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Entry version 108 (07 Apr 2021)
Sequence version 2 (10 Feb 2021)
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Protein

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

Gene

CACNA1C

Organism
Cavia porcellus (Guinea pig)
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 transcript 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:10101289). 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 (By similarity). 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 Publication

<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

Inhibited by dihydropyridines (DHP), such as isradipine (By similarity). Inhibited by nifedipine (PubMed:10101289). Channel activity is regulated by Ca2+ and calmodulin (By similarity). 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 (By similarity). 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%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 bindingi392CalciumBy 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>Sitei392Calcium ion selectivity and permeabilityBy similarity1
Metal bindingi735CalciumBy similarity1
Sitei735Calcium 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%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 bindingi1534 – 1545CuratedAdd 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%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-1C
Alternative name(s):
Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle
Voltage-gated calcium channel subunit alpha Cav1.2
<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:CACNA1C
Synonyms:CACH2, CACN2, CACNL1A1, CCHL1A1
<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>OrganismiCavia porcellus (Guinea pig)
<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 identifieri10141 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricomorphaCaviidaeCavia
<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
  • UP000005447 <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: Unassembled WGS sequence

<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 – 153CytoplasmicCuratedAdd BLAST153
<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>Transmembranei154 – 172Helical; Name=S1 of repeat IBy similarityAdd BLAST19
Topological domaini173 – 187ExtracellularCuratedAdd BLAST15
Transmembranei188 – 208Helical; Name=S2 of repeat IBy similarityAdd BLAST21
Topological domaini209 – 217CytoplasmicCurated9
Transmembranei218 – 238Helical; Name=S3 of repeat IBy similarityAdd BLAST21
Topological domaini239 – 261ExtracellularCuratedAdd BLAST23
Transmembranei262 – 280Helical; Name=S4 of repeat IBy similarityAdd BLAST19
Topological domaini281 – 297CytoplasmicCuratedAdd BLAST17
Transmembranei298 – 319Helical; Name=S5 of repeat IBy similarityAdd BLAST22
Topological domaini320 – 379ExtracellularCuratedAdd BLAST60
<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>Intramembranei380 – 401Pore-formingBy similarityAdd BLAST22
Topological domaini402 – 409ExtracellularCurated8
Transmembranei410 – 430Helical; Name=S6 of repeat IBy similarityAdd BLAST21
Topological domaini431 – 553CytoplasmicCuratedAdd BLAST123
Transmembranei554 – 572Helical; Name=S1 of repeat IIBy similarityAdd BLAST19
Topological domaini573 – 583ExtracellularCuratedAdd BLAST11
Transmembranei584 – 604Helical; Name=S2 of repeat IIBy similarityAdd BLAST21
Topological domaini605 – 615CytoplasmicCuratedAdd BLAST11
Transmembranei616 – 635Helical; Name=S3 of repeat IIBy similarityAdd BLAST20
Topological domaini636 – 644ExtracellularCurated9
Transmembranei645 – 663Helical; Name=S4 of repeat IIBy similarityAdd BLAST19
Topological domaini664 – 682CytoplasmicCuratedAdd BLAST19
Transmembranei683 – 702Helical; Name=S5 of repeat IIBy similarityAdd BLAST20
Topological domaini703 – 722ExtracellularCuratedAdd BLAST20
Intramembranei723 – 744Pore-formingBy similarityAdd BLAST22
Topological domaini745 – 754ExtracellularCurated10
Transmembranei755 – 774Helical; Name=S6 of repeat IIBy similarityAdd BLAST20
Topological domaini775 – 929CytoplasmicCuratedAdd BLAST155
Transmembranei930 – 948Helical; Name=S1 of repeat IIIBy similarityAdd BLAST19
Topological domaini949 – 960ExtracellularCuratedAdd BLAST12
Transmembranei961 – 980Helical; Name=S2 of repeat IIIBy similarityAdd BLAST20
Topological domaini981 – 996CytoplasmicCuratedAdd BLAST16
Transmembranei997 – 1015Helical; Name=S3 of repeat IIIBy similarityAdd BLAST19
Topological domaini1016 – 1022ExtracellularCurated7
Transmembranei1023 – 1041Helical; Name=S4 of repeat IIIBy similarityAdd BLAST19
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
CHEMBL2366456

DrugCentral

More...
DrugCentrali
O35505

<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_00000539271 – 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%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>Glycosylationi182N-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 bondi345 ↔ 361By similarity
Glycosylationi357N-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 residuei498PhosphoserineBy similarity1
Modified residuei505PhosphothreonineBy similarity1
Modified residuei837PhosphoserineBy similarity1
Modified residuei844PhosphoserineBy similarity1
Disulfide bondi1087 ↔ 1098By similarity
Glycosylationi1417N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1460 ↔ 1476By similarity
Glycosylationi1468N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei1699PhosphoserineBy similarity1
Modified residuei1720PhosphoserineBy similarity1
Modified residuei1927PhosphoserineBy similarity1

<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

Phosphorylation by PKA at Ser-1927 activates the channel. Elevated levels of blood glucose lead to increased phosphorylation by PKA.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

<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

Expressed in heart (PubMed:10101289). Expressed in uterus (PubMed:11058528).2 Publications

<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

During gestation, expression in the uterus is relatively constant between 34 and 47 days, increases by approximately threefold relative to the expression level of 34 days by 54 days and persists at the elevated levels through term.1 Publication

<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 (CACNA1C) and ancillary beta, gamma and delta subunits. 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).

Interacts with CACNB1 (By similarity).

Interacts with CACNB2.

Identified in a complex with CACNA2D4 and CACNB3.

Interacts with CACNB3.

Interacts with CACNA2D1.

Interacts with CACNA2D4 (By similarity).

Interacts with the gamma subunits CACNG4, CACNG6, CACNG7 and CACNG8 (By similarity).

Interacts with CALM1.

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

By similarity

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
O35505, 2 interactors

Molecular INTeraction database

More...
MINTi
Q9Z305

STRING: functional protein association networks

More...
STRINGi
10141.ENSCPOP00000009195

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
O35505

<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

3D structure databases

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

More...
SMRi
O35505

Database of comparative protein structure models

More...
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>Repeati140 – 437ICuratedAdd BLAST298
Repeati539 – 785IICuratedAdd BLAST247
Repeati916 – 1198IIICuratedAdd BLAST283
Repeati1235 – 1508IVCuratedAdd 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>Regioni76 – 97Calmodulin-bindingBy similarityAdd BLAST22
Regioni457 – 474AID/alpha-interaction domain; mediates interaction with the beta subunitBy similarityAdd BLAST18
Regioni858 – 905Interaction with STAC2By similarityAdd BLAST48
Regioni1118 – 1207Dihydropyridine bindingBy similarityAdd BLAST90
Regioni1459 – 1527Dihydropyridine bindingBy similarityAdd BLAST69
Regioni1473 – 1515Phenylalkylamine bindingBy similarityAdd BLAST43
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>Motifi390 – 393Selectivity filter of repeat IBy similarity4
Motifi733 – 736Selectivity filter of repeat IIBy similarity4
Motifi1142 – 1145Selectivity filter of repeat IIIBy similarity4
Motifi1443 – 1446Selectivity filter of repeat IVBy similarity4

<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

More...
eggNOGi
KOG2301, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O35505

Identification of Orthologs from Complete Genome Data

More...
OMAi
KQPQWLT

Database of Orthologous Groups

More...
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%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>Sequences (2)i

<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.

This entry describes 2 <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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: O35505-1) [UniParc]FASTAAdd to basket

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
MVPLVQPTTP AYRPLPSHLS ADTEVRGRGT LVHEAQLNCF YISPGGSNYG
60 70 80 90 100
SPRPAHANIN ANAAAGLAPE HIPTPGAALS WQAAIDAGRQ AKLMGSAGNT
110 120 130 140 150
TISTVSSTQR KRQQYGKPKK QSGTTATRPP RALLCLTLKN PIRRACISIV
160 170 180 190 200
EWKPFEIIIL LTIFANCVAL AIYIPFPEDD SNATNSNLER VEYLFLIIFT
210 220 230 240 250
VEAFLKVIAY GLLFHPNAYL RNGWNLLDFI IVVVGLFSAI LEQATKADGA
260 270 280 290 300
NALGGKGAGF DVKALRAFRV LRPLRLVSGV PSLQVVLNSI IKAMVPLLHT
310 320 330 340 350
ALLVLFVIII YAIIGLELFM GKMHKTCYNQ EGITDVPAEE DPSPCALESG
360 370 380 390 400
HGRQCQNGTV CKPGWDGPKH GITNFDNFAF AMLTVFQCIT MEGWTDVLYW
410 420 430 440 450
MQDAMGYELP WVYFVSLVIF GSFFVLNLVL GVLSGEFSKE REKAKARGDF
460 470 480 490 500
QKLREKQQLE EDLKGYLDWI TQAEDIDPEN EDEGVDEEKP RNMSMPTSET
510 520 530 540 550
ESVNTENVAG GDIEGENCGA RLAHRISKSK FSRYWRRWNR FCRRKCRAAV
560 570 580 590 600
KSNVFYWLVI FLVFLNTLTI ASEHYNQPHW LTEVQDTANK ALLALFTAEM
610 620 630 640 650
LLKMYSLGLQ AYFVSLFNRL DCFIVCGGIL ETILVETKIM SPLGISVLRC
660 670 680 690 700
VRLLRIFKIT RYWNSLSNLV ASLLNSVRSI ASLLLLLFLF IIIFSLLGMQ
710 720 730 740 750
LFGGKFNFDE MRTRRSTFDN FPQSLLTVFQ ILTGEDWNSV MYDGIMAYGG
760 770 780 790 800
PSFPGMLVCI YFIILFICGN YILLNVFLAI AVDNLADAES LTSAQKEEEE
810 820 830 840 850
EKERKKLART ASPEKKQEVV EKPAVEETKE EKIELKSITA DGESPPTTKI
860 870 880 890 900
NMDDLQPNEN EDKSPYPNPD AAGEEDEEEP EMPVGPRPRP LSELHLKEKA
910 920 930 940 950
VPMPEASAFF IFSPNNRFRL QCHRIVNDTI FTNLILFFIL LSSISLAAED
960 970 980 990 1000
PVQHTSFRNH ILFYFDIVFT TIFTIEIALK MTAYGAFLHK GSFCRNYFNI
1010 1020 1030 1040 1050
LDLLVVSVSL ISFGIQSSAI NVVKILRVLR VLRPLRAINR AKGLKHVVQC
1060 1070 1080 1090 1100
VFVAIRTIGN IVIVTTLLQF MFACIGVQLF KGKLYTCSDS SKQTEAECKG
1110 1120 1130 1140 1150
NYITYKDGEV DQPIIQPRSW ENSKFDFDNV LAAMMALFTV STFEGWPELL
1160 1170 1180 1190 1200
YRSIDSHTED KGPIYNYRVE ISIFFIIYII IIAFFMMNIF VGFVIVTFQE
1210 1220 1230 1240 1250
QGEQEYKNCE LDKNQRQCVE YALKARPLRR YIPKNQHQYK VWYVVNSTYF
1260 1270 1280 1290 1300
EYLMFVLILL NTICLAMQHY GQSCLFKIAM NILNMLFTGL FTVEMILKLI
1310 1320 1330 1340 1350
AFKPKHYFCD AWNTFDALIV VGSIVDIAIT EVNPAEHTQC SPSMNAEENS
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 APESDPSNST EGETPCGSSF AVFYFISFYM LCAFLIINLF
1510 1520 1530 1540 1550
VAVVMDNFDY LTRDWSILGP HHLDEFKRIW AEYDPEAKGR IKHLDVVTLL
1560 1570 1580 1590 1600
RRIQPPLGFG KLCPHRVACK RLVSMNMPLN SDGTAMFNAT 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 EDDIFGRAGG LFGNHVSYYQ SDSRSTFPQT
1760 1770 1780 1790 1800
FTTQRPLHIN KAGNNQGDTE SPSHEKLVDS TFTPSSYSST GSNANINNAN
1810 1820 1830 1840 1850
NTALGRFPHP AGYPSTVSTV EGHRPPSSPA TWAQEATRKL GAMRCHSRES
1860 1870 1880 1890 1900
QIAVVCQEEP SQDKTYDVEL NKDAEYCSEP SLLSTEMLSY KDDENRQLTP
1910 1920 1930 1940 1950
PEEDKGDTRP SPKKGFLRSA SLGRRASFHL ECLKRQKNHG GDISQKTVLP
1960 1970 1980 1990 2000
LHLVHHQALA VAGLSPLLQR SHSPTAIPRP CATPPATPGS RGWPPKPIPT
2010 2020 2030 2040 2050
LRLEGAESCE KLNSSFPSIH CSSWSEEPSP CGGGSSAARR ARPVSLMVPS
2060 2070 2080 2090 2100
QAGAPGRQFH GSASSLAEAV LISEGLGQFA QDPKFIEVTT QELADACDMT
2110 2120 2130 2140 2150
IGEMENAADN ILSGGAPQSP NGTLLPFVNC RDPGQDRAGG DEDEGCACAL
2160
GRGWSEEELA DSRVHVRSL
Length:2,169
Mass (Da):242,638
Last modified:February 10, 2021 - v2
<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:i8B212C3D74ED2DC3
GO
Isoform 2 (identifier: O35505-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1234-1352: KNQHQYKVWY...SMNAEENSRI → I

Show »
Length:2,051
Mass (Da):229,005
Checksum:i72A9DEF3DC96EE37
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 conflicti1460C → R in AAB62890 (PubMed:11058528).Curated1
Sequence conflicti1465D → E in AAB62890 (PubMed:11058528).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_0609071234 – 1352KNQHQ…ENSRI → I in isoform 2. CuratedAdd BLAST119

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
AB016287 mRNA Translation: BAA34185.2
AF005938 mRNA Translation: AAB62890.1

NCBI Reference Sequences

More...
RefSeqi
NP_001166394.1, NM_001172923.1 [O35505-1]

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
100135490

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
AB016287 mRNA Translation: BAA34185.2
AF005938 mRNA Translation: AAB62890.1
RefSeqiNP_001166394.1, NM_001172923.1 [O35505-1]

3D structure databases

SMRiO35505
ModBaseiSearch...

Protein-protein interaction databases

IntActiO35505, 2 interactors
MINTiQ9Z305
STRINGi10141.ENSCPOP00000009195

Chemistry databases

BindingDBiO35505
ChEMBLiCHEMBL2366456
DrugCentraliO35505

Genome annotation databases

GeneIDi100135490

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
775

Phylogenomic databases

eggNOGiKOG2301, Eukaryota
InParanoidiO35505
OMAiKQPQWLT
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_CAVPO
<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: O35505
Secondary accession number(s): Q9Z305
<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: July 15, 1999
Last sequence update: February 10, 2021
Last modified: April 7, 2021
This is version 108 of the entry and version 2 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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