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Entry version 153 (08 May 2019)
Sequence version 1 (01 Apr 1990)
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Protein

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

Gene

CACNA1C

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-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents (PubMed:2474130, PubMed:2169433, PubMed:8232554, PubMed:9502794, PubMed:9278523, PubMed:15615847, PubMed:17525370, PubMed:21127204, PubMed:22928916, PubMed:23145875, PubMed:29363593, PubMed:22649239). Mediates influx of calcium ions into the cytoplasm, and thereby triggers calcium release from the sarcoplasm (PubMed:23145875). Plays an important role in excitation-contraction coupling in the heart (PubMed:17525370, PubMed:22928916, PubMed:23145875). 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 (Probable).By similarityCurated12 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 (PubMed:2474130, PubMed:9278523). Inhibited by nifedipine (PubMed:23145875). Channel activity is regulated by Ca2+ and calmodulin (PubMed:7491499, PubMed:29363593). Binding of STAC1, STAC2 or STAC3 to a region that overlaps with the calmodulin binding site inhibits channel inactivation by Ca2+ and calmodulin (PubMed:29363593). Binding of calmodulin or CABP1 at the same regulatory sites results in opposite effects on the channel function (By similarity). Shear stress and pressure increases calcium channel activity (By similarity).By similarity5 Publications

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 permeability1 Publication1
Metal bindingi736CalciumBy similarity1
Sitei736Calcium ion selectivity and permeability1 Publication1
Metal bindingi1145CalciumBy similarity1
Sitei1145Calcium ion selectivity and permeability1 Publication1
Sitei1446Calcium ion selectivity and permeability1 Publication1

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 bindingi1535 – 1546Add 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

<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
Smooth muscle calcium channel blocker receptor
Short name:
CACB-receptor
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>OrganismiOryctolagus cuniculus (Rabbit)
<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 identifieri9986 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
<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
  • UP000001811 <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

<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 – 1042Helical; Name=S4 of repeat IIIBy similarityAdd BLAST19
Topological domaini1043 – 1061CytoplasmicCuratedAdd BLAST19
Transmembranei1062 – 1081Helical; Name=S5 of repeat IIIBy similarityAdd BLAST20
Topological domaini1082 – 1131ExtracellularCuratedAdd BLAST50
Intramembranei1132 – 1152Pore-formingBy similarityAdd BLAST21
Topological domaini1153 – 1169ExtracellularCuratedAdd BLAST17
Transmembranei1170 – 1191Helical; Name=S6 of repeat IIIBy similarityAdd BLAST22
Topological domaini1192 – 1249CytoplasmicCuratedAdd BLAST58
Transmembranei1250 – 1271Helical; Name=S1 of repeat IVBy similarityAdd BLAST22
Topological domaini1272 – 1279ExtracellularCurated8
Transmembranei1280 – 1301Helical; Name=S2 of repeat IVBy similarityAdd BLAST22
Topological domaini1302 – 1311CytoplasmicCurated10
Transmembranei1312 – 1331Helical; Name=S3 of repeat IVBy similarityAdd BLAST20
Topological domaini1332 – 1354ExtracellularCuratedAdd BLAST23
Transmembranei1355 – 1373Helical; Name=S4 of repeat IVBy similarityAdd BLAST19
Topological domaini1374 – 1391CytoplasmicCuratedAdd BLAST18
Transmembranei1392 – 1412Helical; Name=S5 of repeat IVBy similarityAdd BLAST21
Topological domaini1413 – 1434ExtracellularCuratedAdd BLAST22
Intramembranei1435 – 1453Pore-formingBy similarityAdd BLAST19
Topological domaini1454 – 1481ExtracellularCuratedAdd BLAST28
Transmembranei1482 – 1506Helical; Name=S6 of repeat IVBy similarityAdd BLAST25
Topological domaini1507 – 2171CytoplasmicCuratedAdd BLAST665

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi168C → G: Small reduction of current amplitude. 1 Publication1
Mutagenesisi168C → K or W: No current. 1 Publication1
Mutagenesisi168C → S: No effect. 1 Publication1
Mutagenesisi168C → Y: Slower channel activation and reduction of current amplitude. 1 Publication1
Mutagenesisi393E → A: Loss of channel activity and ability to trigger cardiomyocyte contraction; when associated with A-736; A-1145 and A-1446. 1 Publication1
Mutagenesisi393E → K: Drastic reduction of barium permeability. Reduction of calcium block of lithium currents. 1 Publication1
Mutagenesisi393E → Q: Attenuates calcium block of inward barium, lithium, or cadmium currents. 1 Publication1
Mutagenesisi449G → R: Decreased rate of channel inactivation. 1 Publication1
Mutagenesisi736E → A: Loss of channel activity and ability to trigger cardiomyocyte contraction; when associated with A-393; A-1145 and A-1446. 1 Publication1
Mutagenesisi736E → K: Drastic reduction of barium permeability. Reduction of calcium block of lithium currents. 1 Publication1
Mutagenesisi736E → Q: Attenuates calcium block of inward barium, lithium, or cadmium currents. 1 Publication1
Mutagenesisi775L → P: Loss of nifedipine-sensitivity and channel activity; when associated with Y-1066. 1 Publication1
Mutagenesisi1066T → Y: Loss of nifedipine-sensitivity and channel activity; when associated with P-775. 1 Publication1
Mutagenesisi1145E → A: Loss of channel activity and ability to trigger cardiomyocyte contraction; when associated with A-393; A-736 and A-1446. 1 Publication1
Mutagenesisi1145E → K: Drastic reduction of barium permeability. Reduction of calcium block of lithium currents. 1 Publication1
Mutagenesisi1145E → Q: Attenuates calcium block of inward barium, lithium, or cadmium currents. 1 Publication1
Mutagenesisi1446E → A: Loss of channel activity and ability to trigger cardiomyocyte contraction; when associated with A-393; A-736 and A-1145. 1 Publication1
Mutagenesisi1446E → K: Moderate reduction of barium permeability. Reduction of calcium block of lithium currents. 1 Publication1
Mutagenesisi1446E → Q: Attenuates calcium block of inward barium, lithium, or cadmium currents. 1 Publication1
Mutagenesisi1648F → A: Mildly decreased interaction with STAC3. 1 Publication1
Mutagenesisi1654I → A: Strongly decreased interaction with STAC3. 1 Publication1
Mutagenesisi1658F → A: Decreased interaction with STAC3. 1 Publication1
Mutagenesisi1659R → A: Mildly decreased interaction with STAC3. 1 Publication1
Mutagenesisi1681 – 1684LQAG → AAAA: Strongly reduced channel clustering at the junctional membrane. 1 Publication4
Mutagenesisi1685 – 1688LRTL → AAAA: Strongly reduced channel clustering at the junctional membrane. 1 Publication4
Mutagenesisi1697 – 1700RAIS → AAAA: Strongly reduced channel clustering at the junctional membrane. 1 Publication4

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2830

<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_00000539301 – 2171Voltage-dependent L-type calcium channel subunit alpha-1CAdd BLAST2171

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 residuei845PhosphoserineBy similarity1
Disulfide bondi1088 ↔ 1099By similarity
Glycosylationi1418N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1461 ↔ 1477By similarity
Glycosylationi1469N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei1517Phosphoserine; by PKASequence analysis1
Modified residuei1700PhosphoserineBy similarity1
Modified residuei1721PhosphoserineBy similarity1
Modified residuei1920Phosphoserine; by PKASequence analysis1
Modified residuei1928Phosphoserine; 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 (PubMed:1325377). Elevated levels of blood glucose lead to increased phosphorylation by PKA (By similarity).By similarity1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

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PRIDEi
P15381

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P15381

<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

Expression in cardiac muscle. In lung, expressed in airway and vascular smooth muscle cells.

<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:17525370, PubMed:21127204). 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 (Probable). CACNA1C channel activity is modulated by ancillary subunits, such as CACNB1, CACNB2, CACNB3, CACNA2D1 and CACNA2D4 (PubMed:9278523, PubMed:15615847, PubMed:17525370, PubMed:21127204).

Interacts with CACNB1 (PubMed:7509046, PubMed:15615847, PubMed:21127204).

Interacts with CACNB2 (PubMed:17525370, PubMed:21127204, PubMed:22649239).

Identified in a complex with CACNA2D4 and CACNB3.

Interacts with CACNB3 (By similarity).

Interacts with CACNA2D1 (PubMed:9278523, PubMed:21127204). Intereracts with the gamma subunits CACNG4, CACNG6, CACNG7 and CACNG8 (PubMed:21127204).

Interacts with CACNA2D4 (By similarity).

Interacts with CALM1 (PubMed:29363593).

Interacts (via the N-terminus and the C-terminal C and IQ motifs) with CABP1; this inhibits Ca2+-dependent channel inactivation. 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 (By similarity). 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 STAC1, STAC2 and STAC3; this inhibits channel inactivation, probably by hindering CALM1 binding (PubMed:25548159, PubMed:29363593).

By similarityCurated8 Publications

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

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DIPi
DIP-61286N

Protein interaction database and analysis system

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IntActi
P15381, 3 interactors

STRING: functional protein association networks

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STRINGi
9986.ENSOCUP00000009984

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P15381

<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

12171
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
P15381

Database of comparative protein structure models

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ModBasei
Search...

<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 – 1199IIIAdd BLAST283
Repeati1236 – 1509IVAdd 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 subunitBy similarityAdd BLAST18
Regioni859 – 906Interaction with STAC2By similarityAdd BLAST48
Regioni1119 – 1208Dihydropyridine bindingBy similarityAdd BLAST90
Regioni1460 – 1528Dihydropyridine bindingBy similarityAdd BLAST69
Regioni1474 – 1516Phenylalkylamine bindingBy similarityAdd BLAST43
Regioni1641 – 1668Important for interaction with STAC1, STAC2 and STAC31 PublicationAdd BLAST28
Regioni1647 – 1667Calmodulin-binding IQ regionBy similarityAdd BLAST21
Regioni1681 – 1700Important for localization in at the junctional membrane1 PublicationAdd 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
Motifi1143 – 1146Selectivity filter of repeat IIIBy similarity4
Motifi1444 – 1447Selectivity 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 biasi1177 – 1183Poly-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.1 Publication

<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

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P15381

KEGG Orthology (KO)

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KOi
K04850

Database of Orthologous Groups

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OrthoDBi
172471at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.120.350, 4 hits

Integrated resource of protein families, domains and functional sites

More...
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, 2 hits
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.
Isoform 1 (identifier: P15381-1) [UniParc]FASTAAdd to basket
Also known as: CACH2A

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
MLRALVQPAT PAYQPLPSHL SAETESTCKG TVVHEAQLNH FYISPGGSNY
60 70 80 90 100
GSPRPAHANM NANAAAGLAP EHIPTPGAAL SWQAAIDAAR QAKLMGSAGN
110 120 130 140 150
ATISTVSSTQ RKRQQYGKPK KQGSTTATRP 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 QEGVADVPAE DDPSPCALET
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 NEDEGMDEEK 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 LETILVETKV MSPLGISVLR
660 670 680 690 700
CVRLLRIFKI TRYWNSLSNL VASLLNSVRS IASLLLLLFL FIIIFSLLGM
710 720 730 740 750
QLFGGKFNFD EMQTRRSTFD NFPQSLLTVF QILTGEDWNS VMYDGIMAYG
760 770 780 790 800
GPSFPGMLVC IYFIILFICG NYILLNVFLA IAVDNLADAE SLTSAQKEEE
810 820 830 840 850
EEKERKKLAR TASPEKKQEV VGKPALEEAK EEKIELKSIT ADGESPPTTK
860 870 880 890 900
INMDDLQPNE SEDKSPYPNP ETTGEEDEEE 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 RVLRPLRAIN RAKGLKHVVQ
1060 1070 1080 1090 1100
CVFVAIRTIG NIVIVTTLLQ FMFACIGVQL FKGKLYTCSD SSKQTEAECK
1110 1120 1130 1140 1150
GNYITYKDGE VDHPIIQPRS WENSKFDFDN VLAAMMALFT VSTFEGWPEL
1160 1170 1180 1190 1200
LYRSIDSHTE DKGPIYNYRV EISIFFIIYI IIIAFFMMNI FVGFVIVTFQ
1210 1220 1230 1240 1250
EQGEQEYKNC ELDKNQRQCV EYALKARPLR RYIPKNQHQY KVWYVVNSTY
1260 1270 1280 1290 1300
FEYLMFVLIL LNTICLAMQH YGQSCLFKIA MNILNMLFTG LFTVEMILKL
1310 1320 1330 1340 1350
IAFKPKGYFS DPWNVFDFLI VIGSIIDVIL SETNPAEHTQ CSPSMNAEEN
1360 1370 1380 1390 1400
SRISITFFRL FRVMRLVKLL SRGEGIRTLL WTFIKSFQAL PYVALLIVML
1410 1420 1430 1440 1450
FFIYAVIGMQ VFGKIALNDT TEINRNNNFQ TFPQAVLLLF RCATGEAWQD
1460 1470 1480 1490 1500
IMLACMPGKK CAPESEPHNS TEGETPCGSS FAVFYFISFY MLCAFLIINL
1510 1520 1530 1540 1550
FVAVIMDNFD YLTRDWSILG PHHLDEFKRI WAEYDPEAKG RIKHLDVVTL
1560 1570 1580 1590 1600
LRRIQPPLGF GKLCPHRVAC KRLVSMNMPL NSDGTVMFNA TLFALVRTAL
1610 1620 1630 1640 1650
RIKTEGNLEQ ANEELRAIIK KIWKRTSMKL LDQVVPPAGD DEVTVGKFYA
1660 1670 1680 1690 1700
TFLIQEYFRK FKKRKEQGLV GKPSQRNALS LQAGLRTLHD IGPEIRRAIS
1710 1720 1730 1740 1750
GDLTAEEELD KAMKEAVSAA SEDDIFRRAG GLFGNHVSYY QSDSRSAFPQ
1760 1770 1780 1790 1800
TFTTQRPLHI SKAGNNQGDT ESPSHEKLVD STFTPSSYSS TGSNANINNA
1810 1820 1830 1840 1850
NNTALGRLPR PAGYPSTVST VEGHGSPLSP AVRAQEAAWK LSSKRCHSQE
1860 1870 1880 1890 1900
SQIAMACQEG ASQDDNYDVR IGEDAECCSE PSLLSTEMLS YQDDENRQLA
1910 1920 1930 1940 1950
PPEEEKRDIR LSPKKGFLRS ASLGRRASFH LECLKRQKNQ GGDISQKTVL
1960 1970 1980 1990 2000
PLHLVHHQAL AVAGLSPLLQ RSHSPTSLPR PCATPPATPG SRGWPPQPIP
2010 2020 2030 2040 2050
TLRLEGADSS EKLNSSFPSI HCGSWSGENS PCRGDSSAAR RARPVSLTVP
2060 2070 2080 2090 2100
SQAGAQGRQF HGSASSLVEA VLISEGLGQF AQDPKFIEVT TQELADACDL
2110 2120 2130 2140 2150
TIEEMENAAD DILSGGARQS PNGTLLPFVN RRDPGRDRAG QNEQDASGAC
2160 2170
APGCGQSEEA LADRRAGVSS L
Length:2,171
Mass (Da):242,784
Last modified:April 1, 1990 - 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:iB64F08F09D71C65D
GO
Isoform 2 (identifier: P15381-2) [UniParc]FASTAAdd to basket
Also known as: CACH2C

The sequence of this isoform differs from the canonical sequence as follows:
     1307-1334: GYFSDPWNVFDFLIVIGSIIDVILSETN → HYFCDAWNTFDALIVVGSIVDIAITEVH

Show »
Length:2,171
Mass (Da):242,759
Checksum:i7F19227123159A9E
GO
Isoform 3 (identifier: P15381-3) [UniParc]FASTAAdd to basket
Also known as: CACH2D

The sequence of this isoform differs from the canonical sequence as follows:
     1335-1345: Missing.

Show »
Length:2,160
Mass (Da):241,615
Checksum:i567DCCDB7351490F
GO
Isoform 4 (identifier: P15381-4) [UniParc]FASTAAdd to basket
Also known as: Lung

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: MLRALVQPATPAYQPLPSHLSAETESTCKGTVVHEAQLNHFYISPG → MVNENTRMYIPEENHQ
     402-421: MQDAMGYELPWVYFVSLVIF → VNDAVGRDWPWIYFVTLIII
     494-494: M → RGTPAGLHAQKKGKFAWFSHSTETHV
     1307-1334: GYFSDPWNVFDFLIVIGSIIDVILSETN → HYFCDAWNTFDALIVVGSIVDIAITEVH

Show »
Length:2,166
Mass (Da):242,485
Checksum:i824857C865A8E5F5
GO
Isoform 5 (identifier: P15381-5) [UniParc]FASTAAdd to basket
Also known as: C141

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: MLRALVQPATPAYQPLPSHLSAETESTCKGTVVHEAQLNHFYISPG → MVNENTRMYIPEENHQ
     66-79: Missing.

Show »
Length:2,127
Mass (Da):238,515
Checksum:iD183FDEC42FB6401
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 conflicti1346N → S in AAA31182 (PubMed:2173707).Curated1
Sequence conflicti1468H → S in AAA31182 (PubMed:2173707).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_0009021 – 46MLRAL…YISPG → MVNENTRMYIPEENHQ in isoform 4 and isoform 5. 1 PublicationAdd BLAST46
Alternative sequenceiVSP_00090366 – 79Missing in isoform 5. 1 PublicationAdd BLAST14
Alternative sequenceiVSP_000904402 – 421MQDAM…SLVIF → VNDAVGRDWPWIYFVTLIII in isoform 4. CuratedAdd BLAST20
Alternative sequenceiVSP_000905494M → RGTPAGLHAQKKGKFAWFSH STETHV in isoform 4. Curated1
Alternative sequenceiVSP_0009061307 – 1334GYFSD…LSETN → HYFCDAWNTFDALIVVGSIV DIAITEVH in isoform 2 and isoform 4. 1 PublicationAdd BLAST28
Alternative sequenceiVSP_0009071335 – 1345Missing in isoform 3. CuratedAdd BLAST11

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
X15539 mRNA Translation: CAA33546.1
X55763 mRNA Translation: CAA39289.1
X60782 mRNA Translation: CAA43196.1
M57974 mRNA Translation: AAA31182.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S05054
S11339

NCBI Reference Sequences

More...
RefSeqi
NP_001129994.1, NM_001136522.1 [P15381-1]

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
100101555

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ocu:100101555

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
X15539 mRNA Translation: CAA33546.1
X55763 mRNA Translation: CAA39289.1
X60782 mRNA Translation: CAA43196.1
M57974 mRNA Translation: AAA31182.1
PIRiS05054
S11339
RefSeqiNP_001129994.1, NM_001136522.1 [P15381-1]

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
4DEYX-ray1.95B435-539[»]
SMRiP15381
ModBaseiSearch...

Protein-protein interaction databases

DIPiDIP-61286N
IntActiP15381, 3 interactors
STRINGi9986.ENSOCUP00000009984

Chemistry databases

BindingDBiP15381
ChEMBLiCHEMBL2830

PTM databases

iPTMnetiP15381

Proteomic databases

PRIDEiP15381

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100101555
KEGGiocu:100101555

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
775

Phylogenomic databases

InParanoidiP15381
KOiK04850
OrthoDBi172471at2759

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, 2 hits
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_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: P15381
Secondary accession number(s): Q03716, Q28676, Q99243
<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: April 1, 1990
Last sequence update: April 1, 1990
Last modified: May 8, 2019
This is version 153 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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