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Identification
HMDB Protein ID HMDBP01347
Secondary Accession Numbers
  • 6643
  • HMDBP10473
Name Plasma membrane calcium-transporting ATPase 4
Synonyms
  1. Matrix-remodeling-associated protein 1
  2. PMCA4
  3. Plasma membrane calcium ATPase isoform 4
  4. Plasma membrane calcium pump isoform 4
  5. SubName: ATPase, Ca++ transporting, plasma membrane 4, isoform CRA_a
Gene Name ATP2B4
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 out of the cell.
Pathways
  • Calcium signaling pathway
  • Pancreatic secretion
  • Salivary secretion
Reactions Not Available
GO Classification
Biological Process
ATP biosynthetic process
blood coagulation
neural retina development
Cellular Component
integral to plasma membrane
Component
membrane
cell part
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. Cell membrane
  2. Cytoplasmic
  3. Multi-pass membrane protein
Gene Properties
Chromosome Location 1
Locus 1q32.1
SNPs ATP2B4
Gene Sequence
>3618 bp
ATGACGAACCCATCAGACCGTGTCTTGCCTGCCAACTCGATGGCCGAGAGCCGTGAAGGG
GACTTTGGCTGCACAGTAATGGAACTGAGGAAGCTCATGGAGCTGCGTTCAAGGGATGCA
CTGACCCAGATTAATGTCCACTATGGAGGTGTACAGAATCTCTGCAGTAGACTGAAAACC
TCCCCTGTGGAAGGTCTGTCTGGGAACCCTGCAGATCTGGAGAAACGTAGGCAGGTGTTT
GGACACAACGTGATCCCCCCCAAAAAGCCCAAGACTTTCTTAGAATTAGTGTGGGAAGCT
CTTCAAGATGTCACGCTCATCATCCTGGAGATTGCAGCCATCATCTCCCTGGTCCTGTCC
TTTTATCGCCCTGCTGGTGAAGAAAATGAACTGTGTGGTCAAGTCGCAACTACCCCAGAA
GATGAAAATGAGGCACAAGCTGGCTGGATTGAGGGGGCAGCCATCCTTTTCTCAGTGATC
ATCGTGGTGTTAGTGACTGCCTTTAATGATTGGAGCAAAGAGAAGCAATTCCGGGGGCTG
CAGTGCCGCATTGAACAGGAGCAAAAGTTCTCCATCATCCGAAACGGTCAACTCATCCAG
CTCCCTGTGGCTGAGATTGTGGTTGGTGATATTGCCCAAGTCAAATACGGTGATCTGCTG
CCTGCAGATGGAATCCTGATCCAAGGGAATGATCTGAAGATTGATGAGAGCTCTCTGACA
GGGGAATCTGACCATGTCAAGAAGTCCCTGGACAAAGACCCCATGTTGCTCTCAGGGACC
CATGTCATGGAAGGTTCTGGCCGGATGGTGGTGACAGCTGTTGGTGTCAACTCTCAGACT
GGAATCATCCTTACTCTCTTGGGGGTCAATGAGGATGACGAAGGGGAGAAAAAGAAGAAA
GGTAAAAAACAAGGAGTCCCTGAAAATCGCAACAAAGCAAAGACCCAAGACGGAGTGGCC
CTGGAAATCCAGCCACTCAACAGCCAGGAGGGAATCGACAATGAGGAAAAGGACAAGAAG
GCAGTCAAGGTGCCTAAAAAGGAGAAGTCAGTGCTGCAGGGCAAGCTGACTCGCCTGGCT
GTTCAGATTGGGAAAGCCGGTCTGCTCATGTCTGCTCTCACGGTTTTCATCCTGATTCTA
TACTTTGTGATTGACAACTTTGTGATAAATCGCAGACCATGGCTCCCTGAGTGTACTCCC
ATCTACATCCAGTACTTTGTCAAGTTCTTCATCATCGGCATCACTGTACTGGTGGTGGCT
GTGCCAGAGGGGCTGCCTCTGGCTGTCACCATCTCACTGGCCTACTCTGTGAAGAAAATG
ATGAAAGACAATAACCTAGTACGGCACTTGGATGCTTGTGAGACCATGGGCAACGCCACC
GCCATCTGCTCTGATAAGACAGGCACGTTGACCATGAACCGCATGACTGTGGTACAAGCT
TATATTGGGGGCATCCATTACCGTCAAATCCCAAGCCCTGATGTCTTCCTGCCCAAAGTC
CTGGACCTCATTGTCAATGGCATTTCTATCAACAGTGCTTATACCTCCAAGATTCTGCCT
CCAGAGAAGGAGGGAGGCCTGCCTCGGCAGGTGGGCAACAAGACCGAGTGTGCTCTGCTA
GGCTTTGTCACAGATCTGAAGCAGGATTATCAGGCTGTGCGTAATGAAGTGCCCGAGGAG
AAGCTCTACAAGGTGTACACCTTTAACTCAGTGCGCAAGTCAATGAGCACCGTCATCAGG
AATCCCAACGGTGGCTTCCGTATGTACAGCAAGGGCGCCTCTGAGATCATCTTGCGCAAG
TGTAATCGAATCCTGGACCGGAAAGGGGAAGCAGTGCCATTCAAGAATAAAGACAGAGAT
GATATGGTACGCACTGTCATCGAGCCCATGGCCTGTGATGGACTCCGGACTATCTGCATA
GCTTACCGGGACTTCGATGACACAGAGCCCTCTTGGGACAATGAGAATGAGATCCTCACC
GAACTGACCTGTATCGCGGTGGTGGGCATTGAGGACCCTGTGCGCCCAGAGGTGCCAGAT
GCTATTGCCAAATGCAAACAAGCTGGCATTACTGTCAGAATGGTGACAGGTGACAACATC
AACACAGCCCGGGCCATTGCCACCAAATGTGGCATTCTGACACCTGGGGATGACTTCCTG
TGCTTAGAAGGCAAAGAATTCAACCGGCTCATCCGCAACGAGAAAGGCGAGGTAGAGCAA
GAAAAGCTGGACAAGATCTGGCCTAAGCTTCGGGTCCTGGCGCGATCTTCTCCCACTGAC
AAGCACACCCTGGTGAAAGGCATAATTGACAGCACTGTTGGGGAACACCGGCAGGTCGTG
GCTGTCACTGGTGATGGCACAAATGACGGGCCTGCTCTGAAGAAAGCGGATGTTGGTTTT
GCCATGGGCATCGCAGGCACAGATGTAGCAAAGGAGGCTTCAGACATCATCCTAACAGAT
GACAACTTCACCAGCATTGTGAAGGCAGTGATGTGGGGACGAAATGTCTATGACAGCATC
TCCAAGTTCCTGCAGTTCCAGCTCACTGTCAATGTGGTGGCCGTGATTGTAGCCTTCACT
GGAGCCTGTATCACTCAGGATTCCCCATTGAAAGCTGTGCAGATGTTGTGGGTTAATCTG
ATCATGGACACTTTTGCTTCATTGGCCCTGGCCACAGAGCCCCCTACGGAATCTCTGTTG
AAGCGGCGCCCCTATGGCCGAAATAAGCCTCTGATCTCACGCACTATGATGAAGAACATC
TTGGGCCATGCATTCTATCAGCTCATTGTCATCTTTATCCTTGTCTTTGCGGGTGAGAAA
TTCTTTGATATTGATAGTGGGAGGAAGGCACCTCTACATTCACCACCCAGCCAGCACTAT
ACCATTGTTTTTAACACCTTCGTGCTGATGCAGCTCTTCAATGAAATCAACTCCCGAAAG
ATCCATGGAGAGAAGAACGTCTTTTCAGGCATCTACCGCAACATTATCTTCTGCTCTGTA
GTCTTGGGCACATTCATCTGCCAGATTTTCATCGTGGAATTTGGGGGTAAACCCTTCAGT
TGTACAAGCCTCAGCCTGTCTCAGTGGCTGTGGTGTCTCTTCATTGGGATTGGAGAACTT
CTGTGGGGCCAGTTCATCTCCGCAATACCTACCCGATCCCTGAAGTTCCTGAAGGAGGCT
GGGCATGGCACCACCAAAGAGGAGATCACCAAGGATGCCGAGGGACTGGATGAGATTGAC
CATGCTGAGATGGAGCTGCGCCGAGGCCAGATCCTCTGGTTCCGGGGCCTGAACCGTATC
CAGACTCAGATCAAAGTGGTCAAAGCGTTCCATAGTTCCCTCCACGAAAGCATTCAGAAA
CCCTACAACCAAAAGTCCATCCACAGCTTCATGACCCACCCTGAATTCGCCATAGAGGAG
GAGTTGCCACGAACACCACTCCTGGATGAGGAAGAGGAGGAAAATCCTGACAAGGCTTCT
AAGTTTGGGACTAGGGTGCTCCTGTTGGATGGTGAGGTCACTCCATATGCCAATACAAAC
AACAATGCGGTGGATTGCAACCAAGTGCAGCTCCCCCAGTCGGACAGCTCTCTACAGAGC
CTAGAGACATCAGTTTGA
Protein Properties
Number of Residues 1241
Molecular Weight 129401.755
Theoretical pI 7.511
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Plasma membrane calcium-transporting ATPase 4
MTNPSDRVLPANSMAESREGDFGCTVMELRKLMELRSRDALTQINVHYGGVQNLCSRLKT
SPVEGLSGNPADLEKRRQVFGHNVIPPKKPKTFLELVWEALQDVTLIILEIAAIISLVLS
FYRPAGEENELCGQVATTPEDENEAQAGWIEGAAILFSVIIVVLVTAFNDWSKEKQFRGL
QCRIEQEQKFSIIRNGQLIQLPVAEIVVGDIAQVKYGDLLPADGILIQGNDLKIDESSLT
GESDHVKKSLDKDPMLLSGTHVMEGSGRMVVTAVGVNSQTGIILTLLGVNEDDEGEKKKK
GKKQGVPENRNKAKTQDGVALEIQPLNSQEGIDNEEKDKKAVKVPKKEKSVLQGKLTRLA
VQIGKAGLLMSALTVFILILYFVIDNFVINRRPWLPECTPIYIQYFVKFFIIGITVLVVA
VPEGLPLAVTISLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTMNRMTVVQA
YIGGIHYRQIPSPDVFLPKVLDLIVNGISINSAYTSKILPPEKEGGLPRQVGNKTECALL
GFVTDLKQDYQAVRNEVPEEKLYKVYTFNSVRKSMSTVIRNPNGGFRMYSKGASEIILRK
CNRILDRKGEAVPFKNKDRDDMVRTVIEPMACDGLRTICIAYRDFDDTEPSWDNENEILT
ELTCIAVVGIEDPVRPEVPDAIAKCKQAGITVRMVTGDNINTARAIATKCGILTPGDDFL
CLEGKEFNRLIRNEKGEVEQEKLDKIWPKLRVLARSSPTDKHTLVKGIIDSTVGEHRQVV
AVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFTSIVKAVMWGRNVYDSI
SKFLQFQLTVNVVAVIVAFTGACITQDSPLKAVQMLWVNLIMDTFASLALATEPPTESLL
KRRPYGRNKPLISRTMMKNILGHAFYQLIVIFILVFAGEKFFDIDSGRKAPLHSPPSQHY
TIVFNTFVLMQLFNEINSRKIHGEKNVFSGIYRNIIFCSVVLGTFICQIFIVEFGGKPFS
CTSLSLSQWLWCLFIGIGELLWGQFISAIPTRSLKFLKEAGHGTTKEEITKDAEGLDEID
HAEMELRRGQILWFRGLNRIQTQIDVINTFQTGASFKGVLRRQNMGQHLDVKLVPSSSYI
KVVKAFHSSLHESIQKPYNQKSIHSFMTHPEFAIEEELPRTPLLDEEEEENPDKASKFGT
RVLLLDGEVTPYANTNNNAVDCNQVQLPQSDSSLQSLETSV
GenBank ID Protein 48255957
UniProtKB/Swiss-Prot ID P23634
UniProtKB/Swiss-Prot Entry Name AT2B4_HUMAN
PDB IDs
GenBank Gene ID AL513343
GeneCard ID ATP2B4
GenAtlas ID ATP2B4
HGNC ID HGNC:817
References
General References
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  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed:17974005 ]
  4. Stauffer TP, Hilfiker H, Carafoli E, Strehler EE: Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes. J Biol Chem. 1993 Dec 5;268(34):25993-6003. [PubMed:8245032 ]
  5. Stauffer TP, Hilfiker H, Carafoli E, Strehler EE: Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes. J Biol Chem. 1994 Dec 16;269(50):32022. [PubMed:7989379 ]
  6. Strehler EE, James P, Fischer R, Heim R, Vorherr T, Filoteo AG, Penniston JT, Carafoli E: Peptide sequence analysis and molecular cloning reveal two calcium pump isoforms in the human erythrocyte membrane. J Biol Chem. 1990 Feb 15;265(5):2835-42. [PubMed:2137451 ]
  7. Brandt P, Neve RL, Kammesheidt A, Rhoads RE, Vanaman TC: Analysis of the tissue-specific distribution of mRNAs encoding the plasma membrane calcium-pumping ATPases and characterization of an alternately spliced form of PMCA4 at the cDNA and genomic levels. J Biol Chem. 1992 Mar 5;267(7):4376-85. [PubMed:1531651 ]
  8. Santiago-Garcia J, Mas-Oliva J, Saavedra D, Zarain-Herzberg A: Analysis of mRNA expression and cloning of a novel plasma membrane Ca(2+)-ATPase splice variant in human heart. Mol Cell Biochem. 1996 Feb 23;155(2):173-82. [PubMed:8700162 ]
  9. James P, Maeda M, Fischer R, Verma AK, Krebs J, Penniston JT, Carafoli E: Identification and primary structure of a calmodulin binding domain of the Ca2+ pump of human erythrocytes. J Biol Chem. 1988 Feb 25;263(6):2905-10. [PubMed:2963820 ]
  10. Brandt P, Zurini M, Neve RL, Rhoads RE, Vanaman TC: A C-terminal, calmodulin-like regulatory domain from the plasma membrane Ca2+-pumping ATPase. Proc Natl Acad Sci U S A. 1988 May;85(9):2914-8. [PubMed:2966397 ]
  11. Elshorst B, Hennig M, Forsterling H, Diener A, Maurer M, Schulte P, Schwalbe H, Griesinger C, Krebs J, Schmid H, Vorherr T, Carafoli E: NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump. Biochemistry. 1999 Sep 21;38(38):12320-32. [PubMed:10493800 ]