| Identification |
|---|
| HMDB Protein ID
| HMDBP01200 |
| Secondary Accession Numbers
| |
| Name
| Plasma membrane calcium-transporting ATPase 1 |
| Synonyms
|
- PMCA1
- Plasma membrane calcium ATPase isoform 1
- Plasma membrane calcium pump isoform 1
|
| Gene Name
| ATP2B1 |
| 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
- Endocrine and other factor-regulated calcium reabsorption
- Mineral absorption
- Pancreatic secretion
- Salivary secretion
|
| Reactions
| Not Available |
| GO Classification
|
| Biological Process |
| ATP biosynthetic process |
| blood coagulation |
| 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
|
- Cell membrane
- Multi-pass membrane protein
|
| Gene Properties |
|---|
| Chromosome Location
| 12 |
| Locus
| 12q21.3 |
| SNPs
| ATP2B1 |
| Gene Sequence
|
>3663 bp
ATGGGCGACATGGCAAACAACTCAGTTGCTTACAGTGGTGTGAAAAACTCTTTGAAGGAA
GCTAATCATGATGGAGACTTTGGAATTACGCTCGCAGAGCTGCGGGCTCTCATGGAGCTC
AGGTCCACAGATGCATTACGAAAAATACAGGAAAGCTATGGAGATGTCTATGGAATTTGC
ACCAAATTGAAAACATCTCCCAATGAAGGTTTAAGTGGAAACCCTGCAGATTTAGAAAGA
AGAGAAGCAGTGTTTGGAAAGAATTTTATACCTCCTAAAAAGCCAAAAACCTTTCTTCAA
TTAGTATGGGAAGCATTACAAGATGTCACTTTAATTATATTAGAAATTGCAGCCATAGTA
TCATTGGGCCTTTCTTTTTATCAGCCTCCAGAAGGGGATAATGCACTTTGTGGAGAAGTT
TCTGTTGGGGAGGAAGAAGGTGAAGGTGAAACTGGTTGGATTGAAGGAGCTGCAATCCTC
TTGTCTGTAGTGTGTGTGGTGTTAGTAACAGCTTTCAATGACTGGAGTAAGGAAAAACAG
TTTAGAGGTTTGCAGAGCCGAATTGAACAAGAACAGAAGTTCACTGTCATCAGGGGTGGT
CAGGTCATTCAGATACCTGTAGCTGACATTACTGTTGGAGATATTGCTCAAGTGAAATAT
GGTGATCTTCTTCCAGCTGACGGCATACTTATTCAAGGCAACGATCTTAAAATTGATGAA
AGCTCATTGACTGGTGAATCAGATCATGTTAAAAAGTCTTTAGATAAGGATCCCTTACTT
CTATCAGGTACTCATGTAATGGAAGGCTCTGGAAGAATGGTAGTTACAGCTGTAGGTGTA
AATTCTCAAACTGGAATTATCTTTACCTTACTTGGAGCTGGAGGTGAAGAGGAAGAGAAG
AAAGATGAGAAGAAAAAGGAAAAGAAAAATAAGAAACAAGATGGAGCTATTGAGAATCGC
AACAAAGCAAAAGCCCAGGATGGTGCAGCCATGGAAATGCAGCCATTGAAGAGTGAAGAA
GGTGGAGATGGTGATGAAAAAGATAAAAAGAAAGCAAATTTGCCAAAAAAGGAAAAATCT
GTTTTACAAGGGAAACTTACAAAACTGGCTGTTCAGATTGGCAAAGCAGGTCTGTTGATG
TCTGCCATCACAGTTATCATTCTAGTATTATATTTTGTCATTGACACCTTCTGGGTTCAG
AAAAGACCATGGCTTGCTGAGTGCACACCAATTTATATACAATACTTTGTGAAGTTCTTC
ATTATTGGAGTTACAGTTTTAGTGGTCGCAGTGCCAGAAGGTCTTCCACTTGCAGTCACG
ATCTCACTGGCTTATTCAGTCAAAAAAATGATGAAAGATAATAACTTAGTAAGGCATCTG
GATGCTTGTGAAACCATGGGAAATGCTACAGCTATTTGTTCAGATAAAACAGGAACTTTG
ACAATGAACAGAATGACAGTCGTTCAAGCTTACATAAATGAAAAACATTATAAAAAGGTT
CCTGAACCAGAAGCTATTCCACCAAATATTTTGTCCTATCTTGTAACAGGAATTTCTGTG
AATTGTGCTTATACATCAAAAATATTGCCACCAGAGAAAGAGGGTGGATTACCTCGTCAC
GTTGGTAATAAAACTGAATGTGCCTTGTTGGGACTTCTTTTGGATTTAAAACGGGATTAT
CAGGATGTTAGAAATGAAATACCAGAAGAAGCACTGTACAAAGTCTACACCTTCAATTCT
GTTAGGAAGTCCATGAGTACTGTCCTGAAAAATTCAGATGGAAGTTATCGAATATTCAGC
AAGGGTGCATCTGAGATAATTCTGAAAAAGTGTTTCAAAATCTTGAGTGCTAATGGTGAG
GCAAAAGTATTCAGACCAAGGGACCGTGATGATATTGTAAAAACTGTGATTGAACCGATG
GCATCAGAAGGCTTGAGAACCATATGTCTTGCATTCAGAGATTTTCCAGCAGGAGAACCA
GAACCAGAGTGGGATAATGAAAATGATATTGTCACCGGCCTTACATGCATTGCTGTTGTG
GGGATTGAAGATCCTGTGAGACCTGAGGTGCCAGATGCAATTAAAAAGTGTCAGAGGGCT
GGAATTACTGTGCGGATGGTCACTGGTGATAATATTAATACTGCTCGGGCCATTGCTACC
AAATGTGGTATTTTACATCCTGGGGAAGATTTTCTGTGCCTAGAAGGTAAAGATTTTAAC
AGAAGAATACGAAATGAAAAAGGAGAGATTGAGCAAGAGAGGATAGACAAGATTTGGCCA
AAACTTCGAGTACTTGCAAGATCATCTCCTACTGATAAGCATACACTGGTTAAAGGTATA
ATTGACAGCACTGTCTCAGACCAACGCCAGGTTGTAGCTGTAACTGGTGATGGTACAAAT
GATGGCCCAGCACTAAAGAAAGCAGATGTTGGATTTGCAATGGGTATTGCTGGAACTGAT
GTAGCTAAAGAAGCATCCGATATTATTCTCACAGATGACAACTTTACAAGCATTGTTAAA
GCAGTTATGTGGGGACGAAATGTCTATGACAGCATCTCAAAATTCCTTCAGTTCCAACTT
ACTGTTAATGTAGTAGCAGTGATTGTTGCTTTTACGGGCGCCTGCATTACTCAAGACTCA
CCGCTTAAGGCTGTGCAGATGCTGTGGGTAAACCTCATAATGGATACACTCGCTTCCCTG
GCTCTGGCAACGGAACCACCCACTGAGTCTCTCTTGCTTCGGAAACCTTATGGTAGAAAT
AAGCCTCTCATCTCACGTACAATGATGAAGAATATTTTGGGTCATGCATTCTATCAACTT
GTAGTAGTCTTTACACTCTTATTTGCTGGAGAAAAGTTTTTTGACATTGATAGTGGAAGA
AATGCTCCTTTGCATGCTCCTCCTTCAGAACATTATACTATTGTTTTTAATACCTTTGTG
CTGATGCAACTTTTCAACGAAATAAATGCCCGGAAAATTCATGGTGAAAGAAATGTATTC
GAAGGAATCTTTAACAATGCCATCTTCTGCACAATTGTTTTAGGCACTTTTGTGGTACAG
ATAATAATTGTGCAGTTTGGTGGAAAACCTTTCAGTTGTTCAGAACTTTCAATAGAACAG
TGGCTATGGTCAATATTCCTAGGAATGGGAACATTACTCTGGGGCCAGCTTATTTCAACA
ATTCCAACTAGCCGTTTAAAATTCCTCAAAGAAGCTGGTCATGGAACACAAAAGGAAGAA
ATACCTGAGGAGGAATTAGCAGAGGATGTTGAAGAGATTGATCACGCTGAAAGGGAGTTG
CGGCGTGGCCAAATCTTGTGGTTTAGAGGTCTGAACAGAATCCAAACACAGATTCGAGTG
GTGAATGCATTTCGTAGTTCTTTATATGAAGGGTTAGAAAAACCGGAATCAAGAAGTTCG
ATTCACAACTTTATGACACATCCTGAGTTTAGGATAGAAGATTCAGAGCCTCATATCCCC
CTTATTGATGACACTGATGCCGAAGATGATGCTCCTACAAAACGTAACTCCAGTCCTCCA
CCCTCTCCCAACAAAAATAACAATGCTGTTGACAGTGGAATTCACCTTACAATAGAAATG
AACAAGTCTGCTACCTCTTCATCCCCAGGAAGCCCACTACATAGTTTGGAAACATCACTC
TGA
|
| Protein Properties |
|---|
| Number of Residues
| 1258 |
| Molecular Weight
| 129515.035 |
| Theoretical pI
| 6.166 |
| Pfam Domain Function
|
|
| Signals
|
Not Available
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
>Plasma membrane calcium-transporting ATPase 1
MGDMANNSVAYSGVKNSLKEANHDGDFGITLAELRALMELRSTDALRKIQESYGDVYGIC
TKLKTSPNEGLSGNPADLERREAVFGKNFIPPKKPKTFLQLVWEALQDVTLIILEIAAIV
SLGLSFYQPPEGDNALCGEVSVGEEEGEGETGWIEGAAILLSVVCVVLVTAFNDWSKEKQ
FRGLQSRIEQEQKFTVIRGGQVIQIPVADITVGDIAQVKYGDLLPADGILIQGNDLKIDE
SSLTGESDHVKKSLDKDPLLLSGTHVMEGSGRMVVTAVGVNSQTGIIFTLLGAGGEEEEK
KDEKKKEKKNKKQDGAIENRNKAKAQDGAAMEMQPLKSEEGGDGDEKDKKKANLPKKEKS
VLQGKLTKLAVQIGKAGLLMSAITVIILVLYFVIDTFWVQKRPWLAECTPIYIQYFVKFF
IIGVTVLVVAVPEGLPLAVTISLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTL
TMNRMTVVQAYINEKHYKKVPEPEAIPPNILSYLVTGISVNCAYTSKILPPEKEGGLPRH
VGNKTECALLGLLLDLKRDYQDVRNEIPEEALYKVYTFNSVRKSMSTVLKNSDGSYRIFS
KGASEIILKKCFKILSANGEAKVFRPRDRDDIVKTVIEPMASEGLRTICLAFRDFPAGEP
EPEWDNENDIVTGLTCIAVVGIEDPVRPEVPDAIKKCQRAGITVRMVTGDNINTARAIAT
KCGILHPGEDFLCLEGKDFNRRIRNEKGEIEQERIDKIWPKLRVLARSSPTDKHTLVKGI
IDSTVSDQRQVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFTSIVK
AVMWGRNVYDSISKFLQFQLTVNVVAVIVAFTGACITQDSPLKAVQMLWVNLIMDTLASL
ALATEPPTESLLLRKPYGRNKPLISRTMMKNILGHAFYQLVVVFTLLFAGEKFFDIDSGR
NAPLHAPPSEHYTIVFNTFVLMQLFNEINARKIHGERNVFEGIFNNAIFCTIVLGTFVVQ
IIIVQFGGKPFSCSELSIEQWLWSIFLGMGTLLWGQLISTIPTSRLKFLKEAGHGTQKEE
IPEEELAEDVEEIDHAERELRRGQILWFRGLNRIQTQMDVVNAFQSGSSIQGALRRQPSI
ASQHHDVTNISTPTHIRVVNAFRSSLYEGLEKPESRSSIHNFMTHPEFRIEDSEPHIPLI
DDTDAEDDAPTKRNSSPPPSPNKNNNAVDSGIHLTIEMNKSATSSSPGSPLHSLETSL
|
| External Links |
|---|
| GenBank ID Protein
| 48255945 |
| UniProtKB/Swiss-Prot ID
| P20020 |
| UniProtKB/Swiss-Prot Entry Name
| AT2B1_HUMAN |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| Not Available |
| GeneCard ID
| ATP2B1 |
| GenAtlas ID
| ATP2B1 |
| HGNC ID
| HGNC:814 |
| References |
|---|
| General References
| - Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
- 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 ]
- 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 ]
- 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 ]
- Verma AK, Filoteo AG, Stanford DR, Wieben ED, Penniston JT, Strehler EE, Fischer R, Heim R, Vogel G, Mathews S, et al.: Complete primary structure of a human plasma membrane Ca2+ pump. J Biol Chem. 1988 Oct 5;263(28):14152-9. [PubMed:2844759 ]
- Kumar R, Haugen JD, Penniston JT: Molecular cloning of a plasma membrane calcium pump from human osteoblasts. J Bone Miner Res. 1993 Apr;8(4):505-13. [PubMed:8386431 ]
- Hilfiker H, Strehler-Page MA, Stauffer TP, Carafoli E, Strehler EE: Structure of the gene encoding the human plasma membrane calcium pump isoform 1. J Biol Chem. 1993 Sep 15;268(26):19717-25. [PubMed:8396145 ]
- Strehler EE, Strehler-Page MA, Vogel G, Carafoli E: mRNAs for plasma membrane calcium pump isoforms differing in their regulatory domain are generated by alternative splicing that involves two internal donor sites in a single exon. Proc Natl Acad Sci U S A. 1989 Sep;86(18):6908-12. [PubMed:2528729 ]
- Kessler F, Falchetto R, Heim R, Meili R, Vorherr T, Strehler EE, Carafoli E: Study of calmodulin binding to the alternatively spliced C-terminal domain of the plasma membrane Ca2+ pump. Biochemistry. 1992 Dec 1;31(47):11785-92. [PubMed:1332771 ]
- Howard A, Legon S, Walters JR: Human and rat intestinal plasma membrane calcium pump isoforms. Am J Physiol. 1993 Nov;265(5 Pt 1):G917-25. [PubMed:7694502 ]
- James PH, Pruschy M, Vorherr TE, Penniston JT, Carafoli E: Primary structure of the cAMP-dependent phosphorylation site of the plasma membrane calcium pump. Biochemistry. 1989 May 16;28(10):4253-8. [PubMed:2548572 ]
- Wang KK, Wright LC, Machan CL, Allen BG, Conigrave AD, Roufogalis BD: Protein kinase C phosphorylates the carboxyl terminus of the plasma membrane Ca(2+)-ATPase from human erythrocytes. J Biol Chem. 1991 May 15;266(14):9078-85. [PubMed:1827443 ]
- Benkwitz C, Kubisch C, Kraft K, Neyses L: Investigation of the Met-267 Arg exchange in isoform 1 of the human plasma membrane calcium pump in patients with essential hypertension by the amplification-created restriction site technique. J Mol Med (Berl). 1997 Jan;75(1):62-6. [PubMed:9020386 ]
|
