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Entry version 170 (07 Apr 2021)
Sequence version 1 (01 Apr 1988)
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Protein

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

Gene

CACNA1S

Organism
Oryctolagus cuniculus (Rabbit)
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-1S subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle (PubMed:9465115, PubMed:15201141, PubMed:25548159, PubMed:27621462, PubMed:29078335, PubMed:29467163). Calcium channels containing the alpha-1S subunit play an important role in excitation-contraction coupling in skeletal muscle via their interaction with RYR1, which triggers Ca2+ release from the sarcplasmic reticulum and ultimately results in muscle contraction (PubMed:9465115 PubMed:15201141, PubMed:27621462). Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group.Curated6 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Channel activity is blocked by dihydropyridines (DHP), phenylalkylamines, and by benzothiazepines.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi292CalciumCombined sources1 Publication1
Metal bindingi614CalciumCombined sources1 Publication1
Metal bindingi1014CalciumCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi1410 – 1421By 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

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.A.1.11.2, the voltage-gated ion channel (vic) superfamily

<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%5Fand%5Ftaxonomy%5Fsection">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-1S
Alternative name(s):
Calcium channel, L type, alpha-1 polypeptide, isoform 3, skeletal muscle
Dihydropyridine receptor alpha-1S subunit3 Publications
Short name:
DHPR2 Publications
Voltage-gated calcium channel subunit alpha Cav1.1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:CACNA1S
Synonyms:CACH1, CACNL1A3
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiOryctolagus cuniculus (Rabbit)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri9986 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000001811 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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 – 51Cytoplasmic1 PublicationAdd BLAST51
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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>Transmembranei52 – 70Helical; Name=S1 of repeat I1 PublicationAdd BLAST19
Topological domaini71 – 85Extracellular1 PublicationAdd BLAST15
Transmembranei86 – 106Helical; Name=S2 of repeat I1 PublicationAdd BLAST21
Topological domaini107 – 115Cytoplasmic1 Publication9
Transmembranei116 – 136Helical; Name=S3 of repeat I1 PublicationAdd BLAST21
Topological domaini137 – 160Extracellular1 PublicationAdd BLAST24
Transmembranei161 – 179Helical; Name=S4 of repeat I1 PublicationAdd BLAST19
Topological domaini180 – 196Cytoplasmic1 PublicationAdd BLAST17
Transmembranei197 – 218Helical; Name=S5 of repeat I1 PublicationAdd BLAST22
Topological domaini219 – 279Extracellular1 PublicationAdd BLAST61
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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>Intramembranei280 – 301Pore-forming2 PublicationsAdd BLAST22
Topological domaini302 – 309Extracellular1 Publication8
Transmembranei310 – 330Helical; Name=S6 of repeat I1 PublicationAdd BLAST21
Topological domaini331 – 432Cytoplasmic1 PublicationAdd BLAST102
Transmembranei433 – 451Helical; Name=S1 of repeat II1 PublicationAdd BLAST19
Topological domaini452 – 462Extracellular1 PublicationAdd BLAST11
Transmembranei463 – 483Helical; Name=S2 of repeat II1 PublicationAdd BLAST21
Topological domaini484 – 494Cytoplasmic1 PublicationAdd BLAST11
Transmembranei495 – 514Helical; Name=S3 of repeat II1 PublicationAdd BLAST20
Topological domaini515 – 523Extracellular1 Publication9
Transmembranei524 – 542Helical; Name=S4 of repeat II1 PublicationAdd BLAST19
Topological domaini543 – 561Cytoplasmic1 PublicationAdd BLAST19
Transmembranei562 – 581Helical; Name=S5 of repeat II1 PublicationAdd BLAST20
Topological domaini582 – 601Extracellular1 PublicationAdd BLAST20
Intramembranei602 – 623Pore-forming2 PublicationsAdd BLAST22
Topological domaini624 – 633Extracellular1 Publication10
Transmembranei634 – 653Helical; Name=S6 of repeat II1 PublicationAdd BLAST20
Topological domaini654 – 799Cytoplasmic1 PublicationAdd BLAST146
Transmembranei800 – 818Helical; Name=S1 of repeat III1 PublicationAdd BLAST19
Topological domaini819 – 830Extracellular1 PublicationAdd BLAST12
Transmembranei831 – 850Helical; Name=S2 of repeat III1 PublicationAdd BLAST20
Topological domaini851 – 866Cytoplasmic1 PublicationAdd BLAST16
Transmembranei867 – 885Helical; Name=S3 of repeat III1 PublicationAdd BLAST19
Topological domaini886 – 892Extracellular1 Publication7
Transmembranei893 – 911Helical; Name=S4 of repeat III1 PublicationAdd BLAST19
Topological domaini912 – 930Cytoplasmic1 PublicationAdd BLAST19
Transmembranei931 – 950Helical; Name=S5 of repeat III1 PublicationAdd BLAST20
Topological domaini951 – 1000Extracellular1 PublicationAdd BLAST50
Intramembranei1001 – 1021Pore-forming2 PublicationsAdd BLAST21
Topological domaini1022 – 1038Extracellular1 PublicationAdd BLAST17
Transmembranei1039 – 1060Helical; Name=S6 of repeat III1 PublicationAdd BLAST22
Topological domaini1061 – 1118Cytoplasmic1 PublicationAdd BLAST58
Transmembranei1119 – 1140Helical; Name=S1 of repeat IV1 PublicationAdd BLAST22
Topological domaini1141 – 1148Extracellular1 Publication8
Transmembranei1149 – 1170Helical; Name=S2 of repeat IV1 PublicationAdd BLAST22
Topological domaini1171 – 1180Cytoplasmic1 Publication10
Transmembranei1181 – 1200Helical; Name=S3 of repeat IV1 PublicationAdd BLAST20
Topological domaini1201 – 1231Extracellular1 PublicationAdd BLAST31
Transmembranei1232 – 1250Helical; Name=S4 of repeat IV1 PublicationAdd BLAST19
Topological domaini1251 – 1268Cytoplasmic1 PublicationAdd BLAST18
Transmembranei1269 – 1289Helical; Name=S5 of repeat IV1 PublicationAdd BLAST21
Topological domaini1290 – 1311Extracellular1 PublicationAdd BLAST22
Intramembranei1312 – 1330Pore-forming2 PublicationsAdd BLAST19
Topological domaini1331 – 1356Extracellular1 PublicationAdd BLAST26
Transmembranei1357 – 1381Helical; Name=S6 of repeat IV1 PublicationAdd BLAST25
Topological domaini1382 – 1873Cytoplasmic1 PublicationAdd BLAST492

Keywords - Cellular componenti

Cell membrane, Membrane

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi752 – 753IP → AA: Loss of interaction with STAC2 and STAC3 and strongly decreased channel activity; when associated with A-757. 1 Publication2
Mutagenesisi756 – 758PRP → ARA: Loss of interaction with STAC3. 1 Publication3
Mutagenesisi757R → A: Loss of interaction with STAC2 and STAC3 and strongly decreased channel activity; when associated with 752-AA-753. 1 Publication1
Mutagenesisi1086R → H: Shifts the threshold potential to more negative values and lowers the concentration threshold for channel activation by caffeine. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4169

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000539451 – 1873Voltage-dependent L-type calcium channel subunit alpha-1SAdd BLAST1873

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Glycosylationi79N-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 bondi226 ↔ 254Combined sources1 Publication
Disulfide bondi245 ↔ 261Combined sources1 Publication
Glycosylationi257N-linked (GlcNAc...) asparagineCombined sources1
<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 residuei393PhosphoserineBy similarity1
Modified residuei397PhosphoserineBy similarity1
Modified residuei687Phosphoserine; by PKA1 Publication1
Disulfide bondi957 ↔ 968Combined sources1 Publication
Disulfide bondi1338 ↔ 1352Combined sources1 Publication
Modified residuei1575Phosphoserine; by PKA and CAMK21 Publication1
Modified residuei1579Phosphothreonine; by CK21 Publication1
Modified residuei1617Phosphoserine; by PKA1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

The alpha-1S subunit is found in two isoforms in the skeletal muscle: a minor form of 212 kDa containing the complete amino acid sequence, and a major form of 190 kDa derived from the full-length form by post-translational proteolysis close to Phe-1690.1 Publication
Phosphorylated. Phosphorylation by PKA activates the calcium channel. Both the minor and major forms are phosphorylated in vitro by PKA (PubMed:2549550, PubMed:2844809). Phosphorylation at Ser-1575 is involved in beta-adrenergic-mediated regulation of the channel (PubMed:20937870).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Sitei1690 – 1691CleavageCurated2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P07293

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P07293

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P07293

<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 skeletal muscle T-tubules (at protein level).4 Publications

<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%5Fsection">'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%5Fsection">'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 (CACNA1S) and the ancillary subunits CACNB1 or CACNB2, CACNG1 and CACNA2D1 (PubMed:3037387, PubMed:27621462, PubMed:15134636, PubMed:25667046, PubMed:26680202, PubMed:27580036). The channel complex contains alpha, beta, gamma and delta subunits in a 1:1:1:1 ratio, i.e. it contains either CACNB1 or CACNB2 (PubMed:15134636, PubMed:25667046, PubMed:26680202, PubMed:27580036). CACNA1S channel activity is modulated by the auxiliary subunits (CACNB1 or CACNB2, CACNG1 and CACNA2D1).

Interacts with DYSF and JSRP1 (By similarity).

Interacts with RYR1 (PubMed:10388749).

Interacts with STAC, STAC2 and STAC3 (via their SH3 domains) (PubMed:28112192, PubMed:29078335, PubMed:29467163). Interaction with STAC3 promotes expression at the cell membrane (PubMed:25548159, PubMed:29467163). Interaction with STAC2 promotes expression at the cell membrane, but with much lower efficiency than STAC3. Interaction with STAC1 leads to very low levels expression at the cell membrane, much less than the levels observed upon interaction with STAC3 and STAC2 (PubMed:29467163).

Interacts with CALM (By similarity).

By similarity11 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
1172604, 1 interactor

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-3189, Skeletal muscle VGCC complex

Database of interacting proteins

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DIPi
DIP-61879N

Protein interaction database and analysis system

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IntActi
P07293, 4 interactors

Molecular INTeraction database

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MINTi
P07293

STRING: functional protein association networks

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STRINGi
9986.ENSOCUP00000003147

<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

11873
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

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BMRBi
P07293

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

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SMRi
P07293

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P07293

<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>Repeati38 – 337ICuratedAdd BLAST300
Repeati418 – 664IICuratedAdd BLAST247
Repeati786 – 1068IIICuratedAdd BLAST283
Repeati1105 – 1384IVCuratedAdd BLAST280

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>Regioni357 – 374Binding to the beta subunit1 PublicationAdd BLAST18
Regioni747 – 760Interaction with STAC, STAC2 and STAC3 (via SH3 domains)1 PublicationAdd BLAST14
Regioni988 – 1077Dihydropyridine binding2 PublicationsAdd BLAST90
Regioni1337 – 1403Dihydropyridine binding1 PublicationAdd BLAST67
Regioni1349 – 1391Phenylalkylamine binding1 PublicationAdd BLAST43
Regioni1522 – 1542Interaction with calmodulinBy similarityAdd BLAST21

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>Motifi290 – 293Selectivity filter of repeat I2 Publications4
Motifi612 – 615Selectivity filter of repeat II2 Publications4
Motifi1012 – 1015Selectivity filter of repeat III2 Publications4
Motifi1321 – 1324Selectivity filter of repeat IV2 Publications4

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 biasi562 – 568Poly-Leu7

<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.2 Publications
The loop between repeats II and III interacts with the ryanodine receptor, and is therefore important for calcium release from the endoplasmic reticulum necessary for muscle contraction.3 Publications

<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

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P07293

Identification of Orthologs from Complete Genome Data

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OMAi
KWILYFR

Database of Orthologous Groups

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OrthoDBi
172471at2759

Family and domain databases

Database of protein disorder

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DisProti
DP00228

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
IPR005450, VDCC_L_a1ssu
IPR005446, VDCC_L_a1su
IPR002077, VDCCAlpha1
IPR027359, Volt_channel_dom_sf

Pfam protein domain database

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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

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PRINTSi
PR00167, CACHANNEL
PR01630, LVDCCALPHA1
PR01634, LVDCCALPHA1S

Simple Modular Architecture Research Tool; a protein domain database

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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%5Flength">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>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P07293-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEPSSPQDEG LRKKQPKKPL PEVLPRPPRA LFCLTLQNPL RKACISIVEW
60 70 80 90 100
KPFETIILLT IFANCVALAV YLPMPEDDNN SLNLGLEKLE YFFLTVFSIE
110 120 130 140 150
AAMKIIAYGF LFHQDAYLRS GWNVLDFIIV FLGVFTAILE QVNVIQSNTA
160 170 180 190 200
PMSSKGAGLD VKALRAFRVL RPLRLVSGVP SLQVVLNSIF KAMLPLFHIA
210 220 230 240 250
LLVLFMVIIY AIIGLELFKG KMHKTCYYIG TDIVATVENE KPSPCARTGS
260 270 280 290 300
GRPCTINGSE CRGGWPGPNH GITHFDNFGF SMLTVYQCIT MEGWTDVLYW
310 320 330 340 350
VNDAIGNEWP WIYFVTLILL GSFFILNLVL GVLSGEFTKE REKAKSRGTF
360 370 380 390 400
QKLREKQQLE EDLRGYMSWI TQGEVMDVED LREGKLSLEE GGSDTESLYE
410 420 430 440 450
IEGLNKIIQF IRHWRQWNRV FRWKCHDLVK SRVFYWLVIL IVALNTLSIA
460 470 480 490 500
SEHHNQPLWL THLQDIANRV LLSLFTIEML LKMYGLGLRQ YFMSIFNRFD
510 520 530 540 550
CFVVCSGILE LLLVESGAMT PLGISVLRCI RLLRLFKITK YWTSLSNLVA
560 570 580 590 600
SLLNSIRSIA SLLLLLFLFI IIFALLGMQL FGGRYDFEDT EVRRSNFDNF
610 620 630 640 650
PQALISVFQV LTGEDWNSVM YNGIMAYGGP SYPGVLVCIY FIILFVCGNY
660 670 680 690 700
ILLNVFLAIA VDNLAEAESL TSAQKAKAEE RKRRKMSRGL PDKTEEEKSV
710 720 730 740 750
MAKKLEQKPK GEGIPTTAKL KVDEFESNVN EVKDPYPSAD FPGDDEEDEP
760 770 780 790 800
EIPVSPRPRP LAELQLKEKA VPIPEASSFF IFSPTNKVRV LCHRIVNATW
810 820 830 840 850
FTNFILLFIL LSSAALAAED PIRAESVRNQ ILGYFDIAFT SVFTVEIVLK
860 870 880 890 900
MTTYGAFLHK GSFCRNYFNI LDLLVVAVSL ISMGLESSTI SVVKILRVLR
910 920 930 940 950
VLRPLRAINR AKGLKHVVQC VFVAIRTIGN IVLVTTLLQF MFACIGVQLF
960 970 980 990 1000
KGKFFSCNDL SKMTEEECRG YYYVYKDGDP TQMELRPRQW IHNDFHFDNV
1010 1020 1030 1040 1050
LSAMMSLFTV STFEGWPQLL YRAIDSNEED MGPVYNNRVE MAIFFIIYII
1060 1070 1080 1090 1100
LIAFFMMNIF VGFVIVTFQE QGETEYKNCE LDKNQRQCVQ YALKARPLRC
1110 1120 1130 1140 1150
YIPKNPYQYQ VWYVVTSSYF EYLMFALIML NTICLGMQHY HQSEEMNHIS
1160 1170 1180 1190 1200
DILNVAFTII FTLEMILKLL AFKARGYFGD PWNVFDFLIV IGSIIDVILS
1210 1220 1230 1240 1250
EIDTFLASSG GLYCLGGGCG NVDPDESARI SSAFFRLFRV MRLIKLLSRA
1260 1270 1280 1290 1300
EGVRTLLWTF IKSFQALPYV ALLIVMLFFI YAVIGMQMFG KIALVDGTQI
1310 1320 1330 1340 1350
NRNNNFQTFP QAVLLLFRCA TGEAWQEILL ACSYGKLCDP ESDYAPGEEY
1360 1370 1380 1390 1400
TCGTNFAYYY FISFYMLCAF LIINLFVAVI MDNFDYLTRD WSILGPHHLD
1410 1420 1430 1440 1450
EFKAIWAEYD PEAKGRIKHL DVVTLLRRIQ PPLGFGKFCP HRVACKRLVG
1460 1470 1480 1490 1500
MNMPLNSDGT VTFNATLFAL VRTALKIKTE GNFEQANEEL RAIIKKIWKR
1510 1520 1530 1540 1550
TSMKLLDQVI PPIGDDEVTV GKFYATFLIQ EHFRKFMKRQ EEYYGYRPKK
1560 1570 1580 1590 1600
DTVQIQAGLR TIEEEAAPEI RRTISGDLTA EEELERAMVE AAMEERIFRR
1610 1620 1630 1640 1650
TGGLFGQVDT FLERTNSLPP VMANQRPLQF AEIEMEELES PVFLEDFPQD
1660 1670 1680 1690 1700
ARTNPLARAN TNNANANVAY GNSNHSNNQM FSSVHCEREF PGEAETPAAG
1710 1720 1730 1740 1750
RGALSHSHRA LGPHSKPCAG KLNGQLVQPG MPINQAPPAP CQQPSTDPPE
1760 1770 1780 1790 1800
RGQRRTSLTG SLQDEAPQRR SSEGSTPRRP APATALLIQE ALVRGGLDTL
1810 1820 1830 1840 1850
AADAGFVTAT SQALADACQM EPEEVEVAAT ELLKARESVQ GMASVPGSLS
1860 1870
RRSSLGSLDQ VQGSQETLIP PRP
Length:1,873
Mass (Da):212,029
Last modified:April 1, 1988 - 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:i047B10D1946B0796
GO

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 conflicti694T → R in AAA31159 (PubMed:2458626).Curated1
Sequence conflicti1808T → M in AAA31159 (PubMed:2458626).Curated1
Sequence conflicti1815A → V in AAA31159 (PubMed:2458626).Curated1
Sequence conflicti1835A → E in AAA31159 (PubMed:2458626).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti165R → K. 1
Natural varianti258G → D. 1
Natural varianti1870P → L. 1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X05921 mRNA Translation: CAA29355.1
M23919 mRNA Translation: AAA31159.1

Protein sequence database of the Protein Information Resource

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PIRi
A30063

NCBI Reference Sequences

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RefSeqi
NP_001095190.1, NM_001101720.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
100009585

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ocu:100009585

<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
X05921 mRNA Translation: CAA29355.1
M23919 mRNA Translation: AAA31159.1
PIRiA30063
RefSeqiNP_001095190.1, NM_001101720.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DU1NMR-A671-690[»]
1JZPNMR-A671-690[»]
1T3LX-ray2.20B357-374[»]
3JBRelectron microscopy4.20A1-1873[»]
5GJVelectron microscopy3.60A1-1873[»]
5GJWelectron microscopy3.90A1-1873[»]
6BYOelectron microscopy3.60A32-1388[»]
6JP5electron microscopy2.90A1-1873[»]
6JP8electron microscopy2.70A1-1873[»]
6JPAelectron microscopy2.60A1-1506[»]
6JPBelectron microscopy2.90A1-1873[»]
7JPKelectron microscopy3.00A1-1873[»]
7JPLelectron microscopy3.40A1-1873[»]
7JPVelectron microscopy3.40A1-1873[»]
7JPWelectron microscopy3.20A1-1873[»]
7JPXelectron microscopy2.90A1-1873[»]
BMRBiP07293
SMRiP07293
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi1172604, 1 interactor
ComplexPortaliCPX-3189, Skeletal muscle VGCC complex
DIPiDIP-61879N
IntActiP07293, 4 interactors
MINTiP07293
STRINGi9986.ENSOCUP00000003147

Chemistry databases

ChEMBLiCHEMBL4169

Protein family/group databases

TCDBi1.A.1.11.2, the voltage-gated ion channel (vic) superfamily

PTM databases

iPTMnetiP07293
SwissPalmiP07293

Proteomic databases

PRIDEiP07293

Genome annotation databases

GeneIDi100009585
KEGGiocu:100009585

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
779

Phylogenomic databases

eggNOGiKOG2301, Eukaryota
InParanoidiP07293
OMAiKWILYFR
OrthoDBi172471at2759

Miscellaneous databases

EvolutionaryTraceiP07293

Protein Ontology

More...
PROi
PR:P07293

Family and domain databases

DisProtiDP00228
Gene3Di1.20.120.350, 4 hits
InterProiView protein in InterPro
IPR031688, CAC1F_C
IPR031649, GPHH_dom
IPR005821, Ion_trans_dom
IPR014873, VDCC_a1su_IQ
IPR005450, VDCC_L_a1ssu
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
PR01634, LVDCCALPHA1S
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 nameiCAC1S_RABIT
<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: P07293
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: April 7, 2021
This is version 170 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, Direct protein sequencing, 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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