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Identification
HMDB Protein ID HMDBP01470
Secondary Accession Numbers
  • 6766
Name Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
Synonyms
  1. Calcium pump 2
  2. Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform
  3. Endoplasmic reticulum class 1/2 Ca(2+) ATPase
  4. SERCA2
  5. SR Ca(2+)-ATPase 2
Gene Name ATP2A2
Protein Type Unknown
Biological Properties
General Function Involved in ATP binding
Specific Function This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Isoform 2 is involved in the regulation of the contraction/relaxation cycle.
Pathways
  • Acebutolol Action Pathway
  • Alprenolol Action Pathway
  • Alzheimer's disease
  • Amiodarone Action Pathway
  • Amlodipine Action Pathway
  • Arbutamine Action Pathway
  • Arrhythmogenic right ventricular cardiomyopathy (ARVC)
  • Atenolol Action Pathway
  • Betaxolol Action Pathway
  • Bevantolol Action Pathway
  • Bisoprolol Action Pathway
  • Bopindolol Action Pathway
  • Bupranolol Action Pathway
  • Calcium signaling pathway
  • Cardiac muscle contraction
  • Carteolol Action Pathway
  • Carvedilol Action Pathway
  • Dilated cardiomyopathy
  • Diltiazem Action Pathway
  • Disopyramide Action Pathway
  • Dobutamine Action Pathway
  • Epinephrine Action Pathway
  • Esmolol Action Pathway
  • Felodipine Action Pathway
  • Flecainide Action Pathway
  • Fosphenytoin (Antiarrhythmic) Action Pathway
  • Hypertrophic cardiomyopathy (HCM)
  • Ibutilide Action Pathway
  • Isoprenaline Action Pathway
  • Isradipine Action Pathway
  • Labetalol Action Pathway
  • Levobunolol Action Pathway
  • Lidocaine (Antiarrhythmic) Action Pathway
  • Metipranolol Action Pathway
  • Metoprolol Action Pathway
  • Mexiletine Action Pathway
  • Muscle/Heart Contraction
  • Nadolol Action Pathway
  • Nebivolol Action Pathway
  • Nifedipine Action Pathway
  • Nimodipine Action Pathway
  • Nisoldipine Action Pathway
  • Nitrendipine Action Pathway
  • Oxprenolol Action Pathway
  • Pancreatic secretion
  • Penbutolol Action Pathway
  • Phenytoin (Antiarrhythmic) Action Pathway
  • Pindolol Action Pathway
  • Practolol Action Pathway
  • Procainamide (Antiarrhythmic) Action Pathway
  • Propranolol Action Pathway
  • Quinidine Action Pathway
  • Sotalol Action Pathway
  • Timolol Action Pathway
  • Tocainide Action Pathway
  • Verapamil Action Pathway
Reactions Not Available
GO Classification
Biological Process
ATP biosynthetic process
cell adhesion
negative regulation of heart contraction
regulation of the force of heart contraction
blood coagulation
cellular calcium ion homeostasis
ER-nucleus signaling pathway
response to peptide hormone stimulus
sarcoplasmic reticulum calcium ion transport
epidermis development
Cellular Component
platelet dense tubular network membrane
sarcoplasmic reticulum membrane
protein complex
integral to plasma membrane
Component
membrane
cell part
membrane part
intrinsic to membrane
integral to membrane
Function
di-, tri-valent inorganic cation transmembrane transporter activity
calcium ion transmembrane transporter activity
calcium-transporting atpase activity
binding
catalytic activity
hydrolase activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
atp binding
transmembrane transporter activity
substrate-specific transmembrane transporter activity
ion transmembrane transporter activity
cation transmembrane transporter activity
inorganic cation transmembrane transporter activity
transporter activity
atpase activity, coupled to transmembrane movement of ions
atpase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
hydrolase activity, acting on acid anhydrides
Molecular Function
ATP binding
calcium-transporting ATPase activity
calcium ion binding
Process
purine nucleotide metabolic process
purine nucleotide biosynthetic process
purine nucleoside triphosphate biosynthetic process
purine ribonucleoside triphosphate biosynthetic process
di-, tri-valent inorganic cation transport
divalent metal ion transport
calcium ion transport
metabolic process
nitrogen compound metabolic process
cellular nitrogen compound metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
establishment of localization
transport
ion transport
atp biosynthetic process
cation transport
Cellular Location
  1. Endoplasmic reticulum membrane
  2. Multi-pass membrane protein
  3. Multi-pass membrane protein
  4. Sarcoplasmic reticulum membrane
Gene Properties
Chromosome Location 12
Locus 12q24.11
SNPs ATP2A2
Gene Sequence
>3129 bp
ATGGAGAACGCGCACACCAAGACGGTGGAGGAGGTGCTGGGCCACTTCGGCGTCAACGAG
AGTACGGGGCTGAGCCTGGAACAGGTCAAGAAGCTTAAGGAGAGATGGGGCTCCAACGAG
TTACCGGCTGAAGAAGGAAAAACCTTGCTGGAACTTGTGATTGAGCAGTTTGAAGACTTG
CTAGTTAGGATTTTATTACTGGCAGCATGTATATCTTTTGTTTTGGCTTGGTTTGAAGAA
GGTGAAGAAACAATTACAGCCTTTGTAGAACCTTTTGTAATTTTACTCATATTAGTAGCC
AATGCAATTGTGGGTGTATGGCAGGAAAGAAATGCTGAAAATGCCATCGAAGCCCTTAAG
GAATATGAGCCTGAAATGGGCAAAGTGTATCGACAGGACAGAAAGAGTGTGCAGCGGATT
AAAGCTAAAGACATAGTTCCTGGTGATATTGTAGAAATTGCTGTTGGTGACAAAGTTCCT
GCTGATATAAGGTTAACTTCCATCAAATCTACCACACTAAGAGTTGACCAGTCAATTCTC
ACAGGTGAATCTGTCTCTGTCATCAAGCACACTGATCCCGTCCCTGACCCACGAGCTGTC
AACCAAGATAAAAAGAACATGCTGTTTTCTGGTACAAACATTGCTGCTGGGAAAGCTATG
GGAGTGGTGGTAGCAACTGGAGTTAACACCGAAATTGGCAAGATCCGGGATGAAATGGTG
GCAACAGAACAGGAGAGAACACCCCTTCAGCAAAAACTAGATGAATTTGGGGAACAGCTT
TCCAAAGTCATCTCCCTTATTTGCATTGCAGTCTGGATCATAAATATTGGGCACTTCAAT
GACCCGGTTCATGGAGGGTCCTGGATCAGAGGTGCTATTTACTACTTTAAAATTGCAGTG
GCCCTGGCTGTAGCAGCCATTCCTGAAGGTCTGCCTGCAGTCATCACCACCTGCCTGGCT
CTTGGAACTCGCAGAATGGCAAAGAAAAATGCCATTGTTCGAAGCCTCCCGTCTGTGGAA
ACCCTTGGTTGTACTTCTGTTATCTGCTCAGACAAGACTGGTACACTTACAACAAACCAG
ATGTCAGTCTGCAGGATGTTCATTCTGGACAGAGTGGAAGGTGATACTTGTTCCCTTAAT
GAGTTTACCATAACTGGATCAACTTATGCACCTATTGGAGAAGTGCATAAAGATGATAAA
CCAGTGAATTGTCACCAGTATGATGGTCTGGTAGAATTAGCAACAATTTGTGCTCTTTGT
AATGACTCTGCTTTGGATTACAATGAGGCAAAGGGTGTGTATGAAAAAGTTGGAGAAGCT
ACAGAGACTGCTCTCACTTGCCTAGTAGAGAAGATGAATGTATTTGATACCGAATTGAAG
GGTCTTTCTAAAATAGAACGTGCAAATGCCTGCAACTCAGTCATTAAACAGCTGATGAAA
AAGGAATTCACTCTAGAGTTTTCACGTGACAGAAAGTCAATGTCGGTTTACTGTACACCA
AATAAACCAAGCAGGACATCAATGAGCAAGATGTTTGTGAAGGGTGCTCCTGAAGGTGTC
ATTGACAGGTGCACCCACATTCGAGTTGGAAGTACTAAGGTTCCTATGACCTCTGGAGTC
AAACAGAAGATCATGTCTGTCATTCGAGAGTGGGGTAGTGGCAGCGACACACTGCGATGC
CTGGCCCTGGCCACTCATGACAACCCACTGAGAAGAGAAGAAATGCACCTTGAGGACTCT
GCCAACTTTATTAAATATGAGACCAATCTGACCTTCGTTGGCTGCGTGGGCATGCTGGAT
CCTCCGAGAATCGAGGTGGCCTCCTCCGTGAAGCTGTGCCGGCAAGCAGGCATCCGGGTC
ATCATGATCACTGGGGACAACAAGGGCACTGCTGTGGCCATCTGTCGCCGCATCGGCATC
TTCGGGCAGGATGAGGACGTGACGTCAAAAGCTTTCACAGGCCGGGAGTTTGATGAACTC
AACCCCTCCGCCCAGCGAGACGCCTGCCTGAACGCCCGCTGTTTTGCTCGAGTTGAACCC
TCCCACAAGTCTAAAATCGTAGAATTTCTTCAGTCTTTTGATGAGATTACAGCTATGACT
GGCGATGGCGTGAACGATGCTCCTGCTCTGAAGAAAGCCGAGATTGGCATTGCTATGGGC
TCTGGCACTGCGGTGGCTAAAACCGCCTCTGAGATGGTCCTGGCGGATGACAACTTCTCC
ACCATTGTGGCTGCCGTTGAGGAGGGGCGGGCAATCTACAACAACATGAAACAGTTCATC
CGCTACCTCATCTCGTCCAACGTCGGGGAAGTTGTCTGTATTTTCCTGACAGCAGCCCTT
GGATTTCCCGAGGCTTTGATTCCTGTTCAGCTGCTCTGGGTCAATCTGGTGACAGATGGC
CTGCCTGCCACTGCACTGGGGTTCAACCCTCCTGATCTGGACATCATGAATAAACCTCCC
CGGAACCCAAAGGAACCATTGATCAGCGGGTGGCTCTTTTTCCGTTACTTGGCTATTGGC
TGTTACGTCGGCGCTGCTACCGTGGGTGCTGCTGCATGGTGGTTCATTGCTGCTGACGGT
GGTCCAAGAGTGTCCTTCTACCAGCTGAGTCATTTCCTACAGTGTAAAGAGGACAACCCG
GACTTTGAAGGCGTGGATTGTGCAATCTTTGAATCCCCATACCCGATGACAATGGCGCTC
TCTGTTCTAGTAACTATAGAAATGTGTAACGCCCTCAACAGCTTGTCCGAAAACCAGTCC
TTGCTGAGGATGCCCCCCTGGGAGAACATCTGGCTCGTGGGCTCCATCTGCCTGTCCATG
TCACTCCACTTCCTGATCCTCTATGTCGAACCCTTGCCACTCATCTTCCAGATCACACCG
CTGAACGTGACCCAGTGGCTGATGGTGCTGAAAATCTCCTTGCCCGTGATTCTCATGGAT
GAGACGCTCAAGTTTGTGGCCCGCAACTACCTGGAACCTGGTAAAGAGTGTGTGCAGCCT
GCCACCAAATCCTGCTCGTTCTCGGCATGCACCGATGGGATTTCCTGGCCGTTTGTGCTG
CTCATAATGCCCCTGGTGATCTGGGTCTATAGCACAGACACTAACTTTAGCGATATGTTC
TGGTCTTGA
Protein Properties
Number of Residues 1042
Molecular Weight 109689.97
Theoretical pI 5.366
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
MENAHTKTVEEVLGHFGVNESTGLSLEQVKKLKERWGSNELPAEEGKTLLELVIEQFEDL
LVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILVANAIVGVWQERNAENAIEALK
EYEPEMGKVYRQDRKSVQRIKAKDIVPGDIVEIAVGDKVPADIRLTSIKSTTLRVDQSIL
TGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKAMGVVVATGVNTEIGKIRDEMV
ATEQERTPLQQKLDEFGEQLSKVISLICIAVWIINIGHFNDPVHGGSWIRGAIYYFKIAV
ALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQ
MSVCRMFILDRVEGDTCSLNEFTITGSTYAPIGEVHKDDKPVNCHQYDGLVELATICALC
NDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTELKGLSKIERANACNSVIKQLMK
KEFTLEFSRDRKSMSVYCTPNKPSRTSMSKMFVKGAPEGVIDRCTHIRVGSTKVPMTSGV
KQKIMSVIREWGSGSDTLRCLALATHDNPLRREEMHLEDSANFIKYETNLTFVGCVGMLD
PPRIEVASSVKLCRQAGIRVIMITGDNKGTAVAICRRIGIFGQDEDVTSKAFTGREFDEL
NPSAQRDACLNARCFARVEPSHKSKIVEFLQSFDEITAMTGDGVNDAPALKKAEIGIAMG
SGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAAL
GFPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMNKPPRNPKEPLISGWLFFRYLAIG
CYVGAATVGAAAWWFIAADGGPRVSFYQLSHFLQCKEDNPDFEGVDCAIFESPYPMTMAL
SVLVTIEMCNALNSLSENQSLLRMPPWENIWLVGSICLSMSLHFLILYVEPLPLIFQITP
LNVTQWLMVLKISLPVILMDETLKFVARNYLEPGKECVQPATKSCSFSACTDGISWPFVL
LIMPLVIWVYSTDTNFSDMFWS
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P16615
UniProtKB/Swiss-Prot Entry Name AT2A2_HUMAN
PDB IDs Not Available
GenBank Gene ID M23114
GeneCard ID ATP2A2
GenAtlas ID ATP2A2
HGNC ID HGNC:812
References
General References
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  8. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed:17081983 ]
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  19. Dhitavat J, Macfarlane S, Dode L, Leslie N, Sakuntabhai A, MacSween R, Saihan E, Hovnanian A: Acrokeratosis verruciformis of Hopf is caused by mutation in ATP2A2: evidence that it is allelic to Darier's disease. J Invest Dermatol. 2003 Feb;120(2):229-32. [PubMed:12542527 ]
  20. Dally S, Bredoux R, Corvazier E, Andersen JP, Clausen JD, Dode L, Fanchaouy M, Gelebart P, Monceau V, Del Monte F, Gwathmey JK, Hajjar R, Chaabane C, Bobe R, Raies A, Enouf J: Ca2+-ATPases in non-failing and failing heart: evidence for a novel cardiac sarco/endoplasmic reticulum Ca2+-ATPase 2 isoform (SERCA2c). Biochem J. 2006 Apr 15;395(2):249-58. [PubMed:16402920 ]
  21. Tsuruta D, Akiyama M, Ishida-Yamamoto A, Imanishi H, Mizuno N, Sowa J, Kobayashi H, Ishii M, Kurokawa I, Shimizu H: Three-base deletion mutation c.120_122delGTT in ATP2A2 leads to the unique phenotype of comedonal Darier disease. Br J Dermatol. 2010 Mar;162(3):687-9. doi: 10.1111/j.1365-2133.2009.09580.x. Epub 2009 Nov 30. [PubMed:19995371 ]