, Fairclough R, Dunne E |title=Hailey-Hailey disease: molecular and clinical characterization of novel mutations in the ATP2C1 gene. |journal=J. Invest. Dermatol. |volume=118 |issue= 2 |pages= 338–43 |year= 2002 |pmid= 11841554 |doi= 10.1046/j.0022-202x.2001.01675.x |display-authors=etal}}
*{{cite journal  | author=Ton VK, Mandal D, Vahadji C, Rao R |title=Functional expression in yeast of the human secretory pathway Ca(2+), Mn(2+)-ATPase defective in Hailey-Hailey disease. |journal=J. Biol. Chem. |volume=277 |issue= 8 |pages= 6422-7 |year= 2002 |pmid= 11741891 |doi= 10.1074/jbc.M110612200 }}
*{{cite journal  | vauthors=Yokota K, Yasukawa K, Shimizu H |title=Analysis of ATP2C1 gene mutation in 10 unrelated Japanese families with Hailey-Hailey disease. |journal=J. Invest. Dermatol. |volume=118 |issue= 3 |pages= 550–1 |year= 2002 |pmid= 11874499 |doi= 10.1046/j.0022-202x.2001.01686.x }}
*{{cite journal  | author=Dobson-Stone C, Fairclough R, Dunne E, ''et al.'' |title=Hailey-Hailey disease: molecular and clinical characterization of novel mutations in the ATP2C1 gene. |journal=J. Invest. Dermatol. |volume=118 |issue= 2 |pages= 338-43 |year= 2002 |pmid= 11841554 |doi= 10.1046/j.0022-202x.2001.01675.x }}
*{{cite journal  | vauthors=Chao SC, Tsai YM, Yang MH |title=Mutation analysis of ATP2C1 gene in Taiwanese patients with Hailey-Hailey disease. |journal=Br. J. Dermatol. |volume=146 |issue= 4 |pages= 595–600 |year= 2002 |pmid= 11966689 |doi=10.1046/j.1365-2133.2002.04697.x }}
*{{cite journal  | author=Yokota K, Yasukawa K, Shimizu H |title=Analysis of ATP2C1 gene mutation in 10 unrelated Japanese families with Hailey-Hailey disease. |journal=J. Invest. Dermatol. |volume=118 |issue= 3 |pages= 550-1 |year= 2002 |pmid= 11874499 |doi= 10.1046/j.0022-202x.2001.01686.x }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |display-authors=etal}}
*{{cite journal  | author=Chao SC, Tsai YM, Yang MH |title=Mutation analysis of ATP2C1 gene in Taiwanese patients with Hailey-Hailey disease. |journal=Br. J. Dermatol. |volume=146 |issue= 4 |pages= 595-600 |year= 2002 |pmid= 11966689 |doi= }}
*{{cite journal  | vauthors=Fairclough RJ, Dode L, Vanoevelen J |title=Effect of Hailey-Hailey Disease mutations on the function of a new variant of human secretory pathway Ca2+/Mn2+-ATPase (hSPCA1). |journal=J. Biol. Chem. |volume=278 |issue= 27 |pages= 24721–30 |year= 2003 |pmid= 12707275 |doi= 10.1074/jbc.M300509200 |display-authors=etal}}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | vauthors=Matsuda A, Suzuki Y, Honda G |title=Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. |journal=Oncogene |volume=22 |issue= 21 |pages= 3307–18 |year= 2003 |pmid= 12761501 |doi= 10.1038/sj.onc.1206406 |display-authors=etal}}
*{{cite journal  | author=Fairclough RJ, Dode L, Vanoevelen J, ''et al.'' |title=Effect of Hailey-Hailey Disease mutations on the function of a new variant of human secretory pathway Ca2+/Mn2+-ATPase (hSPCA1). |journal=J. Biol. Chem. |volume=278 |issue= 27 |pages= 24721-30 |year= 2003 |pmid= 12707275 |doi= 10.1074/jbc.M300509200 }}
*{{cite journal  | vauthors=Van Baelen K, Vanoevelen J, Callewaert G |title=The contribution of the SPCA1 Ca2+ pump to the Ca2+ accumulation in the Golgi apparatus of HeLa cells assessed via RNA-mediated interference. |journal=Biochem. Biophys. Res. Commun. |volume=306 |issue= 2 |pages= 430–6 |year= 2003 |pmid= 12804581 |doi=10.1016/S0006-291X(03)00977-X  |display-authors=etal}}
*{{cite journal  | author=Matsuda A, Suzuki Y, Honda G, ''et al.'' |title=Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. |journal=Oncogene |volume=22 |issue= 21 |pages= 3307-18 |year= 2003 |pmid= 12761501 |doi= 10.1038/sj.onc.1206406 }}
*{{cite journal  | vauthors=Callewaert G, Parys JB, De Smedt H |title=Similar Ca(2+)-signaling properties in keratinocytes and in COS-1 cells overexpressing the secretory-pathway Ca(2+)-ATPase SPCA1. |journal=Cell Calcium |volume=34 |issue= 2 |pages= 157–62 |year= 2004 |pmid= 12810057 |doi=10.1016/S0143-4160(03)00070-8  |display-authors=etal}}
*{{cite journal  | author=Van Baelen K, Vanoevelen J, Callewaert G, ''et al.'' |title=The contribution of the SPCA1 Ca2+ pump to the Ca2+ accumulation in the Golgi apparatus of HeLa cells assessed via RNA-mediated interference. |journal=Biochem. Biophys. Res. Commun. |volume=306 |issue= 2 |pages= 430-6 |year= 2003 |pmid= 12804581 |doi= }}
*{{cite journal  | vauthors=Aronchik I, Behne MJ, Leypoldt L |title=Actin reorganization is abnormal and cellular ATP is decreased in Hailey-Hailey keratinocytes. |journal=J. Invest. Dermatol. |volume=121 |issue= 4 |pages= 681–7 |year= 2003 |pmid= 14632182 |doi= 10.1046/j.1523-1747.2003.12472.x |display-authors=etal}}
*{{cite journal  | author=Callewaert G, Parys JB, De Smedt H, ''et al.'' |title=Similar Ca(2+)-signaling properties in keratinocytes and in COS-1 cells overexpressing the secretory-pathway Ca(2+)-ATPase SPCA1. |journal=Cell Calcium |volume=34 |issue= 2 |pages= 157-62 |year= 2004 |pmid= 12810057 |doi= }}
*{{cite journal  | vauthors=Behne MJ, Tu CL, Aronchik I |title=Human keratinocyte ATP2C1 localizes to the Golgi and controls Golgi Ca2+ stores. |journal=J. Invest. Dermatol. |volume=121 |issue= 4 |pages= 688–94 |year= 2003 |pmid= 14632183 |doi= 10.1046/j.1523-1747.2003.12528.x |display-authors=etal}}
*{{cite journal  | author=Aronchik I, Behne MJ, Leypoldt L, ''et al.'' |title=Actin reorganization is abnormal and cellular ATP is decreased in Hailey-Hailey keratinocytes. |journal=J. Invest. Dermatol. |volume=121 |issue= 4 |pages= 681-7 |year= 2003 |pmid= 14632182 |doi= 10.1046/j.1523-1747.2003.12472.x }}
*{{cite journal  | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
*{{cite journal  | author=Behne MJ, Tu CL, Aronchik I, ''et al.'' |title=Human keratinocyte ATP2C1 localizes to the Golgi and controls Golgi Ca2+ stores. |journal=J. Invest. Dermatol. |volume=121 |issue= 4 |pages= 688-94 |year= 2003 |pmid= 14632183 |doi= 10.1046/j.1523-1747.2003.12528.x }}
*{{cite journal  | vauthors=Mitchell KJ, Tsuboi T, Rutter GA |title=Role for plasma membrane-related Ca2+-ATPase-1 (ATP2C1) in pancreatic beta-cell Ca2+ homeostasis revealed by RNA silencing. |journal=Diabetes |volume=53 |issue= 2 |pages= 393–400 |year= 2004 |pmid= 14747290 |doi=10.2337/diabetes.53.2.393  }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | vauthors=Fairclough RJ, Lonie L, Van Baelen K |title=Hailey-Hailey disease: identification of novel mutations in ATP2C1 and effect of missense mutation A528P on protein expression levels. |journal=J. Invest. Dermatol. |volume=123 |issue= 1 |pages= 67–71 |year= 2004 |pmid= 15191544 |doi= 10.1111/j.0022-202X.2004.22713.x |display-authors=etal}}
*{{cite journal  | author=Mitchell KJ, Tsuboi T, Rutter GA |title=Role for plasma membrane-related Ca2+-ATPase-1 (ATP2C1) in pancreatic beta-cell Ca2+ homeostasis revealed by RNA silencing. |journal=Diabetes |volume=53 |issue= 2 |pages= 393-400 |year= 2004 |pmid= 14747290 |doi=  }}
*{{cite journal  | author=Fairclough RJ, Lonie L, Van Baelen K, ''et al.'' |title=Hailey-Hailey disease: identification of novel mutations in ATP2C1 and effect of missense mutation A528P on protein expression levels. |journal=J. Invest. Dermatol. |volume=123 |issue= 1 |pages= 67-71 |year= 2004 |pmid= 15191544 |doi= 10.1111/j.0022-202X.2004.22713.x }}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{ATPases}}
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Latest revision as of 18:24, 29 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Calcium-transporting ATPase type 2C member 1 is an enzyme that in humans is encoded by the ATP2C1 gene.[1][2][3]

This gene encodes one of the SPCA proteins, a Ca2+ ion-transporting P-type ATPase. This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of the calcium. Defects in this gene cause Hailey-Hailey disease, an autosomal dominant disorder. Alternatively spliced transcript variants encoding different isoforms have been identified.[3]

References

  1. Hu Z, Bonifas JM, Beech J, Bench G, Shigihara T, Ogawa H, Ikeda S, Mauro T, Epstein EH Jr (Feb 2000). "Mutations in ATP2C1, encoding a calcium pump, cause Hailey-Hailey disease". Nat Genet. 24 (1): 61–5. doi:10.1038/71701. PMID 10615129.
  2. Sudbrak R, Brown J, Dobson-Stone C, Carter S, Ramser J, White J, Healy E, Dissanayake M, Larregue M, Perrussel M, Lehrach H, Munro CS, Strachan T, Burge S, Hovnanian A, Monaco AP (Jun 2000). "Hailey-Hailey disease is caused by mutations in ATP2C1 encoding a novel Ca(2+) pump". Hum Mol Genet. 9 (7): 1131–40. doi:10.1093/hmg/9.7.1131. PMID 10767338.
  3. 3.0 3.1 "Entrez Gene: ATP2C1 ATPase, Ca++ transporting, type 2C, member 1".

External links

Further reading