Reviewed,
UniProtKB/Swiss-Prot Q16720 (AT2B3_HUMAN)
Last modified
July 22, 2008.
Version 83.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
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Names and origin
| Protein names | Recommended name: Plasma membrane calcium-transporting ATPase 3 Short name=PMCA3 EC=3.6.3.8 Alternative name(s): Plasma membrane calcium ATPase isoform 3 Plasma membrane calcium pump isoform 3 | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 1220 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell. |
| Catalytic activity | ATP + H(2)O + Ca(2+)(Cis) = ADP + phosphate + Ca(2+)(Trans). |
| Subcellular location | |
| Tissue specificity | Isoforms XE and XB are the most abundant isoforms and are detected at low levels in brain and fetal skeletal muscle. The other isoforms are only found at lower levels and not in fetal tissues. |
| Sequence similarities | Belongs to the cation transport ATPase (P-type) family. Type IIB subfamily. |
Ontologies
Keywords | |
|---|---|
| Biological process | Calcium transport Ion transport Transport |
| Cellular component | Cell membrane Membrane |
| Coding sequence diversity | Alternative splicing Polymorphism |
| Domain | Transmembrane |
| Ligand | ATP-binding Calcium Calmodulin-binding Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Hydrolase |
| PTM | Phosphoprotein |
Gene Ontology (GO) | |
| Biological process | transport Ref.1 Traceable author statement. Source: ProtInc |
| Cellular component | plasma membrane Ref.1 Traceable author statement. Source: ProtInc |
| Molecular function | calcium-transporting ATPase activity Ref.1 Traceable author statement. Source: ProtInc |
| Complete GO annotation... | |
Alternative products
| This entry describes 8 isoforms produced by alternative splicing. [Align] [Select] Notes: There is a combination of two alternatively spliced domains at N-terminal site A (X and Z) and at C-terminal site C (A, B, E and G). The splice sites have mostly been studied independently. Full isoforms so far detected are isoform XA and isoform XB. Experimental confirmation may be lacking for some isoforms. | |||||
| Isoform XB (identifier: Q16720-1) Also known as: AIICI; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | |||||
| Isoform XA (identifier: Q16720-2) Also known as: AIICII; The sequence of this isoform differs from the canonical sequence as follows: 1115-1220: IRVVKAFRSS...SPLHSVETSL → MEVVSTFKRS...AGNPGGESVP | |||||
| Isoform ZA (identifier: Q16720-3) Also known as: AICII; The sequence of this isoform differs from the canonical sequence as follows: 306-319: Missing. 1115-1220: IRVVKAFRSS...SPLHSVETSL → MEVVSTFKRS...AGNPGGESVP | |||||
| Isoform ZB (identifier: Q16720-4) Also known as: AICI; The sequence of this isoform differs from the canonical sequence as follows: 306-319: Missing. | |||||
| Isoform XE (identifier: Q16720-5) Also known as: AIICV; The sequence of this isoform differs from the canonical sequence as follows: 1115-1220: IRVVKAFRSS...SPLHSVETSL → MEVVSTFKRS...NPTSAAGSES | |||||
| Isoform ZE (identifier: Q16720-6) Also known as: AICV; The sequence of this isoform differs from the canonical sequence as follows: 306-319: Missing. 1115-1220: IRVVKAFRSS...SPLHSVETSL → MEVVSTFKRS...NPTSAAGSES | |||||
| Isoform XG (identifier: Q16720-7) Also known as: AIICVII; The sequence of this isoform differs from the canonical sequence as follows: 1115-1220: IRVVKAFRSS...SPLHSVETSL → VCWDGKKMLRTTEVG | |||||
| Isoform ZG (identifier: Q16720-8) Also known as: AICVII; The sequence of this isoform differs from the canonical sequence as follows: 306-319: Missing. 1115-1220: IRVVKAFRSS...SPLHSVETSL → VCWDGKKMLRTTEVG |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | ||||
Molecule processing | ||||||||
|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1220 | 1220 | Plasma membrane calcium-transporting ATPase 3 | |||||
Regions | ||||||||
| Topological domain | 1 – 97 | 97 | Cytoplasmic Potential | |||||
| Transmembrane | 98 – 118 | 21 | Potential | |||||
| Topological domain | 119 – 155 | 37 | Extracellular Potential | |||||
| Transmembrane | 156 – 176 | 21 | Potential | |||||
| Topological domain | 177 – 364 | 188 | Cytoplasmic Potential | |||||
| Transmembrane | 365 – 384 | 20 | Potential | |||||
| Topological domain | 385 – 417 | 33 | Extracellular Potential | |||||
| Transmembrane | 418 – 435 | 18 | Potential | |||||
| Topological domain | 436 – 849 | 414 | Cytoplasmic Potential | |||||
| Transmembrane | 850 – 869 | 20 | Potential | |||||
| Topological domain | 870 – 879 | 10 | Extracellular Potential | |||||
| Transmembrane | 880 – 900 | 21 | Potential | |||||
| Topological domain | 901 – 920 | 20 | Cytoplasmic Potential | |||||
| Transmembrane | 921 – 943 | 23 | Potential | |||||
| Topological domain | 944 – 961 | 18 | Extracellular Potential | |||||
| Transmembrane | 962 – 983 | 22 | Potential | |||||
| Topological domain | 984 – 1002 | 19 | Cytoplasmic Potential | |||||
| Transmembrane | 1003 – 1024 | 22 | Potential | |||||
| Topological domain | 1025 – 1034 | 10 | Extracellular Potential | |||||
| Transmembrane | 1035 – 1056 | 22 | Potential | |||||
| Topological domain | 1057 – 1220 | 164 | Cytoplasmic Potential | |||||
| Region | 1097 – 1114 | 18 | Calmodulin-binding subdomain A By similarity | |||||
| Region | 1115 – 1124 | 10 | Calmodulin-binding subdomain B By similarity | |||||
| Compositional bias | 297 – 300 | 4 | Poly-Glu | |||||
| Compositional bias | 1174 – 1179 | 6 | Poly-Pro | |||||
Sites | ||||||||
| Active site | 473 | 1 | 4-aspartylphosphate intermediate By similarity | |||||
| Metal binding | 794 | 1 | Magnesium By similarity | |||||
| Metal binding | 798 | 1 | Magnesium By similarity | |||||
Amino acid modifications | ||||||||
| Modified residue | 1113 | 1 | Phosphothreonine; by PKC By similarity | |||||
Natural variations | ||||||||
| Alternative sequence | 306 – 319 | 14 | Missing in isoform ZA, isoform ZB, isoform ZE and isoform ZG. | |||||
| Alternative sequence | 1115 – 1220 | 106 | IRVVK…VETSL → MEVVSTFKRSGSVQGAVRRR SSVLSQLHDVTNLSTPTHAI LSAANPTSAAGNPGGESVP in isoform XA and isoform ZA. | |||||
| Alternative sequence | 1115 – 1220 | 106 | IRVVK…VETSL → MEVVSTFKRSGSVQGAVRRR SSVLSQLHDVTNLSTPTHAI LSAANPTSAAGSES in isoform XE and isoform ZE. | |||||
| Alternative sequence | 1115 – 1220 | 106 | IRVVK…VETSL → VCWDGKKMLRTTEVG in isoform XG and isoform ZG. | |||||
| Natural variant | 198 | 1 | I → M: dbSNP rs2269409. | |||||
Experimental info | ||||||||
| Sequence conflict | 587 | 1 | I → V in AAB09762 and AAB38530. Ref.1 | |||||
| Sequence conflict | 654 | 1 | S → Y in AAB09762 and AAB38530. Ref.1 | |||||
Sequences
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References
| [1] | "Primary structure of human plasma membrane Ca(2+)-ATPase isoform 3." Brown B., Hilfiker H., Demarco S.J., Zacharias D.A., Greenwood T.M., Carafoli E., Strehler E.E. Biochim. Biophys. Acta 1283:10-13(1996) [PubMed: 8765088] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS XA AND XB). Tissue: Brain. |
| [2] | "Localization of two genes encoding plasma membrane Ca2+ ATPases isoforms 2 (ATP2B2) and 3 (ATP2B3) to human chromosomes 3p26-->p25 and Xq28, respectively." Wang M.G., Yi H., Hilfiker H., Carafoli E., Strehler E.E., McBride O.W. Cytogenet. Cell Genet. 67:41-45(1994) [PubMed: 8187550] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-319 (ISOFORM X). |
| [3] | "Comparative genome sequence analysis of the Bpa/Str region in mouse and man." Mallon A.-M., Platzer M., Bate R., Gloeckner G., Botcherby M.R.M., Nordsiek G., Strivens M.A., Kioschis P., Dangel A., Cunningham D., Straw R.N.A., Weston P., Gilbert M., Fernando S., Goodall K., Hunter G., Greystrong J.S., Clarke D. |

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