Reviewed,
UniProtKB/Swiss-Prot O54827 (AT10A_MOUSE)
Last modified
November 3, 2009.
Version 87.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Probable phospholipid-transporting ATPase VA EC=3.6.3.1 Alternative name(s): ATPase class V type 10A P-locus fat-associated ATPase | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 1508 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | ATP + H2O + phospholipid(In) = ADP + phosphate + phospholipid(Out). |
| Subcellular location | |
| Tissue specificity | Found in testis and in white adipose tissue. Also detected in fetal tissues. Ref.5 |
| Post-translational modification | Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.6 |
| Sequence similarities | Belongs to the cation transport ATPase (P-type) family. Type IV subfamily. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Membrane |
| Domain | Transmembrane |
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Hydrolase |
| PTM | Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | ATP biosynthetic process Inferred from electronic annotation. Source: InterPro phospholipid transportInferred from electronic annotation. Source: InterPro |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanismInferred from electronic annotation. Source: InterPro magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW phospholipid-translocating ATPase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1508 | 1508 | Probable phospholipid-transporting ATPase VA | PRO_0000046380 | |||||
Regions | |||||||||
| Topological domain | 1 – 79 | 79 | Cytoplasmic Potential | ||||||
| Transmembrane | 80 – 101 | 22 | Potential | ||||||
| Topological domain | 102 – 107 | 6 | Extracellular Potential | ||||||
| Transmembrane | 108 – 129 | 22 | Potential | ||||||
| Topological domain | 130 – 313 | 184 | Cytoplasmic Potential | ||||||
| Transmembrane | 314 – 335 | 22 | Potential | ||||||
| Topological domain | 336 – 366 | 31 | Extracellular Potential | ||||||
| Transmembrane | 367 – 388 | 22 | Potential | ||||||
| Topological domain | 389 – 1101 | 713 | Cytoplasmic Potential | ||||||
| Transmembrane | 1102 – 1122 | 21 | Potential | ||||||
| Topological domain | 1123 – 1134 | 12 | Extracellular Potential | ||||||
| Transmembrane | 1135 – 1154 | 20 | Potential | ||||||
| Topological domain | 1155 – 1184 | 30 | Cytoplasmic Potential | ||||||
| Transmembrane | 1185 – 1206 | 22 | Potential | ||||||
| Topological domain | 1207 – 1213 | 7 | Extracellular Potential | ||||||
| Transmembrane | 1214 – 1236 | 23 | Potential | ||||||
| Topological domain | 1237 – 1242 | 6 | Cytoplasmic Potential | ||||||
| Transmembrane | 1243 – 1263 | 21 | Potential | ||||||
| Topological domain | 1264 – 1281 | 18 | Extracellular Potential | ||||||
| Transmembrane | 1282 – 1306 | 25 | Potential | ||||||
| Topological domain | 1307 – 1508 | 202 | Cytoplasmic Potential | ||||||
| Compositional bias | 17 – 23 | 7 | Poly-Arg | ||||||
| Compositional bias | 471 – 474 | 4 | Poly-Glu | ||||||
Sites | |||||||||
| Active site | 431 | 1 | 4-aspartylphosphate intermediate By similarity | ||||||
| Metal binding | 1045 | 1 | Magnesium By similarity | ||||||
| Metal binding | 1049 | 1 | Magnesium By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 650 | 1 | Phosphoserine Ref.6 | ||||||
Experimental info | |||||||||
| Sequence conflict | 16 – 22 | 7 | WRRPRRR → KLAAAKK Ref.2 | ||||||
| Sequence conflict | 435 | 1 | T → L Ref.2 | ||||||
| Sequence conflict | 554 | 1 | I → V in AAM20894. Ref.3 | ||||||
| Sequence conflict | 687 | 1 | E → D in AAF09447. Ref.1 | ||||||
| Sequence conflict | 840 – 842 | 3 | CWL → TRP Ref.4 | ||||||
| Sequence conflict | 978 | 1 | T → A in AAM20894. Ref.3 | ||||||
| Sequence conflict | 1113 | 1 | F → S in AAF09447. Ref.1 | ||||||
| Sequence conflict | 1434 | 1 | T → S in AAF09447. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Differential expression of putative transbilayer amphipath transporters." Halleck M.S., Lawler J.F. Jr., Blackshaw S., Gao L., Nagarajan P., Hacker C., Pyle S., Newman J.T., Nakanishi Y., Ando H., Weinstock D., Williamson P.L., Schlegel R.A. Physiol. Genomics 1:139-150(1999) [PubMed: 11015572] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Teratocarcinoma. |
| [2] | "Multiple members of a third subfamily of P-type ATPases identified by genomic sequences and ESTs." Halleck M.S., Pradhan D., Blackman C.F., Berkes C., Williamson P.L., Schlegel R.A. Genome Res. 8:354-361(1998) [PubMed: 9548971] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-435. |
| [3] | "An aminophospholipid translocase associated with body fat and type 2 diabetes phenotypes." Dhar M., Hauser L., Johnson D. Obes. Res. 10:695-702(2002) [PubMed: 12105293] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 155-1508. |
| [4] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 840-1508. |
| [5] | "A novel ATPase on mouse chromosome 7 is a candidate gene for increased body fat." Dhar M., Webb L.S., Smith L., Hauser L., Johnson D., West D.B. Physiol. Genomics 4:93-100(2000) [PubMed: 11074018] [Abstract] Cited for: TISSUE SPECIFICITY. |
| [6] | "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-650, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AF156549 mRNA. Translation: AAF09447.1. AF011337 mRNA. Translation: AAC02902.1. AF372979 Genomic DNA. Translation: AAM20894.1. BC025643 mRNA. Translation: AAH25643.1. | |
| IPI | IPI00338618. |
| RefSeq | NP_033858.2. |
| UniGene | Mm.135129 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | O54827. |
PTM databases | |
| PhosphoSite | O54827. |
Proteomic databases | |
| PRIDE | O54827. |
Genome annotation databases | |
| Ensembl | ENSMUST00000055764; ENSMUSP00000055608; ENSMUSG00000025324; Mus musculus. [Genome view] |
| GeneID | 11982. |
| KEGG | mmu:11982. |
Organism-specific databases | |
| CTD | 11982. |
| MGI | MGI:1330809. Atp10a. |
Phylogenomic databases | |
| HOVERGEN | O54827. |
| OMA | KETFAQG. |
Enzyme and pathway databases | |
| BRENDA | 3.6.3.1. 244. |
Gene expression databases | |
| ArrayExpress | O54827. |
| Bgee | O54827. |
| CleanEx | MM_ATP10A. |
| Genevestigator | O54827. |
| GermOnline | ENSMUSG00000025324. Mus musculus. |
Family and domain databases | |
| InterPro | IPR008250. ATPase_P-typ_ATPase-assoc-reg. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR006539. ATPase_P-typ_Plipid-transl. IPR013200. HAD-SF_hydro-like_3. [Graphical view] |
| PANTHER | PTHR11939. ATPase_P. 1 hit. |
| Pfam | PF00122. E1-E2_ATPase. 1 hit. PF08282. Hydrolase_3. 1 hit. [Graphical view] |
| PRINTS | PR00119. CATATPASE. |
| TIGRFAMs | TIGR01652. ATPase-Plipid. 1 hit. TIGR01494. ATPase_P-type. 2 hits. |
| PROSITE | PS00154. ATPASE_E1_E2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 280129. |
| SOURCE | Search... |
Entry information
| Entry name | AT10A_MOUSE | ||||||||
| Accession | Primary (citable) accession number: O54827 Secondary accession number(s): Q8R3B8 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


