Reviewed,
UniProtKB/Swiss-Prot P61023 (CHP1_RAT)
Last modified
January 19, 2010.
Version 58.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Calcium-binding protein p22 Alternative name(s): Calcium-binding protein CHP Calcineurin homologous protein | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 195 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Required for constitutive membrane traffic. Inhibits GTPase-stimulated Na+/H+ exchange. Also inhibits calcineurin phosphatase activity. Required for activity of SLC9A1/NHE1. |
| Subunit structure | Specifically binds to SLC9A1/NHE1 at a domain that is critical for growth factor stimulation of exchange activity By similarity. Monomer. Ref.4 |
| Subcellular location | |
| Tissue specificity | Ubiquitously expressed. |
| Post-translational modification | Both N-myristoylation and calcium-mediated conformational changes are essential for its function. |
| Sequence similarities | Contains 4 EF-hand domains. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Domain | Repeat |
| Ligand | Calcium Metal-binding |
| PTM | Lipoprotein Myristate |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological process | calcium ion-dependent exocytosis Ref.1 Inferred from direct assay. Source: RGD calcium-mediated signaling Ref.1Traceable author statement. Source: RGD transcytosis Ref.1Inferred from genetic interaction. Source: RGD |
| Cellular component | cytosol Ref.1 Inferred from direct assay. Source: RGD |
| Molecular function | calcium ion binding Ref.1 Inferred from direct assay. Source: RGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Probable | |||||||||||||||||||||||||||||||||||||
| Chain | 2 – 195 | 194 | Calcium-binding protein p22 | PRO_0000073846 | ||||||||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||||||||
| Domain | 26 – 61 | 36 | EF-hand 1 | |||||||||||||||||||||||||||||||||||||
| Domain | 71 – 106 | 36 | EF-hand 2 | |||||||||||||||||||||||||||||||||||||
| Domain | 110 – 145 | 36 | EF-hand 3 | |||||||||||||||||||||||||||||||||||||
| Domain | 151 – 186 | 36 | EF-hand 4 | |||||||||||||||||||||||||||||||||||||
| Calcium binding | 123 – 134 | 12 | 1 | |||||||||||||||||||||||||||||||||||||
| Calcium binding | 164 – 175 | 12 | 2 | |||||||||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||||||||||
| Lipidation | 2 | 1 | N-myristoyl glycine Probable | |||||||||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 134 | 1 | E → A: Loss of targeting/fusion function. | |||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||
| Helix | 4 – 7 | 4 | ||||||||||||||||||||||||||||||||||||||
| Helix | 11 – 21 | 11 | ||||||||||||||||||||||||||||||||||||||
| Helix | 25 – 38 | 14 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 43 – 46 | 4 | ||||||||||||||||||||||||||||||||||||||
| Helix | 49 – 53 | 5 | ||||||||||||||||||||||||||||||||||||||
| Helix | 55 – 58 | 4 | ||||||||||||||||||||||||||||||||||||||
| Helix | 63 – 68 | 6 | ||||||||||||||||||||||||||||||||||||||
| Helix | 80 – 88 | 9 | ||||||||||||||||||||||||||||||||||||||
| Helix | 111 – 122 | 12 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 127 – 130 | 4 | ||||||||||||||||||||||||||||||||||||||
| Helix | 132 – 142 | 11 | ||||||||||||||||||||||||||||||||||||||
| Helix | 149 – 163 | 15 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 165 – 172 | 8 | ||||||||||||||||||||||||||||||||||||||
| Helix | 173 – 178 | 6 | ||||||||||||||||||||||||||||||||||||||
| Turn | 179 – 182 | 4 | ||||||||||||||||||||||||||||||||||||||
| Helix | 185 – 187 | 3 | ||||||||||||||||||||||||||||||||||||||
| Helix | 189 – 195 | 7 | ||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "A novel Ca2+-binding protein, p22, is required for constitutive membrane traffic." Barroso M.R., Bernd K.K., Dewitt N.D., Chang A., Mills K., Sztul E.S. J. Biol. Chem. 271:10183-10187(1996) [PubMed: 8626580] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver. |
| [2] | "A serine/threonine kinase which causes apoptosis-like cell death interacts with a calcineurin B-like protein capable of binding Na+/H+ exchanger." Matsumoto M., Miyake Y., Nagita M., Inoue H., Shitakubo D., Takemoto K., Ohtsuka C., Murakami H., Nakamura N., Kanazawa H. J. Biochem. 130:217-225(2001) [PubMed: 11481038] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain. |
| [3] | "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]. Tissue: Prostate. |
| [4] | "Structural characterization of calcineurin B homologous protein 1." Naoe Y., Arita K., Hashimoto H., Kanazawa H., Sato M., Shimizu T. J. Biol. Chem. 280:32372-32378(2005) [PubMed: 15987692] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS, SUBUNIT. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | U39875 mRNA. Translation: AAB04146.1. AB070350 mRNA. Translation: BAB63369.1. BC062029 mRNA. Translation: AAH62029.1. | ||||||||||||
| IPI | IPI00394419. | ||||||||||||
| RefSeq | NP_077053.1. | ||||||||||||
| UniGene | Rn.11041 | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| STRING | P61023. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | P61023. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | P61023. | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSRNOT00000056405; ENSRNOP00000053243; ENSRNOG00000004742; Rattus norvegicus. [Genome view] | ||||||||||||
| GeneID | 64152. | ||||||||||||
| KEGG | rno:64152. | ||||||||||||
| UCSC | NM_024139. rat. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 64152. | ||||||||||||
| RGD | 620447. Chp. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | roNOG10716. | ||||||||||||
| HOVERGEN | P61023. | ||||||||||||
| OMA | REDFLRI. | ||||||||||||
| PhylomeDB | P61023. | ||||||||||||
Gene expression databases | |||||||||||||
| Genevestigator | P61023. | ||||||||||||
| GermOnline | ENSRNOG00000004742. Rattus norvegicus. ENSRNOG00000008946. Rattus norvegicus. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR011992. EF-hand-like_dom. IPR018247. EF_Hand_1_Ca_BS. IPR018249. EF_HAND_2. IPR002048. EF_hand_Ca_bd. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:1.10.238.10. EF-Hand_type. 1 hit. | ||||||||||||
| SMART | SM00054. EFh. 2 hits. [Graphical view] | ||||||||||||
| PROSITE | PS00018. EF_HAND_1. 1 hit. PS50222. EF_HAND_2. 3 hits. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other Resources | |||||||||||||
| NextBio | 612777. | ||||||||||||
Entry information
| Entry name | CHP1_RAT | ||||||||
| Accession | Primary (citable) accession number: P61023 Secondary accession number(s): Q62877 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


