ATP2A3

ATP2A3

Identifiers

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

External IDs

OMIM: 601929 MGI: 1194503 HomoloGene: 69131 GeneCards: ATP2A3

Gene location (Human)

Chr.	Chromosome 17 (human)^[1]

Band	17p13.2	Start	3,923,870 bp^[1]
Band	17p13.2	End	3,964,464 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 11 (mouse)^[2]

Band	11\|11 B4	Start	72,851,995 bp^[2]
Band	11\|11 B4	End	72,883,870 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

spleen

thymus

lymph node

blood

bone marrow cells

appendix

minor salivary gland

rectum

thymus

gastric mucosa

Top expressed in

submandibular gland

parotid gland

islet of Langerhans

pyloric antrum

crypt of lieberkuhn of small intestine

colon

left colon

thymus

epithelium of stomach

lymph node

More reference expression data

BioGPS


More reference expression data

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

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 NP_777613 NP_777614 NP_777615 NP_777616
NP_777617 NP_777618


NP_001156808 NP_001156809 NP_058025

Location (UCSC)

Chr 17: 3.92 – 3.96 Mb

Chr 11: 72.85 – 72.88 Mb

PubMed search

^[3]

^[4]

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.^[5]^[6]

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.^[6]

YouTube Encyclopedic

1/2
Views:
411
388

Transcription

Cancer

ATP2A3 gene has been observed progressively downregulated in Human papillomavirus-positive neoplastic keratinocytes derived from uterine cervical preneoplastic lesions at different levels of malignancy.^[7] For this reason, ATP2A3 is likely to be associated with tumorigenesis and may be a potential prognostic marker for uterine cervical preneoplastic lesions progression.^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000074370 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000020788 - Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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. doi:10.1042/bj3180689. PMC 1217674. PMID 8809064.
^ ^a ^b "Entrez Gene: ATP2A3 ATPase, Ca++ transporting, ubiquitous".
^ ^a ^b Rotondo JC, Bosi S, Bassi C, Ferracin M, Lanza G, Gafà R, Magri E, Selvatici R, Torresani S, Marci R, Garutti P, Negrini M, Tognon M, Martini F (April 2015). "Gene expression changes in progression of cervical neoplasia revealed by microarray analysis of cervical neoplastic keratinocytes". J Cell Physiol. 230 (4): 802–812. doi:10.1002/jcp.24808. hdl:11392/2066612. PMID 25205602. S2CID 24986454.

External links

Human ATP2A3 genome location and ATP2A3 gene details page in the UCSC Genome Browser.

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. doi:10.1016/S0021-9258(17)42273-3. PMID 8288608.
Dode L, De Greef C, Mountain 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. doi:10.1152/ajpcell.1998.275.6.C1449. 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. Bibcode:2002PNAS...9916899M. 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. S2CID 23783563.
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. S2CID 24473757.
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_olf G_αi GNAI1 GNAI2 GNAI3 Transducin GNAT1 GNAT2 Gustducin GNAT3 G_αq/11 GNAQ GNA11 G_α12/13 GNA12 GNA13
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 superfamily Dynamin Guanylate-binding protein Mitofusin-1 MX1 and MX2 OPA1 Tubulin

This article on a gene on human chromosome 17 is a stub. You can help Wikipedia by expanding it.

This page was last edited on 13 August 2023, at 19:42

From Wikipedia, the free encyclopedia

YouTube Encyclopedic

Transcription

Cancer

References

External links

Further reading