CACNA1C
entrez
775
canonical
uniprot
Q13936
canonical
ensembl
ENSG00000151067
resolver
ensembl
ENSG00000285479
resolver
ensp
ENSP00000266376
resolver
ensp
ENSP00000329877
resolver
ensp
ENSP00000336982
resolver
ensp
ENSP00000341092
resolver
ensp
ENSP00000382500
resolver
ensp
ENSP00000382504
resolver
ensp
ENSP00000382506
resolver
ensp
ENSP00000382510
resolver
ensp
ENSP00000382512
resolver
ensp
ENSP00000382515
resolver
ensp
ENSP00000382526
resolver
ensp
ENSP00000382530
resolver
ensp
ENSP00000382537
resolver
ensp
ENSP00000382542
resolver
ensp
ENSP00000382546
resolver
ensp
ENSP00000382547
resolver
ensp
ENSP00000382549
resolver
ensp
ENSP00000382552
resolver
ensp
ENSP00000382557
resolver
ensp
ENSP00000382563
resolver
ensp
ENSP00000385724
resolver
ensp
ENSP00000494109
resolver
ensp
ENSP00000494149
resolver
ensp
ENSP00000495321
resolver
ensp
ENSP00000506882
resolver
ensp
ENSP00000507105
resolver
ensp
ENSP00000507169
resolver
ensp
ENSP00000507184
resolver
ensp
ENSP00000507309
resolver
ensp
ENSP00000507434
resolver
ensp
ENSP00000507612
resolver
ensp
ENSP00000507867
resolver
ensp
ENSP00000518304
resolver
ensp
ENSP00000518353
resolver
ensp
ENSP00000518362
resolver
ensp
ENSP00000518363
resolver
ensp
ENSP00000518365
resolver
enst
ENST00000327702
resolver
enst
ENST00000335762
resolver
enst
ENST00000399617
resolver
enst
ENST00000399634
resolver
enst
ENST00000642375
resolver
enst
ENST00000646280
resolver
enst
ENST00000647229
resolver
enst
ENST00000682462
resolver
enst
ENST00000683781
resolver
enst
ENST00000683824
resolver
enst
ENST00000683956
resolver
enst
ENST00000710478
resolver
enst
ENST00000710582
resolver
enst
ENST00000710592
resolver
enst
ENST00000710593
resolver
enst
ENST00000710595
resolver
genesymbol
CACNA1C
resolver
genesymbol_syn
CACH2
resolver
genesymbol_syn
CACN2
resolver
genesymbol_syn
CACNL1A1
resolver
genesymbol_syn
CCHL1A1
resolver
hgnc
HGNC:1390
resolver
uniprot
A0A0A0MR67
resolver
uniprot
A0A0A0MSA1
resolver
uniprot
A0A804HI37
resolver
uniprot
A0A804HIJ8
resolver
uniprot
A0A804HJB6
resolver
uniprot
A0A804HKC4
resolver
uniprot
B2RUT3
resolver
uniprot
E9PDI6
resolver
uniprot
E9PDJ0
resolver
uniprot
F5H522
resolver
uniprot
Q13917
resolver
uniprot
Q13918
resolver
uniprot
Q13919
resolver
uniprot
Q13920
resolver
uniprot
Q13921
resolver
uniprot
Q13922
resolver
uniprot
Q13923
resolver
uniprot
Q13924
resolver
uniprot
Q13925
resolver
uniprot
Q13926
resolver
uniprot
Q13927
resolver
uniprot
Q13928
resolver
uniprot
Q13929
resolver
uniprot
Q13930
resolver
uniprot
Q13932
resolver
uniprot
Q13933
resolver
uniprot
Q14743
resolver
uniprot
Q14744
resolver
uniprot
Q15877
resolver
uniprot
Q4VMI7
resolver
uniprot
Q4VMI8
resolver
uniprot
Q4VMI9
resolver
uniprot
Q59GU3
resolver
uniprot
Q5V9X9
resolver
uniprot
Q6PKM7
resolver
uniprot
Q8N6C0
resolver
uniprot
Q99025
resolver
uniprot
Q99241
resolver
uniprot
Q99875
resolver
uniprot_entry
A0A0A0MR67_HUMAN
resolver
uniprot_entry
A0A0A0MSA1_HUMAN
resolver
uniprot_entry
A0A804HI37_HUMAN
resolver
uniprot_entry
A0A804HIJ8_HUMAN
resolver
uniprot_entry
A0A804HJB6_HUMAN
resolver
uniprot_entry
A0A804HKC4_HUMAN
resolver
uniprot_entry
CAC1C_HUMAN
resolver
uniprot_entry
E9PDI6_HUMAN
resolver
uniprot_entry
F5H522_HUMAN
resolver
uniprot_entry
Q59GU3_HUMAN
resolver
uniprot_entry
Q5V9X9_HUMAN
resolver
uniprot_sec
B2RUT3
resolver
uniprot_sec
E9PDJ0
resolver
uniprot_sec
Q13917
resolver
uniprot_sec
Q13918
resolver
uniprot_sec
Q13919
resolver
uniprot_sec
Q13920
resolver
uniprot_sec
Q13921
resolver
uniprot_sec
Q13922
resolver
uniprot_sec
Q13923
resolver
uniprot_sec
Q13924
resolver
uniprot_sec
Q13925
resolver
uniprot_sec
Q13926
resolver
uniprot_sec
Q13927
resolver
uniprot_sec
Q13928
resolver
uniprot_sec
Q13929
resolver
uniprot_sec
Q13930
resolver
uniprot_sec
Q13932
resolver
uniprot_sec
Q13933
resolver
uniprot_sec
Q14743
resolver
uniprot_sec
Q14744
resolver
uniprot_sec
Q15877
resolver
uniprot_sec
Q4VMI7
resolver
uniprot_sec
Q4VMI8
resolver
uniprot_sec
Q4VMI9
resolver
uniprot_sec
Q6PKM7
resolver
uniprot_sec
Q8N6C0
resolver
uniprot_sec
Q99025
resolver
uniprot_sec
Q99241
resolver
uniprot_sec
Q99875
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by dihydropyridines (DHP), such as isradipine (PubMed:7737988, PubMed:8099908, PubMed:8392192, PubMed:9607315). Inhibited by nifedipine (By similarity). Selectively inhibited by the snake venom calciseptine (PubMed:37972591). Inhibited by pinaverium bromide (PIN) (PubMed:37972591). Channel activity is regulated by Ca(2+) and calmodulin (Probable) (PubMed:29742403). Binding of STAC1, STAC2 or STAC3 to a region that overlaps with the calmodulin binding site inhibits channel inactivation by Ca(2+) and calmodulin (PubMed:29078335). Binding of calmodulin or CABP1 at the same regulatory sites results in opposite effects on the channel function (PubMed:15140941, PubMed:15980432). Shear stress and pressure increases calcium channel activity (PubMed:12176756). {ECO:0000250|UniProtKB:P15381, ECO:0000269|PubMed:12176756, ECO:0000269|PubMed:15140941, ECO:0000269|PubMed:15980432, ECO:0000269|PubMed:29078335, ECO:0000269|PubMed:29742403, ECO:0000269|PubMed:7737988, ECO:0000269|PubMed:8099908, ECO:0000269|PubMed:8392192, ECO:0000269|PubMed:9607315, ECO:0000305|PubMed:16299511}.
uniprot
proteins
amino_acid_sequence
MVNENTRMYIPEENHQGSNYGSPRPAHANMNANAAAGLAPEHIPTPGAALSWQAAIDAARQAKLMGSAGNATISTVSSTQRKRQQYGKPKKQGSTTATRPPRALLCLTLKNPIRRACISIVEWKPFEIIILLTIFANCVALAIYIPFPEDDSNATNSNLERVEYLFLIIFTVEAFLKVIAYGLLFHPNAYLRNGWNLLDFIIVVVGLFSAILEQATKADGANALGGKGAGFDVKALRAFRVLRPLRLVSGVPSLQVVLNSIIKAMVPLLHIALLVLFVIIIYAIIGLELFMGKMHKTCYNQEGIADVPAEDDPSPCALETGHGRQCQNGTVCKPGWDGPKHGITNFDNFAFAMLTVFQCITMEGWTDVLYWVNDAVGRDWPWIYFVTLIIIGSFFVLNLVLGVLSGEFSKEREKAKARGDFQKLREKQQLEEDLKGYLDWITQAEDIDPENEDEGMDEEKPRNMSMPTSETESVNTENVAGGDIEGENCGARLAHRISKSKFSRYWRRWNRFCRRKCRAAVKSNVFYWLVIFLVFLNTLTIASEHYNQPNWLTEVQDTANKALLALFTAEMLLKMYSLGLQAYFVSLFNRFDCFVVCGGILETILVETKIMSPLGISVLRCVRLLRIFKITRYWNSLSNLVASLLNSVRSIASLLLLLFLFIIIFSLLGMQLFGGKFNFDEMQTRRSTFDNFPQSLLTVFQILTGEDWNSVMYDGIMAYGGPSFPGMLVCIYFIILFICGNYILLNVFLAIAVDNLADAESLTSAQKEEEEEKERKKLARTASPEKKQELVEKPAVGESKEEKIELKSITADGESPPATKINMDDLQPNENEDKSPYPNPETTGEEDEEEPEMPVGPRPRPLSELHLKEKAVPMPEASAFFIFSSNNRFRLQCHRIVNDTIFTNLILFFILLSSISLAAEDPVQHTSFRNHILFYFDIVFTTIFTIEIALKILGNADYVFTSIFTLEIILKMTAYGAFLHKGSFCRNYFNILDLLVVSVSLISFGIQSSAINVVKILRVLRVLRPLRAINRAKGLKHVVQCVFVAIRTIGNIVIVTTLLQFMFACIGVQLFKGKLYTCSDSSKQTEAECKGNYITYKDGEVDHPIIQPRSWENSKFDFDNVLAAMMALFTVSTFEGWPELLYRSIDSHTEDKGPIYNYRVEISIFFIIYIIIIAFFMMNIFVGFVIVTFQEQGEQEYKNCELDKNQRQCVEYALKARPLRRYIPKNQHQYKVWYVVNSTYFEYLMFVLILLNTICLAMQHYGQSCLFKIAMNILNMLFTGLFTVEMILKLIAFKPKGYFSDPWNVFDFLIVIGSIIDVILSETNHYFCDAWNTFDALIVVGSIVDIAITEVNPAEHTQCSPSMNAEENSRISITFFRLFRVMRLVKLLSRGEGIRTLLWTFIKSFQALPYVALLIVMLFFIYAVIGMQVFGKIALNDTTEINRNNNFQTFPQAVLLLFRCATGEAWQDIMLACMPGKKCAPESEPSNSTEGETPCGSSFAVFYFISFYMLCAFLIINLFVAVIMDNFDYLTRDWSILGPHHLDEFKRIWAEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKLCPHRVACKRLVSMNMPLNSDGTVMFNATLFALVRTALRIKTEGNLEQANEELRAIIKKIWKRTSMKLLDQVVPPAGDDEVTVGKFYATFLIQEYFRKFKKRKEQGLVGKPSQRNALSLQAGLRTLHDIGPEIRRAISGDLTAEEELDKAMKEAVSAASEDDIFRRAGGLFGNHVSYYQSDGRSAFPQTFTTQRPLHINKAGSSQGDTESPSHEKLVDSTFTPSSYSSTGSNANINNANNTALGRLPRPAGYPSTVSTVEGHGPPLSPAIRVQEVAWKLSSNRERHVPMCEDLELRRDSGSAGTQAHCLLLRKANPSRCHSRESQAAMAGQEETSQDETYEVKMNHDTEACSEPSLLSTEMLSYQDDENRQLTLPEEDKRDIRQSPKRGFLRSASLGRRASFHLECLKRQKDRGGDISQKTVLPLHLVHHQALAVAGLSPLLQRSHSPASFPRPFATPPATPGSRGWPPQPVPTLRLEGVESSEKLNSSFPSIHCGSWAETTPGGGGSSAARRVRPVSLMVPSQAGAPGRQFHGSASSLVEAVLISEGLGQFAQDPKFIEVTTQELADACDMTIEEMESAADNILSGGAPQSPNGALLPFVNCRDAGQDRAGGEEDAGCVRARGRPSEEELQDSRVYVSSL
uniprot
proteins
disease_involvement
DISEASE: Timothy syndrome (TS) [MIM:601005]: Disorder characterized by multiorgan dysfunction including lethal arrhythmias, webbing of fingers and toes, congenital heart disease, immune deficiency, intermittent hypoglycemia, cognitive abnormalities and autism. {ECO:0000269|PubMed:15454078, ECO:0000269|PubMed:15863612, ECO:0000269|PubMed:25260352, ECO:0000269|PubMed:26253506, ECO:0000269|PubMed:30023270, ECO:0000269|PubMed:30172029, ECO:0000269|PubMed:31430211, ECO:0000269|PubMed:8099908}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Brugada syndrome 3 (BRGDA3) [MIM:611875]: A heart disease characterized by the association of Brugada syndrome with shortened QT intervals. Brugada syndrome is a tachyarrhythmia characterized by right bundle branch block and ST segment elevation on an electrocardiogram (ECG). It can cause the ventricles to beat so fast that the blood is prevented from circulating efficiently in the body. When this situation occurs, the individual will faint and may die in a few minutes if the heart is not reset. {ECO:0000269|PubMed:17224476, ECO:0000269|PubMed:20817017}. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Long QT syndrome 8 (LQT8) [MIM:618447]: A form of long QT syndrome, a heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy. LQT8 transmission pattern is consistent with autosomal dominant inheritance with incomplete penetrance. {ECO:0000269|PubMed:23677916, ECO:0000269|PubMed:24728418, ECO:0000269|PubMed:25633834, ECO:0000269|PubMed:30345660}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Neurodevelopmental disorder with hypotonia, language delay, and skeletal defects with or without seizures (NEDHLSS) [MIM:620029]: An autosomal dominant disorder characterized by global developmental delay apparent from infancy, intellectual disability, poor or absent speech, behavioral abnormalities, and hypotonia with delayed walking or inability to walk. Additional features include epilepsy, mild skeletal defects, and non-specific dysmorphic features. {ECO:0000269|PubMed:30513141, ECO:0000269|PubMed:34163037}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents (PubMed:12181424, PubMed:15454078, PubMed:15863612, PubMed:16299511, PubMed:17224476, PubMed:20953164, PubMed:23677916, PubMed:24728418, PubMed:26253506, PubMed:27218670, PubMed:29078335, PubMed:29742403, PubMed:30023270, PubMed:30172029, PubMed:34163037, PubMed:8099908). 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. Required for normal heart development and normal regulation of heart rhythm (PubMed:15454078, PubMed:15863612, PubMed:17224476, PubMed:24728418, PubMed:26253506). 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 (PubMed:28119464). Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group (Probable). {ECO:0000250|UniProtKB:P15381, ECO:0000269|PubMed:12181424, ECO:0000269|PubMed:15454078, ECO:0000269|PubMed:15863612, ECO:0000269|PubMed:16299511, ECO:0000269|PubMed:17224476, ECO:0000269|PubMed:20953164, ECO:0000269|PubMed:23677916, ECO:0000269|PubMed:24728418, ECO:0000269|PubMed:25260352, ECO:0000269|PubMed:25633834, ECO:0000269|PubMed:26253506, ECO:0000269|PubMed:27218670, ECO:0000269|PubMed:28119464, ECO:0000269|PubMed:29078335, ECO:0000269|PubMed:29742403, ECO:0000269|PubMed:30023270, ECO:0000269|PubMed:30172029, ECO:0000269|PubMed:31430211, ECO:0000269|PubMed:34163037, ECO:0000269|PubMed:8099908, ECO:0000305}.; FUNCTION: [Isoform 12]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:12176756, ECO:0000269|PubMed:7737988}.; FUNCTION: [Isoform 13]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:17071743}.; FUNCTION: [Isoform 14]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:17071743}.; FUNCTION: [Isoform 15]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:17071743}.; FUNCTION: [Isoform 16]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:9087614}.; FUNCTION: [Isoform 17]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:9087614}.; FUNCTION: [Isoform 18]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:8392192}.; FUNCTION: [Isoform 19]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:7737988}.; FUNCTION: [Isoform 20]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:7737988}.; FUNCTION: [Isoform 21]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:9607315}.; FUNCTION: [Isoform 22]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:9607315}.; FUNCTION: [Isoform 23]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:9607315}.; FUNCTION: [Isoform 24]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:17071743}.; FUNCTION: [Isoform 25]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:17071743}.; FUNCTION: [Isoform 26]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:9013606}.; FUNCTION: [Isoform 27]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:9013606}.; FUNCTION: [Isoform 34]: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. {ECO:0000269|PubMed:11741969}.; FUNCTION: (Microbial infection) Acts as a receptor for Influenzavirus (PubMed:29779930). May play a critical role in allowing virus entry when sialylated and expressed on lung tissues (PubMed:29779930). {ECO:0000269|PubMed:29779930}.
uniprot
proteins
mass_dalton
248977
uniprot
proteins
mutagenesis
MUTAGEN 363; /note="E->K: Loss of selectivity for divalent over monovalent cations."; /evidence="ECO:0000269|PubMed:8099908"; MUTAGEN 954; /note="G->F: Affects voltage-dependent inhibition by dihydropyridines; when associated with I-958."; /evidence="ECO:0000269|PubMed:7737988"; MUTAGEN 958; /note="Y->I: Affects voltage-dependent inhibition by dihydropyridines; when associated with F-954."; /evidence="ECO:0000269|PubMed:7737988"; MUTAGEN 1135; /note="E->Q: Decreased selectivity for divalent over monovalent cations."; /evidence="ECO:0000269|PubMed:8099908"; MUTAGEN 1464; /note="E->A: Decreased selectivity for divalent over monovalent cations."; /evidence="ECO:0000269|PubMed:8099908"; MUTAGEN 1610; /note="L->A: Loss of a low-affinity interaction with CALM1. No effect on channel inactivation by Ca(2+) and calmodulin."; /evidence="ECO:0000269|PubMed:20953164"; MUTAGEN 1666..1670; /note="FYATF->AAATA: Mildly decreased channel activity. No effect on channel inactivation. Loss of channel inactivation by Ca(2+) and calmodulin; when associated with A-1672."; /evidence="ECO:0000269|PubMed:16299511"; MUTAGEN 1672; /note="I->A: Loss of channel inactivation by Ca(2+) and calmodulin; when associated with 1666-A--A-1670."; /evidence="ECO:0000269|PubMed:16299511
uniprot
proteins
post_translational_modification
PTM: Phosphorylation by PKA at Ser-1981 activates the channel. Elevated levels of blood glucose lead to increased phosphorylation by PKA. {ECO:0000269|PubMed:28119464}.
uniprot
proteins
protein_family
CACNA1C subfamily
uniprot
proteins
protein_family
Calcium channel alpha-1 subunit (TC 1.A.1.11) family
uniprot
proteins
pubmed
11741969
uniprot
proteins
pubmed
12176756
uniprot
proteins
pubmed
12181424
uniprot
proteins
pubmed
1316612
uniprot
proteins
pubmed
1335957
uniprot
proteins
pubmed
15140941
uniprot
proteins
pubmed
15141227
uniprot
proteins
pubmed
15454078
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15863612
uniprot
proteins
pubmed
15980432
uniprot
proteins
pubmed
16299511
uniprot
proteins
pubmed
16338416
uniprot
proteins
pubmed
1653763
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
17071743
uniprot
proteins
pubmed
17224476
uniprot
proteins
pubmed
19279214
uniprot
proteins
pubmed
20817017
uniprot
proteins
pubmed
20953164
uniprot
proteins
pubmed
21248752
uniprot
proteins
pubmed
2173707
uniprot
proteins
pubmed
22518098
uniprot
proteins
pubmed
23677916
uniprot
proteins
pubmed
24728418
uniprot
proteins
pubmed
25260352
uniprot
proteins
pubmed
25633834
uniprot
proteins
pubmed
26253506
uniprot
proteins
pubmed
26637798
uniprot
proteins
pubmed
27218670
uniprot
proteins
pubmed
28119464
uniprot
proteins
pubmed
29078335
uniprot
proteins
pubmed
29742403
uniprot
proteins
pubmed
29779930
uniprot
proteins
pubmed
30023270
uniprot
proteins
pubmed
30172029
uniprot
proteins
pubmed
30345660
uniprot
proteins
pubmed
30513141
uniprot
proteins
pubmed
31430211
uniprot
proteins
pubmed
34163037
uniprot
proteins
pubmed
34522029
uniprot
proteins
pubmed
37972591
uniprot
proteins
pubmed
7737988
uniprot
proteins
pubmed
7959794
uniprot
proteins
pubmed
8099908
uniprot
proteins
pubmed
8392192
uniprot
proteins
pubmed
9013606
uniprot
proteins
pubmed
9087614
uniprot
proteins
pubmed
9607315
uniprot
proteins
sequence_length
2221
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11741969, ECO:0000269|PubMed:12176756, ECO:0000269|PubMed:12181424, ECO:0000269|PubMed:15454078, ECO:0000269|PubMed:15863612, ECO:0000269|PubMed:16299511, ECO:0000269|PubMed:17071743, ECO:0000269|PubMed:17224476, ECO:0000269|PubMed:20953164, ECO:0000269|PubMed:24728418, ECO:0000269|PubMed:26253506, ECO:0000269|PubMed:27218670, ECO:0000269|PubMed:29078335, ECO:0000269|PubMed:29742403, ECO:0000269|PubMed:7737988, ECO:0000269|PubMed:8099908, ECO:0000269|PubMed:8392192, ECO:0000269|PubMed:9013606, ECO:0000269|PubMed:9087614, ECO:0000269|PubMed:9607315}; Multi-pass membrane protein {ECO:0000305}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P15381}; Multi-pass membrane protein {ECO:0000305}. Perikaryon {ECO:0000250|UniProtKB:P22002}. Postsynaptic density membrane {ECO:0000250|UniProtKB:P22002}. Cell projection, dendrite {ECO:0000250|UniProtKB:P22002}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:Q01815}. Note=Colocalizes with ryanodine receptors in distinct clusters at the junctional membrane, where the sarcolemma and the sarcoplasmic reticulum are in close contact. The interaction between RRAD and CACNB2 promotes the expression of CACNA1C at the cell membrane. {ECO:0000250|UniProtKB:P15381}.
uniprot
proteins
transmembrane_region
TRANSMEM 125..143; /note="Helical; Name=S1 of repeat I"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 159..179; /note="Helical; Name=S2 of repeat I"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 189..209; /note="Helical; Name=S3 of repeat I"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 233..251; /note="Helical; Name=S4 of repeat I"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 269..290; /note="Helical; Name=S5 of repeat I"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 381..401; /note="Helical; Name=S6 of repeat I"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 525..543; /note="Helical; Name=S1 of repeat II"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 555..575; /note="Helical; Name=S2 of repeat II"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 587..606; /note="Helical; Name=S3 of repeat II"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 616..634; /note="Helical; Name=S4 of repeat II"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 654..673; /note="Helical; Name=S5 of repeat II"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 726..745; /note="Helical; Name=S6 of repeat II"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 901..919; /note="Helical; Name=S1 of repeat III"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 932..952; /note="Helical; Name=S2 of repeat III"; /evidence="ECO:0000255"; TRANSMEM 988..1006; /note="Helical; Name=S3 of repeat III"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1014..1032; /note="Helical; Name=S4 of repeat III"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1052..1071; /note="Helical; Name=S5 of repeat III"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1160..1181; /note="Helical; Name=S6 of repeat III"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1240..1261; /note="Helical; Name=S1 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1270..1291; /note="Helical; Name=S2 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1302..1321; /note="Helical; Name=S3 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1373..1391; /note="Helical; Name=S4 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1410..1430; /note="Helical; Name=S5 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P07293"; TRANSMEM 1500..1524; /note="Helical; Name=S6 of repeat IV"; /evidence="ECO:0000250|UniProtKB:P07293
uniprot
proteins