ATP2A3

Identifiers

ATP2A3, SERCA3, ATPase sarcoplasmic/endoplasmic reticulum Ca2+ transporting 3

External IDs

MGI: 1194503 HomoloGene: 69131 GeneCards: ATP2A3

Gene ontology
Molecular function	• nucleotide binding • calcium-transporting ATPase activity • metal ion binding • hydrolase activity • ATP binding
Cellular component	• integral component of membrane • nuclear membrane • endoplasmic reticulum membrane • membrane • integral component of plasma membrane • sarcoplasmic reticulum • platelet dense tubular network membrane • endoplasmic reticulum • sarcoplasmic reticulum membrane • nucleus
Biological process	• regulation of cardiac conduction • cellular calcium ion homeostasis • ion transport • ion transmembrane transport • calcium ion transmembrane transport • transport • calcium ion transport
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


489


53313

Ensembl


ENSG00000074370


ENSMUSG00000020788

UniProt


Q93084


Q64518

RefSeq (mRNA)

NM_005173 NM_174953 NM_174954 NM_174955 NM_174956
NM_174957 NM_174958


NM_001163336 NM_001163337 NM_016745

RefSeq (protein)

NP_005164.2 NP_777613.1 NP_777614.1 NP_777615.1 NP_777616.1
NP_777617.1 NP_777618.1


NP_001156809.1 NP_058025.2

Location (UCSC)

Chr 17: 3.92 – 3.96 Mb

Chr 11: 72.96 – 72.99 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Sarcoplasmic/endoplasmic reticulum calcium ATPase 3 is an enzyme that in humans is encoded by the ATP2A3 gene.^[3]^[4]

This gene encodes one of the SERCA Ca²⁺-ATPases, which are intracellular pumps located in the sarcoplasmic or endoplasmic reticula of cells. SERCA3 expression was originally described as non-muscular, but was recently observed in cardiomyocyte. This enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen, and is involved in calcium sequestration associated with muscular excitation and contraction. Alternative splicing results in 6 transcript variants encoding different isoforms named SERCA3a to SERCA3f.^[4]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Dode L, Wuytack F, Kools PF, Baba-Aissa F, Raeymaekers L, Brike F, van de Ven WJ, Casteels R (Nov 1996). "cDNA cloning, expression and chromosomal localization of the human sarco/endoplasmic reticulum Ca²⁺-ATPase 3 gene". Biochem J. 318 (2): 689–99. PMC 1217674. PMID 8809064.
1 2 "Entrez Gene: ATP2A3 ATPase, Ca++ transporting, ubiquitous".

Wuytack F, Papp B, Verboomen H, et al. (1994). "A sarco/endoplasmic reticulum Ca²⁺-ATPase 3-type Ca²⁺ pump is expressed in platelets, in lymphoid cells, and in mast cells". J. Biol. Chem. 269 (2): 1410–6. PMID 8288608.
Dode L, De Greef C, Mountian I, et al. (1998). "Structure of the human sarco/endoplasmic reticulum Ca²⁺-ATPase 3 gene. Promoter analysis and alternative splicing of the SERCA3 pre-mRNA". J. Biol. Chem. 273 (22): 13982–94. doi:10.1074/jbc.273.22.13982. PMID 9593748.
Poch E, Leach S, Snape S, et al. (1999). "Functional characterization of alternatively spliced human SERCA3 transcripts". Am. J. Physiol. 275 (6 Pt 1): C1449–58. PMID 9843705.
Martin V, Bredoux R, Corvazier E, et al. (2002). "Three novel sarco/endoplasmic reticulum Ca²⁺-ATPase (SERCA) 3 isoforms. Expression, regulation, and function of the membranes of the SERCA3 family". J. Biol. Chem. 277 (27): 24442–52. doi:10.1074/jbc.M202011200. PMID 11956212.
Gélébart P, Kovács T, Brouland JP, et al. (2002). "Expression of endomembrane calcium pumps in colon and gastric cancer cells. Induction of SERCA3 expression during differentiation". J. Biol. Chem. 277 (29): 26310–20. doi:10.1074/jbc.M201747200. PMID 11986315.
Dode L, Vilsen B, Van Baelen K, et al. (2003). "Dissection of the functional differences between sarco(endo)plasmic reticulum Ca²⁺-ATPase (SERCA) 1 and 3 isoforms by steady-state and transient kinetic analyses". J. Biol. Chem. 277 (47): 45579–91. doi:10.1074/jbc.M207778200. PMID 12207029.
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.
Houston R (2003). "Longitudinal sections of unfixed muscle". Biotechnic & Histochemistry. 77 (4): 229–30. PMID 12503734.
Borge PD, Wolf BA (2003). "Insulin receptor substrate 1 regulation of sarco-endoplasmic reticulum calcium ATPase 3 in insulin-secreting beta-cells". J. Biol. Chem. 278 (13): 11359–68. doi:10.1074/jbc.M209521200. PMID 12524443.
Chandrasekera CP, Lytton J (2003). "Inhibition of human SERCA3 by PL/IM430. Molecular analysis of the interaction". J. Biol. Chem. 278 (14): 12482–8. doi:10.1074/jbc.M212745200. PMID 12540840.
Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
Bobe R, Bredoux R, Corvazier E, et al. (2004). "Identification, expression, function, and localization of a novel (sixth) isoform of the human sarco/endoplasmic reticulum Ca²⁺ATPase 3 gene". J. Biol. Chem. 279 (23): 24297–306. doi:10.1074/jbc.M314286200. PMID 15028735.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Brouland JP, Gélébart P, Kovàcs T, et al. (2005). "The loss of sarco/endoplasmic reticulum calcium transport ATPase 3 expression is an early event during the multistep process of colon carcinogenesis". Am. J. Pathol. 167 (1): 233–42. doi:10.1016/S0002-9440(10)62968-9. PMC 1603437. PMID 15972967.
Hadri L, Pavoine C, Lipskaia L, et al. (2006). "Transcription of the sarcoplasmic/endoplasmic reticulum Ca²⁺-ATPase type 3 gene, ATP2A3, is regulated by the calcineurin/NFAT pathway in endothelial cells". Biochem. J. 394 (Pt 1): 27–33. doi:10.1042/BJ20051387. PMC 1385999. PMID 16250893.
Wootton LL, Michelangeli F (2006). "The effects of the phenylalanine 256 to valine mutation on the sensitivity of sarcoplasmic/endoplasmic reticulum Ca²⁺ ATPase (SERCA) Ca²⁺ pump isoforms 1, 2, and 3 to thapsigargin and other inhibitors". J. Biol. Chem. 281 (11): 6970–6. doi:10.1074/jbc.M510978200. PMID 16410239.
Chaâbane C, Corvazier E, Bredoux R, et al. (2006). "Sarco/endoplasmic reticulum Ca²⁺ATPase type 3 isoforms (SERCA3b and SERCA3f): distinct roles in cell adhesion and ER stress". Biochem. Biophys. Res. Commun. 345 (4): 1377–85. doi:10.1016/j.bbrc.2006.05.054. PMID 16725111.
Bredoux R, Corvazier E, Dally S, et al. (2006). "Human platelet Ca²⁺-ATPases: new markers of cell differentiation as illustrated in idiopathic scoliosis". Platelets. 17 (6): 421–33. doi:10.1080/09537100600758719. PMID 16973504.
Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

Hydrolases: acid anhydride hydrolases (EC 3.6)

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)	SERCA ATP2A1 ATP2A2 ATP2A3 Plasma membrane ATP2B1 ATP2B2 ATP2B3 ATP2B4 SPCA ATP2C1 ATP2C2

Na+/K+ (3.6.3.9)	ATP1A1 ATP1A2 ATP1A3 ATP1A4 ATP1B1 ATP1B2 ATP1B3 ATP1B4

H+/K+ (3.6.3.10)	ATP4A

Other P-type ATPase	ATP8B1 ATP10A ATP11B ATP12A ATP13A2 ATP13A3

3.6.4

3.6.5: GTPase

3.6.5.1: Heterotrimeric G protein	G_αs G_αi GNAI1 GNAI2 GNAI3 G_αq/11 GNAQ GNA11 G_α12/13 GNA12 GNA13 Transducin GNAT1 GNAT2 Gustducin GNAT3

3.6.5.2: Small GTPase > Ras superfamily	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 RGK

3.6.5.3: Protein-synthesizing GTPase	Prokaryotic IF-2 EF-Tu EF-G Eukaryotic

3.6.5.5-6: Polymerization motors	Dynamin Tubulin

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ATP2A3

References

Further reading