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Entry version 176 (08 May 2019)
Sequence version 1 (01 Aug 1991)
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Protein

Voltage-dependent L-type calcium channel subunit alpha-1C

Gene

Cacna1c

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents (Probable) (PubMed:15140941, PubMed:15170217). Mediates influx of calcium ions into the cytoplasm, and thereby triggers calcium release from the sarcoplasm (By similarity). Plays an important role in excitation-contraction coupling in the heart (By similarity). Required for normal heart development and normal regulation of heart rhythm (By similarity). Required for normal contraction of smooth muscle cells in blood vessels and in the intestine. Essential for normal blood pressure regulation via its role in the contraction of arterial smooth muscle cells (By similarity). Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group (By similarity).By similarity1 Publication2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by dihydropyridines (DHP), such as isradipine (By similarity). Inhibited by nifedipine (By similarity). Channel activity is regulated by Ca2+ and calmodulin (PubMed:15140941). Binding of STAC1, STAC2 or STAC3 to a region that overlaps with the calmodulin binding site inhibits channel inactivation by Ca2+ and calmodulin (By similarity). Binding of calmodulin or CABP1 at the same regulatory sites results in opposite effects on the channel function (PubMed:15140941). Shear stress and pressure increases calcium channel activity (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi393CalciumBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei393Calcium ion selectivity and permeabilityBy similarity1
Metal bindingi736CalciumBy similarity1
Sitei736Calcium ion selectivity and permeabilityBy similarity1
Metal bindingi1144CalciumBy similarity1
Sitei1144Calcium ion selectivity and permeabilityBy similarity1
Sitei1445Calcium ion selectivity and permeabilityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) of the calcium-binding region(s) within the protein. One common calcium-binding motif is the EF-hand, but other calcium-binding motifs also exist.<p><a href='/help/ca_bind' target='_top'>More...</a></p>Calcium bindingi1534 – 1545By similarityAdd BLAST12

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionCalcium channel, Calmodulin-binding, Ion channel, Voltage-gated channel
Biological processCalcium transport, Ion transport, Transport
LigandCalcium, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-422356 Regulation of insulin secretion
R-RNO-5576892 Phase 0 - rapid depolarisation
R-RNO-5576893 Phase 2 - plateau phase

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Voltage-dependent L-type calcium channel subunit alpha-1C
Alternative name(s):
Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle
Rat brain class C1 Publication
Short name:
RBC1 Publication
Voltage-gated calcium channel subunit alpha Cav1.2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Cacna1c
Synonyms:Cach2, Cacn2, Cacnl1a1, Cchl1a1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
2245 Cacna1c

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 154CytoplasmicCuratedAdd BLAST154
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei155 – 173Helical; Name=S1 of repeat IBy similarityAdd BLAST19
Topological domaini174 – 188ExtracellularCuratedAdd BLAST15
Transmembranei189 – 209Helical; Name=S2 of repeat IBy similarityAdd BLAST21
Topological domaini210 – 218CytoplasmicCurated9
Transmembranei219 – 239Helical; Name=S3 of repeat IBy similarityAdd BLAST21
Topological domaini240 – 262ExtracellularCuratedAdd BLAST23
Transmembranei263 – 281Helical; Name=S4 of repeat IBy similarityAdd BLAST19
Topological domaini282 – 298CytoplasmicCuratedAdd BLAST17
Transmembranei299 – 320Helical; Name=S5 of repeat IBy similarityAdd BLAST22
Topological domaini321 – 380ExtracellularCuratedAdd BLAST60
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei381 – 402Pore-formingBy similarityAdd BLAST22
Topological domaini403 – 410ExtracellularCurated8
Transmembranei411 – 431Helical; Name=S6 of repeat IBy similarityAdd BLAST21
Topological domaini432 – 554CytoplasmicCuratedAdd BLAST123
Transmembranei555 – 573Helical; Name=S1 of repeat IIBy similarityAdd BLAST19
Topological domaini574 – 584ExtracellularCuratedAdd BLAST11
Transmembranei585 – 605Helical; Name=S2 of repeat IIBy similarityAdd BLAST21
Topological domaini606 – 616CytoplasmicCuratedAdd BLAST11
Transmembranei617 – 636Helical; Name=S3 of repeat IIBy similarityAdd BLAST20
Topological domaini637 – 645ExtracellularCurated9
Transmembranei646 – 664Helical; Name=S4 of repeat IIBy similarityAdd BLAST19
Topological domaini665 – 683CytoplasmicCuratedAdd BLAST19
Transmembranei684 – 703Helical; Name=S5 of repeat IIBy similarityAdd BLAST20
Topological domaini704 – 723ExtracellularCuratedAdd BLAST20
Intramembranei724 – 745Pore-formingBy similarityAdd BLAST22
Topological domaini746 – 755ExtracellularCurated10
Transmembranei756 – 775Helical; Name=S6 of repeat IIBy similarityAdd BLAST20
Topological domaini776 – 930CytoplasmicCuratedAdd BLAST155
Transmembranei931 – 949Helical; Name=S1 of repeat IIIBy similarityAdd BLAST19
Topological domaini950 – 961ExtracellularCuratedAdd BLAST12
Transmembranei962 – 981Helical; Name=S2 of repeat IIIBy similarityAdd BLAST20
Topological domaini982 – 997CytoplasmicCuratedAdd BLAST16
Transmembranei998 – 1016Helical; Name=S3 of repeat IIIBy similarityAdd BLAST19
Topological domaini1017 – 1023ExtracellularCurated7
Transmembranei1024 – 1041Helical; Name=S4 of repeat IIIBy similarityAdd BLAST18
Topological domaini1042 – 1060CytoplasmicCuratedAdd BLAST19
Transmembranei1061 – 1080Helical; Name=S5 of repeat IIIBy similarityAdd BLAST20
Topological domaini1081 – 1130ExtracellularCuratedAdd BLAST50
Intramembranei1131 – 1151Pore-formingBy similarityAdd BLAST21
Topological domaini1152 – 1168ExtracellularCuratedAdd BLAST17
Transmembranei1169 – 1190Helical; Name=S6 of repeat IIIBy similarityAdd BLAST22
Topological domaini1191 – 1248CytoplasmicCuratedAdd BLAST58
Transmembranei1249 – 1270Helical; Name=S1 of repeat IVBy similarityAdd BLAST22
Topological domaini1271 – 1278ExtracellularCurated8
Transmembranei1279 – 1300Helical; Name=S2 of repeat IVBy similarityAdd BLAST22
Topological domaini1301 – 1310CytoplasmicCurated10
Transmembranei1311 – 1330Helical; Name=S3 of repeat IVBy similarityAdd BLAST20
Topological domaini1331 – 1353ExtracellularCuratedAdd BLAST23
Transmembranei1354 – 1372Helical; Name=S4 of repeat IVBy similarityAdd BLAST19
Topological domaini1373 – 1390CytoplasmicCuratedAdd BLAST18
Transmembranei1391 – 1411Helical; Name=S5 of repeat IVBy similarityAdd BLAST21
Topological domaini1412 – 1433ExtracellularCuratedAdd BLAST22
Intramembranei1434 – 1452Pore-formingBy similarityAdd BLAST19
Topological domaini1453 – 1480ExtracellularCuratedAdd BLAST28
Transmembranei1481 – 1505Helical; Name=S6 of repeat IVBy similarityAdd BLAST25
Topological domaini1506 – 2169CytoplasmicCuratedAdd BLAST664

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane, Postsynaptic cell membrane, Synapse

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3762

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
529

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000539311 – 2169Voltage-dependent L-type calcium channel subunit alpha-1CAdd BLAST2169

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi183N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi328 ↔ 356By similarity
Disulfide bondi346 ↔ 362By similarity
Glycosylationi358N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei499PhosphoserineBy similarity1
Modified residuei506PhosphothreonineBy similarity1
Modified residuei838PhosphoserineBy similarity1
Modified residuei845PhosphoserineCombined sources1
Glycosylationi1417N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1460 ↔ 1476By similarity
Glycosylationi1468N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei1516Phosphoserine; by PKASequence analysis1
Modified residuei1699PhosphoserineCombined sources1
Modified residuei1720PhosphoserineCombined sources1
Modified residuei1919Phosphoserine; by PKASequence analysis1
Modified residuei1927Phosphoserine; by PKABy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation by PKA activates the channel (By similarity). Elevated levels of blood glucose lead to increased phosphorylation by PKA (By similarity). Is also phosphorylated in vitro by CaM-kinase II, PKC and CGPK (PubMed:8396138).By similarity1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P22002

PRoteomics IDEntifications database

More...
PRIDEi
P22002

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P22002

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P22002

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in hippocampus and brain cortex, on neuronal cell bodies and dendrites, and in post-synaptic density in brain (at protein level) (PubMed:15140941). Isoforms 4 and 5 are expressed throughout the central nervous system, with highest levels in the olfactory bulb and cerebellum. Also expressed in heart, pituitary, adrenal gland, liver, kidney, and in a much lesser extent in testes and spleen.1 Publication

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed from embryonic day 16 until the adult stage.

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of a calcium channel complex consisting of a pore-forming alpha subunit (CACNA1C) and ancillary beta, gamma and delta subunits (PubMed:15170217). The channel complex contains alpha, beta, gamma and delta subunits in a 1:1:1:1 ratio, i.e. it contains only one of each type of subunit. CACNA1C channel activity is modulated by ancillary subunits, such as CACNB1, CACNB2, CACNB3, CACNA2D1 and CACNA2D4 (By similarity). Intereracts with the gamma subunits CACNG4, CACNG6, CACNG7 and CACNG8 (By similarity).

Interacts with CACNB1 (By similarity).

Interacts with CACNB2.

Identified in a complex with CACNA2D4 and CACNB3 (By similarity).

Interacts with CACNB3 (PubMed:24751537, PubMed:15170217).

Interacts with CACNA2D1.

Interacts with CACNA2D4.

Interacts with CALM1.

Interacts (via the N-terminus and the C-terminal C and IQ motifs) with CABP1; this inhibits Ca2+-dependent channel inactivation (PubMed:15140941). The binding via the C motif is calcium independent whereas the binding via IQ requires the presence of calcium and is mutually exclusive with calmodulin binding (PubMed:15140941). The binding to the cytoplasmic N-terminal domain is calcium independent but is essential for the channel modulation.

Interacts (via C-terminal CDB motif) with CABP5; in a calcium-dependent manner.

Interacts with CIB1; the interaction increases upon cardiomyocytes hypertrophy (By similarity).

Interacts with STAC2 and STAC3; this inhibits channel inactivation (By similarity).

By similarity3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
246425, 4 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P22002

Protein interaction database and analysis system

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IntActi
P22002, 4 interactors

Molecular INTeraction database

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MINTi
P22002

STRING: functional protein association networks

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STRINGi
10116.ENSRNOP00000009268

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P22002

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

12169
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P22002

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P22002

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati141 – 438IAdd BLAST298
Repeati540 – 786IIAdd BLAST247
Repeati917 – 1198IIIAdd BLAST282
Repeati1235 – 1508IVAdd BLAST274

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni77 – 98Calmodulin-bindingBy similarityAdd BLAST22
Regioni458 – 475AID/alpha-interaction domain; mediates interaction with the beta subunit1 PublicationAdd BLAST18
Regioni859 – 906Interaction with STAC2By similarityAdd BLAST48
Regioni1118 – 1207Dihydropyridine bindingBy similarityAdd BLAST90
Regioni1459 – 1527Dihydropyridine bindingBy similarityAdd BLAST69
Regioni1473 – 1515Phenylalkylamine bindingBy similarityAdd BLAST43
Regioni1640 – 1673Calmodulin-bindingBy similarityAdd BLAST34
Regioni1640 – 1667Important for interaction with STAC1, STAC2 and STAC3By similarityAdd BLAST28
Regioni1646 – 1666Calmodulin-binding IQ regionBy similarityAdd BLAST21
Regioni1680 – 1699Important for localization in at the junctional membraneBy similarityAdd BLAST20

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi391 – 394Selectivity filter of repeat IBy similarity4
Motifi734 – 737Selectivity filter of repeat IIBy similarity4
Motifi1142 – 1145Selectivity filter of repeat IIIBy similarity4
Motifi1443 – 1446Selectivity filter of repeat IVBy similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi684 – 690Poly-Leu7
Compositional biasi798 – 804Poly-Glu7
Compositional biasi1176 – 1182Poly-Ile7

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Each of the four internal repeats contains five hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one positively charged transmembrane segment (S4). S4 segments probably represent the voltage-sensor and are characterized by a series of positively charged amino acids at every third position.
Binding of intracellular calcium through the EF-hand motif inhibits the opening of the channel.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG2301 Eukaryota
ENOG410XNP6 LUCA

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P22002

KEGG Orthology (KO)

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KOi
K04850

Database of Orthologous Groups

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OrthoDBi
172471at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P22002

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.20.120.350, 4 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR031688 CAC1F_C
IPR031649 GPHH_dom
IPR005821 Ion_trans_dom
IPR014873 VDCC_a1su_IQ
IPR005451 VDCC_L_a1csu
IPR005446 VDCC_L_a1su
IPR002077 VDCCAlpha1
IPR027359 Volt_channel_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF08763 Ca_chan_IQ, 1 hit
PF16885 CAC1F_C, 1 hit
PF16905 GPHH, 1 hit
PF00520 Ion_trans, 4 hits

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00167 CACHANNEL
PR01630 LVDCCALPHA1
PR01635 LVDCCALPHA1C

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01062 Ca_chan_IQ, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (5+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 5 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Note: Additional isoforms seem to exist.

This entry has 5 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 2 (identifier: P22002-1) [UniParc]FASTAAdd to basket
Also known as: S3B

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MIRAFAQPST PPYQPLSSCL SEDTERKFKG KVVHEAQLNC FYISPGGSNY
60 70 80 90 100
GSPRPAHANM NANAAAGLAP EHIPTPGAAL SWLAAIDAAR QAKLMGSAGN
110 120 130 140 150
ATISTVSSTQ RKRQQYGKPK KQGGTTATRP PRALLCLTLK NPIRRACISI
160 170 180 190 200
VEWKPFEIII LLTIFANCVA LAIYIPFPED DSNATNSNLE RVEYLFLIIF
210 220 230 240 250
TVEAFLKVIA YGLLFHPNAY LRNGWNLLDF IIVVVGLFSA ILEQATKADG
260 270 280 290 300
ANALGGKGAG FDVKALRAFR VLRPLRLVSG VPSLQVVLNS IIKAMVPLLH
310 320 330 340 350
IALLVLFVII IYAIIGLELF MGKMHKTCYN QEGIIDVPAE EDPSPCALET
360 370 380 390 400
GHGRQCQNGT VCKPGWDGPK HGITNFDNFA FAMLTVFQCI TMEGWTDVLY
410 420 430 440 450
WMQDAMGYEL PWVYFVSLVI FGSFFVLNLV LGVLSGEFSK EREKAKARGD
460 470 480 490 500
FQKLREKQQL EEDLKGYLDW ITQAEDIDPE NEDEGMDEDK PRNMSMPTSE
510 520 530 540 550
TESVNTENVA GGDIEGENCG ARLAHRISKS KFSRYWRRWN RFCRRKCRAA
560 570 580 590 600
VKSNVFYWLV IFLVFLNTLT IASEHYNQPH WLTEVQDTAN KALLALFTAE
610 620 630 640 650
MLLKMYSLGL QAYFVSLFNR FDCFIVCGGI LETILVETKI MSPLGISCWR
660 670 680 690 700
CVRLLRIFKI TRYWNSLSNL VASLLNSLRS IASLLLLLFL FIIIFSLLGM
710 720 730 740 750
QLFGGKFNFD EMQTRRSTFD NFPQSLLTVF QILTGEDWNS VMYDGIMAYG
760 770 780 790 800
GPSFPGMLVC IYFIILFISP NYILLNLFLA IAVDNLADAE SLTSAQKEEE
810 820 830 840 850
EEKERKKLAR TASPEKKQEV MEKPAVEESK EEKIELKSIT ADGESPPTTK
860 870 880 890 900
INMDDLQPSE NEDKSPHSNP DTAGEEDEEE PEMPVGPRPR PLSELHLKEK
910 920 930 940 950
AVPMPEASAF FIFSPNNRFR LQCHRIVNDT IFTNLILFFI LLSSISLAAE
960 970 980 990 1000
DPVQHTSFRN HILFYFDIVF TTIFTIEIAL KMTAYGAFLH KGSFCRNYFN
1010 1020 1030 1040 1050
ILDLLVVSVS LISFGIQSSA INVVKILRVL RVLRPLRINR AKGLKHVVQC
1060 1070 1080 1090 1100
VFVAIRTIGN IVIVTTLLQF MFACIGVQLF KGKLYTCSDS SKQTEAESKG
1110 1120 1130 1140 1150
NYITYKTGEV DHPIIQPRSW ENSKFDFDNV LAAMMALFTV STFEGWPELL
1160 1170 1180 1190 1200
YRSIDSHTED KGPIYNYRVE ISIFFIIYII IIAFFMMNIF VGFVIVTFQE
1210 1220 1230 1240 1250
QGEQEYKNCE LDKNQRQCVE YALKARPLPR YIPKNQHQYK VWYVVNSTYF
1260 1270 1280 1290 1300
EYLMFVLILL NTICLAMQHY GQSCLFKIAM NILNMLFTGL FTVEMILKLI
1310 1320 1330 1340 1350
AFKPKHYFCD AWNTFDALIV VGSIVDIAIT EVHPAEHTQC SPSMSAEENS
1360 1370 1380 1390 1400
RISITFFRLF RVMRLVKLLS RGEGIRTLLW TFIKSFQALP YVALLIVMLF
1410 1420 1430 1440 1450
FIYAVIGMQV FGKIALNDTT EINRNNNFQT FPQAVLLLFR CATGEAWQDI
1460 1470 1480 1490 1500
MLACMPGKKC APESEPSNST EGETPCGSSF AVFYFISFYM LCAFLIINLF
1510 1520 1530 1540 1550
VAVIMDNFDY LTRDWSILGP HHLDEFKRIW AEYDPEAKGR IKHLDVVTLL
1560 1570 1580 1590 1600
RRIQPPLGFG KLCPHRVACK RLVSMNMPLN SDGTVMFNAT LFALVRTALR
1610 1620 1630 1640 1650
IKTEGNLEQA NEELRAIIKK IWKRTSMKLL DQVVPPAGDD EVTVGKFYAT
1660 1670 1680 1690 1700
FLIQEYFRKF KKRKEQGLVG KPSQRNALSL QAGLRTLHDI GPEIRRAISG
1710 1720 1730 1740 1750
DLTAEEELDK AMKEAVSAAS EDDIFRRAGG LFGNHVSYYQ SDSRSNFPQT
1760 1770 1780 1790 1800
FATQRPLHIN KTGNNQADTE SPSHEKLVDS TFTPSSYSST GSNANINNAN
1810 1820 1830 1840 1850
NTALGRFPHP AGYSSTVSTV EGHGPPLSPA VRVQEAAWKL SSKRCHSRES
1860 1870 1880 1890 1900
QGATVSQDMF PDETRSSVRL SEEVEYCSEP SLLSTDILSY QDDENRQLTC
1910 1920 1930 1940 1950
LEEDKREIQP CPKRSFLRSA SLGRRASFHL ECLKRQKDQG GDISQKTALP
1960 1970 1980 1990 2000
LHLVHHQALA VAGLSPLLQR SHSPSTFPRP RPTPPVTPGS RGRPLQPIPT
2010 2020 2030 2040 2050
LRLEGAESSE KLNSSFPSIH CSSWSEETTA CSGGSSMARR ARPVSLTVPS
2060 2070 2080 2090 2100
QAGAPGRQFH GSASSLVEAV LISEGLGQFA QDPKFIEVTT QELADACDMT
2110 2120 2130 2140 2150
IEEMENAADN ILSGGAQQSP NGTLLPFVNC RDPGQDRAVV PEDESCVYAL
2160
GRGRSEEALP DSRSYVSNL
Length:2,169
Mass (Da):243,482
Last modified:August 1, 1991 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD3ADBD20E4763B69
GO
Isoform 1 (identifier: P22002-2) [UniParc]FASTAAdd to basket
Also known as: S3A

The sequence of this isoform differs from the canonical sequence as follows:
     1306-1333: HYFCDAWNTFDALIVVGSIVDIAITEVH → GYFSDPSNVFDFLIVIGSIIAVILSETN

Show »
Length:2,169
Mass (Da):243,364
Checksum:i1539479E670D0D2A
GO
Isoform 3 (identifier: P22002-3) [UniParc]FASTAAdd to basket
Also known as: D1, ROB2

The sequence of this isoform differs from the canonical sequence as follows:
     1334-1344: Missing.

Show »
Length:2,158
Mass (Da):242,313
Checksum:i498718087DA7DC10
GO
Isoform 4 (identifier: P22002-4) [UniParc]FASTAAdd to basket
Also known as: rbC-I

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: MIRAFAQPSTPPYQPLSSCLSEDTERKFKGKVVHEAQLNCFYISPG → MVNENTRMYVPEENHQ
     964-979: FYFDIVFTTIFTIEIA → GNADYVFTSIFTLEII
     1306-1333: HYFCDAWNTFDALIVVGSIVDIAITEVH → GYFSDPSNVFDFLIVIGSIIAVILSETN

Show »
Length:2,139
Mass (Da):240,045
Checksum:i8A3C3354E8BDB60D
GO
Isoform 5 (identifier: P22002-5) [UniParc]FASTAAdd to basket
Also known as: rbC-II

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: MIRAFAQPSTPPYQPLSSCLSEDTERKFKGKVVHEAQLNCFYISPG → MVNENTRMYVPEENHQ
     810-810: R → RPAR
     964-979: FYFDIVFTTIFTIEIA → GNADYVFTSIFTLEII

Show »
Length:2,142
Mass (Da):240,488
Checksum:i4207AD0217F19CB2
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2QC25A0A0G2QC25_RAT
Voltage-dependent L-type calcium ch...
Cacna1c
2,006Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F1MA84F1MA84_RAT
Voltage-dependent L-type calcium ch...
Cacna1c
1,981Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PT56E9PT56_RAT
Voltage-dependent L-type calcium ch...
Cacna1c
1,901Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti83L → Q in AAA18905 (PubMed:1648941).Curated1
Sequence conflicti83L → Q in AAA42016 (PubMed:1648941).Curated1
Sequence conflicti87D → G in AAA18905 (PubMed:1648941).Curated1
Sequence conflicti520G → R in AAA18905 (PubMed:1648941).Curated1
Sequence conflicti648 – 649CW → VL in AAA18905 (PubMed:1648941).Curated2
Sequence conflicti648 – 649CW → VL in AAA42016 (PubMed:1648941).Curated2
Sequence conflicti678L → V in AAA18905 (PubMed:1648941).Curated1
Sequence conflicti678L → V in AAA42016 (PubMed:1648941).Curated1
Sequence conflicti769 – 770SP → CG in AAA18905 (PubMed:1648941).Curated2
Sequence conflicti769 – 770SP → CG in AAA42016 (PubMed:1648941).Curated2
Sequence conflicti777L → V in AAA18905 (PubMed:1648941).Curated1
Sequence conflicti777L → V in AAA42016 (PubMed:1648941).Curated1
Sequence conflicti871D → N in AAA18905 (PubMed:1648941).Curated1
Sequence conflicti1037R → RA in AAA18905 (PubMed:1648941).Curated1
Sequence conflicti1037R → RA in AAA42016 (PubMed:1648941).Curated1
Sequence conflicti1098S → C in AAA18905 (PubMed:1648941).Curated1
Sequence conflicti1098S → C in AAA42016 (PubMed:1648941).Curated1
Sequence conflicti1107T → D in AAA18905 (PubMed:1648941).Curated1
Sequence conflicti1107T → D in AAA42016 (PubMed:1648941).Curated1
Sequence conflicti1229P → R in AAA18905 (PubMed:1648941).Curated1
Sequence conflicti1229P → R in AAA42016 (PubMed:1648941).Curated1
Sequence conflicti1229P → R no nucleotide entry (PubMed:1692134).Curated1
Sequence conflicti1229P → R in AAA89157 (PubMed:7479909).Curated1
Sequence conflicti1306H → D in AAB35528 (PubMed:7485440).Curated1
Sequence conflicti1306H → G in AAA42016 (PubMed:1648941).Curated1
Sequence conflicti1306H → G in AAA89157 (PubMed:7479909).Curated1
Sequence conflicti1329I → L in AAB35528 (PubMed:7485440).Curated1
Sequence conflicti1471E → K in AAA18905 (PubMed:1648941).Curated1
Sequence conflicti1911C → S in AAA18905 (PubMed:1648941).Curated1
Sequence conflicti1911C → S in AAA42016 (PubMed:1648941).Curated1
Sequence conflicti2084K → N in AAA18905 (PubMed:1648941).Curated1
Sequence conflicti2154R → Q in AAA42016 (PubMed:1648941).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0009081 – 46MIRAF…YISPG → MVNENTRMYVPEENHQ in isoform 4 and isoform 5. 1 PublicationAdd BLAST46
Alternative sequenceiVSP_000909810R → RPAR in isoform 5. 1 Publication1
Alternative sequenceiVSP_000910964 – 979FYFDI…TIEIA → GNADYVFTSIFTLEII in isoform 4 and isoform 5. 1 PublicationAdd BLAST16
Alternative sequenceiVSP_0009111306 – 1333HYFCD…ITEVH → GYFSDPSNVFDFLIVIGSII AVILSETN in isoform 1 and isoform 4. 2 PublicationsAdd BLAST28
Alternative sequenceiVSP_0009121334 – 1344Missing in isoform 3. 1 PublicationAdd BLAST11

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M59786 mRNA Translation: AAA85463.1
M67515 mRNA Translation: AAA18905.1
M67516 mRNA Translation: AAA42016.1
M91242
, M91240, M89924, M91241 Genomic DNA Translation: AAA41460.1
S80558 mRNA Translation: AAB35528.1
U31815 mRNA Translation: AAA89157.1

NCBI Reference Sequences

More...
RefSeqi
NP_036649.2, NM_012517.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
24239

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:24239

UCSC genome browser

More...
UCSCi
RGD:2245 rat [P22002-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59786 mRNA Translation: AAA85463.1
M67515 mRNA Translation: AAA18905.1
M67516 mRNA Translation: AAA42016.1
M91242
, M91240, M89924, M91241 Genomic DNA Translation: AAA41460.1
S80558 mRNA Translation: AAB35528.1
U31815 mRNA Translation: AAA89157.1
RefSeqiNP_036649.2, NM_012517.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VYTX-ray2.60E/F452-476[»]
SMRiP22002
ModBaseiSearch...

Protein-protein interaction databases

BioGridi246425, 4 interactors
CORUMiP22002
IntActiP22002, 4 interactors
MINTiP22002
STRINGi10116.ENSRNOP00000009268

Chemistry databases

BindingDBiP22002
ChEMBLiCHEMBL3762
GuidetoPHARMACOLOGYi529

PTM databases

iPTMnetiP22002
PhosphoSitePlusiP22002

Proteomic databases

PaxDbiP22002
PRIDEiP22002

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24239
KEGGirno:24239
UCSCiRGD:2245 rat [P22002-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
775
RGDi2245 Cacna1c

Phylogenomic databases

eggNOGiKOG2301 Eukaryota
ENOG410XNP6 LUCA
InParanoidiP22002
KOiK04850
OrthoDBi172471at2759
PhylomeDBiP22002

Enzyme and pathway databases

ReactomeiR-RNO-422356 Regulation of insulin secretion
R-RNO-5576892 Phase 0 - rapid depolarisation
R-RNO-5576893 Phase 2 - plateau phase

Miscellaneous databases

EvolutionaryTraceiP22002

Protein Ontology

More...
PROi
PR:P22002

Family and domain databases

Gene3Di1.20.120.350, 4 hits
InterProiView protein in InterPro
IPR031688 CAC1F_C
IPR031649 GPHH_dom
IPR005821 Ion_trans_dom
IPR014873 VDCC_a1su_IQ
IPR005451 VDCC_L_a1csu
IPR005446 VDCC_L_a1su
IPR002077 VDCCAlpha1
IPR027359 Volt_channel_dom_sf
PfamiView protein in Pfam
PF08763 Ca_chan_IQ, 1 hit
PF16885 CAC1F_C, 1 hit
PF16905 GPHH, 1 hit
PF00520 Ion_trans, 4 hits
PRINTSiPR00167 CACHANNEL
PR01630 LVDCCALPHA1
PR01635 LVDCCALPHA1C
SMARTiView protein in SMART
SM01062 Ca_chan_IQ, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCAC1C_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P22002
Secondary accession number(s): P27733
, P27734, Q62816, Q63271, Q64178
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: May 8, 2019
This is version 176 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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