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Showing Protein Sarcoplasmic/endoplasmic reticulum calcium ATPase 3 (HMDBP01255)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 6 metabolites
Identification
HMDB Protein ID HMDBP01255
Secondary Accession Numbers
  • 6551
Name Sarcoplasmic/endoplasmic reticulum calcium ATPase 3
Synonyms
  1. Calcium pump 3
  2. SERCA3
  3. SR Ca(2+)-ATPase 3
Gene Name ATP2A3
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 transport of calcium. Transports calcium ions from the cytosol into the sarcoplasmic/endoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction.
Pathways
  • Alzheimer disease
  • Calcium signaling pathway
  • Pancreatic secretion
Reactions Not Available
GO Classification
Biological Process
ATP biosynthetic process
blood coagulation
Cellular Component
endoplasmic reticulum membrane
platelet dense tubular network membrane
sarcoplasmic reticulum
sarcoplasmic reticulum membrane
nuclear membrane
integral to 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
metal ion binding
ATP binding
calcium-transporting ATPase activity
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. Multi-pass membrane protein
  5. Sarcoplasmic reticulum membrane
  6. Nucleus membrane
Gene Properties
Chromosome Location 17
Locus 17p13.3
SNPs ATP2A3
Gene Sequence 
>3132 bp
ATGGAGGCGGCGCATCTGCTCCCGGCCGCCGACGTGCTGCGCCACTTCTCGGTGACAGCC
GAGGGCGGCCTGAGCCCGGCGCAGGTGACCGGCGCGCGGGAGCGCTACGGCCCCAACGAG
CTCCCGAGTGAGGAAGGGAAGTCCCTGTGGGAGCTGGTGCTGGAACAGTTTGAGGACCTC
CTGGTGCGCATCCTGCTGCTGGCTGCCCTTGTCTCCTTTGTCCTGGCCTGGTTCGAGGAG
GGCGAGGAGACCACGACCGCCTTCGTGGAGCCCCTGGTCATCATGCTGATCCTCGTGGCC
AACGCCATTGTGGGCGTGTGGCAGGAACGCAACGCCGAGAGTGCCATCGAGGCCCTGAAG
GAGTATGAGCCTGAGATGGGCAAGGTGATCCGCTCGGACCGCAAGGGCGTGCAGAGGATC
CGTGCCCGGGACATCGTCCCAGGGGACATTGTAGAAGTGGCAGTGGGGGACAAAGTGCCT
GCTGACCTCCGCCTCATCGAGATCAAGTCCACCACGCTGCGAGTGGACCAGTCCATCCTG
ACGGGTGAATCTGTGTCCGTGACCAAGCACACAGAGGCCATCCCAGACCCCAGAGCTGTG
AACCAGGACAAGAAGAACATGCTGTTTTCTGGCACCAATATCACATCGGGCAAAGCGGTG
GGTGTGGCCGTGGCCACCGGCCTGCACACGGAGCTGGGCAAGATCCGGAGCCAGATGGCG
GCAGTCGAGCCCGAGCGGACGCCGCTGCAGCGCAAGCTGGACGAGTTTGGACGGCAGCTG
TCCCACGCCATCTCTGTGATCTGCGTGGCCGTGTGGGTCATCAACATCGGCCACTTCGCC
GACCCGGCCCACGGTGGCTCCTGGCTGCGTGGCGCTGTCTACTACTTCAAGATCGCCGTG
GCCCTGGCGGTGGCGGCCATCCCCGAGGGCCTCCCGGCTGTCATCACTACATGCCTGGCA
CTGGGCACGCGGCGCATGGCACGCAAGAACGCCATCGTGCGAAGCCTGCCGTCCGTGGAG
ACCCTGGGCTGCACCTCAGTCATCTGCTCCGACAAGACGGGCACGCTCACCACCAATCAG
ATGTCTGTCTGCCGGATGTTCGTGGTAGCCGAGGCCGATGCGGGCTCCTGCCTTTTGCAC
GAGTTCACCATCTCGGGTACCACGTATACCCCCGAGGGCGAAGTGCGGCAGGGGGATCAG
CCTGTGCGCTGCGGCCAGTTCGACGGGCTGGTGGAGCTGGCGACCATCTGCGCCCTGTGC
AACGACTCGGCTCTGGACTACAACGAGGCCAAGGGTGTGTATGAGAAGGTGGGAGAGGCC
ACGGAGACAGCTCTGACTTGCCTGGTGGAGAAGATGAACGTGTTCGACACCGACCTGCAG
GCTCTGTCCCGGGTGGAGCGAGCTGGCGCCTGTAACACGGTCATCAAGCAGCTGATGCGG
AAGGAGTTCACCCTGGAGTTCTCCCGAGACCGGAAATCCATGTCCGTGTACTGCACGCCC
ACCCGCCCTCACCCTACTGGCCAGGGCAGCAAGATGTTTGTGAAGGGGGCTCCTGAGAGT
GTGATCGAGCGCTGTAGCTCAGTCCGCGTGGGGAGCCGCACAGCACCCCTGACCCCCACC
TCCAGGGAGCAGATCCTGGCAAAGATCCGGGATTGGGGCTCAGGCTCAGACACGCTGCGC
TGCCTGGCACTGGCCACCCGGGACGCGCCCCCAAGGAAGGAGGACATGGAGCTGGACGAC
TGCAGCAAGTTTGTGCAGTACGAGACGGACCTGACCTTCGTGGGCTGCGTAGGCATGCTG
GACCCGCCGCGACCTGAGGTGGCTGCCTGCATCACACGCTGCTACCAGGCGGGCATCCGC
GTGGTCATGATCACGGGGGATAACAAAGGCACTGCCGTGGCCATCTGCCGCAGGCTTGGC
ATCTTTGGGGACACGGAAGACGTGGCGGGCAAGGCCTACACGGGCCGCGAGTTTGATGAC
CTCAGCCCCGAGCAGCAGCGCCAGGCCTGCCGCACCGCCCGCTGCTTCGCCCGCGTGGAG
CCCGCACACAAGTCCCGCATCGTGGAGAACCTGCAGTCCTTTAACGAGATCACTGCTATG
ACTGGCGATGGAGTGAACGACGCACCAGCCCTGAAGAAAGCAGAGATCGGCATCGCCATG
GGCTCAGGCACGGCCGTGGCCAAGTCGGCGGCAGAGATGGTGCTGTCAGATGACAACTTT
GCCTCCATCGTGGCTGCGGTGGAGGAGGGCCGGGCCATCTACAGCAACATGAAGCAATTC
ATCCGCTACCTCATCTCCTCCAATGTTGGCGAGGTCGTCTGCATCTTCCTCACGGCAATT
CTGGGCCTGCCCGAAGCCCTGATCCCTGTGCAGCTGCTCTGGGTGAACCTGGTGACAGAC
GGCCTACCTGCCACGGCTCTGGGCTTCAACCCGCCAGACCTGGACATCATGGAGAAGCTG
CCCCGGAGCCCCCGAGAAGCCCTCATCAGTGGCTGGCTCTTCTTCCGATACCTGGCTATC
GGAGTGTACGTAGGCCTGGCCACAGTGGCTGCCGCCACCTGGTGGTTTGTGTATGACGCC
GAGGGACCTCACATCAACTTCTACCAGCTGAGGAACTTCCTGAAGTGCTCCGAAGACAAC
CCGCTCTTTGCCGGCATCGACTGTGAGGTGTTCGAGTCACGCTTCCCCACCACCATGGCC
TTGTCCGTGCTCGTGACCATTGAAATGTGCAATGCCCTCAACAGCGTCTCGGAGAACCAG
TCGCTGCTGCGGATGCCGCCCTGGATGAACCCCTGGCTGCTGGTGGCTGTGGCCATGTCC
ATGGCCCTGCACTTCCTCATCCTGCTCGTGCCGCCCCTGCCTCTCATTTTCCAGGTGACC
CCACTGAGCGGGCGCCAGTGGGTGGTGGTGCTCCAGATATCTCTGCCTGTCATCCTGCTG
GATGAGGCCCTCAAGTACCTGTCCCGGAACCACATGCACGCCTGTCTTTATCCAGGCCTT
CTCAGGACAGTCTCGCAGGCCTGGAGTAGGCAGCCGCTGACCACCTCTTGGACCCCAGAC
CACACCGGAAGAAATGAGCCAGAAGTGAGCGCTGGGAACAGAGTGGAGTCTCCGGTGTGT
ACCTCAGACTGA
Protein Properties
Number of Residues 1043
Molecular Weight 109255.08
Theoretical pI 5.518
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Sarcoplasmic/endoplasmic reticulum calcium ATPase 3
MEAAHLLPAADVLRHFSVTAEGGLSPAQVTGARERYGPNELPSEEGKSLWELVLEQFEDL
LVRILLLAALVSFVLAWFEEGEETTTAFVEPLVIMLILVANAIVGVWQERNAESAIEALK
EYEPEMGKVIRSDRKGVQRIRARDIVPGDIVEVAVGDKVPADLRLIEIKSTTLRVDQSIL
TGESVSVTKHTEAIPDPRAVNQDKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMA
AVEPERTPLQRKLDEFGRQLSHAISVICVAVWVINIGHFADPAHGGSWLRGAVYYFKIAV
ALAVAAIPEGLPAVITTCLALGTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQ
MSVCRMFVVAEADAGSCLLHEFTISGTTYTPEGEVRQGDQPVRCGQFDGLVELATICALC
NDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTDLQALSRVERAGACNTVIKQLMR
KEFTLEFSRDRKSMSVYCTPTRPHPTGQGSKMFVKGAPESVIERCSSVRVGSRTAPLTPT
SREQILAKIRDWGSGSDTLRCLALATRDAPPRKEDMELDDCSKFVQYETDLTFVGCVGML
DPPRPEVAACITRCYQAGIRVVMITGDNKGTAVAICRRLGIFGDTEDVAGKAYTGREFDD
LSPEQQRQACRTARCFARVEPAHKSRIVENLQSFNEITAMTGDGVNDAPALKKAEIGIAM
GSGTAVAKSAAEMVLSDDNFASIVAAVEEGRAIYSNMKQFIRYLISSNVGEVVCIFLTAI
LGLPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMEKLPRSPREALISGWLFFRYLAI
GVYVGLATVAAATWWFVYDAEGPHINFYQLRNFLKCSEDNPLFAGIDCEVFESRFPTTMA
LSVLVTIEMCNALNSVSENQSLLRMPPWMNPWLLVAVAMSMALHFLILLVPPLPLIFQVT
PLSGRQWVVVLQISLPVILLDEALKYLSRNHMHACLYPGLLRTVSQAWSRQPLTTSWTPD
HTGRNEPEVSAGNRVESPVCTSD
GenBank ID Protein 28373109
UniProtKB/Swiss-Prot ID Q93084
UniProtKB/Swiss-Prot Entry Name AT2A3_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_174955.1
GeneCard ID ATP2A3
GenAtlas ID ATP2A3
HGNC ID HGNC:813
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed:16625196 ]
  3. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed:16959974 ]
  4. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed:12665801 ]
  5. Dode L, Wuytack F, Kools PF, Baba-Aissa F, Raeymaekers L, Brike F, van de Ven WJ, Casteels R: cDNA cloning, expression and chromosomal localization of the human sarco/endoplasmic reticulum Ca(2+)-ATPase 3 gene. Biochem J. 1996 Sep 1;318 ( Pt 2):689-99. [PubMed:8809064 ]
  6. Dode L, De Greef C, Mountian I, Attard M, Town MM, Casteels R, Wuytack F: Structure of the human sarco/endoplasmic reticulum Ca2+-ATPase 3 gene. Promoter analysis and alternative splicing of the SERCA3 pre-mRNA. J Biol Chem. 1998 May 29;273(22):13982-94. [PubMed:9593748 ]
  7. Poch E, Leach S, Snape S, Cacic T, MacLennan DH, Lytton J: Functional characterization of alternatively spliced human SERCA3 transcripts. Am J Physiol. 1998 Dec;275(6 Pt 1):C1449-58. [PubMed:9843705 ]
  8. Wuytack F, Papp B, Verboomen H, Raeymaekers L, Dode L, Bobe R, Enouf J, Bokkala S, Authi KS, Casteels R: A sarco/endoplasmic reticulum Ca(2+)-ATPase 3-type Ca2+ pump is expressed in platelets, in lymphoid cells, and in mast cells. J Biol Chem. 1994 Jan 14;269(2):1410-6. [PubMed:8288608 ]