Reviewed,
UniProtKB/Swiss-Prot P49015 (ATP7A_CRIGR)
Last modified
November 25, 2008.
Version 67.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Copper-transporting ATPase 1 EC=3.6.3.4 Alternative name(s): Copper pump 1 | ||
| Gene names |
| ||
| Organism | Cricetulus griseus (Chinese hamster) | ||
| Taxonomic identifier | 10029 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus |
Protein attributes
| Sequence length | 1476 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | May function in the export of copper from the cytoplasm to an intracellular organelle. It may serve as well for the export of other metals. |
| Catalytic activity | ATP + H(2)O + Cu(2+)(In) = ADP + phosphate + Cu(2+)(Out). |
| Subunit structure | Monomer. |
| Subcellular location | |
| Tissue specificity | Expressed in most tissues except liver. |
| Sequence similarities | Belongs to the cation transport ATPase (P-type) family. Contains 6 HMA domains. |
Ontologies
Keywords | |
|---|---|
| Biological process | Copper transport Ion transport Transport |
| Cellular component | Membrane |
| Domain | Repeat Transmembrane |
| Ligand | ATP-binding Copper Metal-binding Nucleotide-binding |
| Molecular function | Hydrolase |
| PTM | Glycoprotein Phosphoprotein |
Gene Ontology (GO) | |
| Biological process | copper ion transport Inferred from electronic annotation. Source: InterPro metabolic processInferred from electronic annotation. Source: InterPro |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: InterPro |
| Molecular function | ATP binding Inferred from electronic annotation. Source: InterPro copper ion bindingInferred from electronic annotation. Source: InterPro copper-exporting ATPase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – ›1476 | ›1476 | Copper-transporting ATPase 1 | PRO_0000046310 | |||||
Regions | |||||||||
| Topological domain | 1 – 642 | 642 | Cytoplasmic Potential | ||||||
| Transmembrane | 643 – 665 | 23 | Potential | ||||||
| Transmembrane | 695 – 717 | 23 | Potential | ||||||
| Transmembrane | 736 – 760 | 25 | Potential | ||||||
| Transmembrane | 770 – 788 | 19 | Potential | ||||||
| Transmembrane | 930 – 952 | 23 | Potential | ||||||
| Transmembrane | 978 – 998 | 21 | Potential | ||||||
| Transmembrane | 1347 – 1373 | 27 | Potential | ||||||
| Transmembrane | 1379 – 1397 | 19 | Potential | ||||||
| Domain | 9 – 75 | 67 | HMA 1 | ||||||
| Domain | 172 – 238 | 67 | HMA 2 | ||||||
| Domain | 277 – 343 | 67 | HMA 3 | ||||||
| Domain | 377 – 443 | 67 | HMA 4 | ||||||
| Domain | 479 – 545 | 67 | HMA 5 | ||||||
| Domain | 555 – 621 | 67 | HMA 6 | ||||||
Sites | |||||||||
| Active site | 1034 | 1 | 4-aspartylphosphate intermediate Probable | ||||||
Amino acid modifications | |||||||||
| Modified residue | 352 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 355 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 356 | 1 | Phosphoserine By similarity | ||||||
| Glycosylation | 674 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 685 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 887 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 953 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1130 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1134 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1448 | 1 | N-linked (GlcNAc...) Potential | ||||||
Experimental info | |||||||||
| Non-terminal residue | 1476 | 1 | |||||||
Sequences
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References
| [1] | "Gene amplification of the Menkes (MNK; ATP7A) P-type ATPase gene of CHO cells is associated with copper resistance and enhanced copper efflux." Camakaris J., Petris M.J., Bailey L., Shen P., Lockhart P., Glover T.W., Barcroft C., Patton J., Mercer J.F.B. Hum. Mol. Genet. 4:2117-2123(1995) [PubMed: 8589689] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Ovary. |
Cross-references
Sequence databases | |
|---|---|
| U29946 mRNA. Translation: AAB39918.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1AW0 based on UniProtKB Q04656. |
| SMR | P49015. Positions 1-79, 164-246, 274-350, 374-445. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | P49015. |
Family and domain databases | |
| InterPro | IPR006416. ATPase-IB_hvy. IPR001757. ATPase_P. IPR006403. ATPase_P_cat/Cu. IPR001877. Cu_ATPase1. IPR006122. Cu_ion_bd. IPR005834. Dehalogen-like_hydro. IPR008250. E1-E2_ATPase_reg. IPR006121. HeavyMe_transpt. [Graphical view] |
| PANTHER | PTHR11939. ATPase_P. 1 hit. |
| Pfam | PF00122. E1-E2_ATPase. 1 hit. PF00403. HMA. 6 hits. PF00702. Hydrolase. 1 hit. [Graphical view] |
| PRINTS | PR00119. CATATPASE. PR00942. CUATPASEI. |
| TIGRFAMs | TIGR01511. ATPase-IB1_Cu. 1 hit. TIGR01525. ATPase-IB_hvy. 1 hit. TIGR01494. ATPase_P-type. 2 hits. TIGR00003. Cu_ion_bd. 2 hits. |
| PROSITE | PS00154. ATPASE_E1_E2. 1 hit. PS01047. HMA_1. 5 hits. PS50846. HMA_2. 6 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ATP7A_CRIGR | ||||||||
| Accession | Primary (citable) accession number: P49015 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Protein Spotlight Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


