Q9TV52 (AT12A_RABIT) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 89.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Potassium-transporting ATPase alpha chain 2 EC=3.6.3.10 Alternative name(s): HK alpha 2 Non-gastric H(+)/K(+) ATPase subunit alpha Proton pump | ||||
| Gene names |
| ||||
| Organism | Oryctolagus cuniculus (Rabbit) [Complete proteome] | ||||
| Taxonomic identifier | 9986 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus |
Protein attributes
| Sequence length | 1094 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Catalyzes the hydrolysis of ATP coupled with the exchange of H+ and K+ ions across the plasma membrane. Responsible for potassium absorption in various tissues. |
| Catalytic activity | ATP + H2O + H+(In) + K+(Out) = ADP + phosphate + H+(Out) + K+(In). |
| Subunit structure | Composed of two subunits: alpha (catalytic) and beta. |
| Subcellular location | |
| Tissue specificity | Found in the skin, kidney, distal colon and brain. In the kidney it is found in the connecting tubule, cortical collecting duct and outer medullary collecting duct while in the brain it is specific to choroid plexus and cortex. Ref.3 |
| Sequence similarities | Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily. [View classification] |
Ontologies
| Keywords | |
|---|---|
| Biological process | Hydrogen ion transport Ion transport Potassium transport Transport |
| Cellular component | Membrane |
| Coding sequence diversity | Alternative splicing |
| Domain | Transmembrane Transmembrane helix |
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding Potassium |
| Molecular function | Hydrolase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | ATP biosynthetic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW hydrogen:potassium-exchanging ATPase activityInferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform Long (identifier: Q9TV52-1) Also known as: 2c; 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 Short (identifier: Q9TV52-2) Also known as: 2a; The sequence of this isoform differs from the canonical sequence as follows: 1-63: MAGGAHRADRATGEERKEGGGRWRAPHSPSPPGPRGCPVPLKAAAQSLCRKPTWGRYCTLLLF → MR |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1094 | 1094 | Potassium-transporting ATPase alpha chain 2 | PRO_0000046262 | |||||
Regions | |||||||||
| Topological domain | 56 – 157 | 102 | Cytoplasmic Potential | ||||||
| Transmembrane | 158 – 178 | 21 | Helical; Potential | ||||||
| Topological domain | 179 – 201 | 23 | Lumenal Potential | ||||||
| Transmembrane | 202 – 222 | 21 | Helical; Potential | ||||||
| Topological domain | 223 – 358 | 136 | Cytoplasmic Potential | ||||||
| Transmembrane | 359 – 378 | 20 | Helical; Potential | ||||||
| Topological domain | 379 – 390 | 12 | Lumenal Potential | ||||||
| Transmembrane | 391 – 408 | 18 | Helical; Potential | ||||||
| Topological domain | 409 – 842 | 434 | Cytoplasmic Potential | ||||||
| Transmembrane | 843 – 862 | 20 | Helical; Potential | ||||||
| Topological domain | 863 – 872 | 10 | Lumenal Potential | ||||||
| Transmembrane | 873 – 893 | 21 | Helical; Potential | ||||||
| Topological domain | 894 – 913 | 20 | Cytoplasmic Potential | ||||||
| Transmembrane | 914 – 936 | 23 | Helical; Potential | ||||||
| Topological domain | 937 – 988 | 52 | Lumenal Potential | ||||||
| Transmembrane | 989 – 1008 | 20 | Helical; Potential | ||||||
| Topological domain | 1009 – 1022 | 14 | Cytoplasmic Potential | ||||||
| Transmembrane | 1023 – 1041 | 19 | Helical; Potential | ||||||
| Topological domain | 1042 – 1056 | 15 | Lumenal Potential | ||||||
| Transmembrane | 1057 – 1077 | 21 | Helical; Potential | ||||||
| Topological domain | 1078 – 1094 | 17 | Cytoplasmic Potential | ||||||
Sites | |||||||||
| Active site | 446 | 1 | 4-aspartylphosphate intermediate By similarity | ||||||
| Metal binding | 787 | 1 | Magnesium By similarity | ||||||
| Metal binding | 791 | 1 | Magnesium By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1013 | 1 | Phosphoserine; by PKA By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 63 | 63 | MAGGA…TLLLF → MR in isoform Short. | VSP_000413 | |||||
Experimental info | |||||||||
| Sequence conflict | 300 | 1 | G → E in AAD11800. Ref.2 | ||||||
| Sequence conflict | 421 | 1 | V → M in AAD11800. Ref.2 | ||||||
Sequences
| ||||||||||||||||||||||||
References
| [1] | "H-K-ATPase in the RCCT-28A rabbit cortical collecting duct cell line." Campbell W.G., Weiner I.D., Wingo C.S., Cain B.D. Am. J. Physiol. 276:F237-F245(1999) [PubMed: 9950954] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT). Strain: New Zealand white. Tissue: Kidney cortex. |
| [2] | "Intrarenal distribution of the colonic H,K-ATPase mRNA in rabbit." Fejes-Toth G., Naray-Fejes-Toth A., Velazquez H. Kidney Int. 56:1029-1036(1999) [PubMed: 10469371] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT). Tissue: Renal collecting duct. |
| [3] | "Ouabain-sensitive H,K-ATPase: tissue-specific expression of the mammalian genes encoding the catalytic alpha subunit." Pestov N.B., Romanova L.G., Korneenko T.V., Egorov M.V., Kostina M.B., Sverdlov V.E., Askari A., Shakhparonov M.I., Modyanov N.N. FEBS Lett. 440:320-324(1998) [PubMed: 9872395] [Abstract] Cited for: TISSUE SPECIFICITY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF023128 mRNA. Translation: AAB80941.1. AF023129 mRNA. Translation: AAC13887.1. AF106063 mRNA. Translation: AAD11800.1. |
| RefSeq | NP_001075496.1. NM_001082027.1. |
| UniGene | Ocu.2056. |
3D structure databases | |
| ProteinModelPortal | Q9TV52. |
| SMR | Q9TV52. Positions 97-1094. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q9TV52. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 100008669. |
Organism-specific databases | |
| CTD | 479. |
Phylogenomic databases | |
| GeneTree | ENSGT00560000076866. |
| HOVERGEN | HBG004298. |
| OrthoDB | EOG41C6VF. |
Family and domain databases | |
| InterPro | IPR023306. ATPase_cation_domN. IPR008250. ATPase_P-typ_ATPase-assoc-dom. IPR005775. ATPase_P-typ_cation-ex_asu_euk. IPR006069. ATPase_P-typ_cation-exchng_asu. IPR006068. ATPase_P-typ_cation-transptr_C. IPR004014. ATPase_P-typ_cation-transptr_N. IPR023300. ATPase_P-typ_cyto_domA. IPR023299. ATPase_P-typ_cyto_domN. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR023298. ATPase_P-typ_TM_dom. IPR005834. Dehalogen-like_hydro. IPR023214. HAD-like_dom. [Graphical view] |
| Gene3D | G3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 1 hit. G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit. G3DSA:1.20.1110.10. ATPase_P-typ_TM_dom. 2 hits. |
| Pfam | PF00689. Cation_ATPase_C. 1 hit. PF00690. Cation_ATPase_N. 1 hit. PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view] |
| PRINTS | PR00119. CATATPASE. PR00121. NAKATPASE. |
| SMART | SM00831. Cation_ATPase_N. 1 hit. [Graphical view] |
| SUPFAM | SSF81660. ATPase_cation_domN. 1 hit. SSF56784. HAD-like_dom. 1 hit. |
| TIGRFAMs | TIGR01106. ATPase-IIC_X-K. 1 hit. TIGR01494. ATPase_P-type. 2 hits. |
| PROSITE | PS00154. ATPASE_E1_E2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AT12A_RABIT | ||||||||
| Accession | Primary (citable) accession number: Q9TV52 Secondary accession number(s): Q9TSI2, Q9TV53 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with