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P22002 (CAC1C_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Voltage-dependent L-type calcium channel subunit alpha-1C
Alternative name(s):
Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle
Rat brain class C
Short name=RBC
Voltage-gated calcium channel subunit alpha Cav1.2
Gene names
Name:Cacna1c
Synonyms:Cach2, Cacn2, Cacnl1a1, Cchl1a1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length2169 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1C gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to omega-conotoxin-GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing the alpha-1C subunit play an important role in excitation-contraction coupling in the heart. Binding of calmodulin or CABP1 at the same regulatory sites results in an opposit effects on the channel function.

Subunit structure

Voltage-dependent calcium channels are multisubunit complexes, consisting of alpha-1, alpha-2, beta and delta subunits in a 1:1:1:1 ratio. The channel activity is directed by the pore-forming and voltage-sensitive alpha-1 subunit. In many cases, this subunit is sufficient to generate voltage-sensitive calcium channel activity. The auxiliary subunits beta and alpha-2/delta linked by a disulfide bridge regulate the channel activity. Interacts (via C-terminal C and IQ motifs) with CABP1. 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. Interacts with CACNA2D4 By similarity. Interacts (via C-terminal CDB motif) with CABP5; in a calcium-dependent manner By similarity. Ref.8

Subcellular location

Membrane; Multi-pass membrane protein. Cell membrane By similarity. Note: The interaction between RRAD and CACNB2 regulates its trafficking to the cell membrane By similarity.

Tissue specificity

Isoforms 4 and 5 are expressed throughout the central nervous system, with highest levels in the olfactory bulb and cerebellum. Also expressed in heart, pituitary, adrenal gland, liver, kidney, and in a much lesser extent in testes and spleen.

Developmental stage

Expressed from embryonic day 16 until the adult stage.

Domain

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.

Post-translational modification

Phosphorylation by PKA activates the channel Probable. Is also phosphorylated in vitro by CaM-kinase II, PKC and CGPK. Ref.7

Sequence similarities

Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family. CACNA1C subfamily. [View classification]

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 2 (identifier: P22002-1)

Also known as: S3B;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 1 (identifier: P22002-2)

Also known as: S3A;

The sequence of this isoform differs from the canonical sequence as follows:
     1306-1333: HYFCDAWNTFDALIVVGSIVDIAITEVH → GYFSDPSNVFDFLIVIGSIIAVILSETN
Isoform 3 (identifier: P22002-3)

Also known as: D1; ROB2;

The sequence of this isoform differs from the canonical sequence as follows:
     1334-1344: Missing.
Isoform 4 (identifier: P22002-4)

Also known as: rbC-I;

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: MIRAFAQPSTPPYQPLSSCLSEDTERKFKGKVVHEAQLNCFYISPG → MVNENTRMYVPEENHQ
     964-979: FYFDIVFTTIFTIEIA → GNADYVFTSIFTLEII
     1306-1333: HYFCDAWNTFDALIVVGSIVDIAITEVH → GYFSDPSNVFDFLIVIGSIIAVILSETN
Isoform 5 (identifier: P22002-5)

Also known as: rbC-II;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 21692169Voltage-dependent L-type calcium channel subunit alpha-1C
PRO_0000053931

Regions

Topological domain1 – 154154Cytoplasmic Potential
Transmembrane155 – 17319Helical; Name=S1 of repeat I; Potential
Topological domain174 – 19017Extracellular Potential
Transmembrane191 – 21121Helical; Name=S2 of repeat I; Potential
Topological domain212 – 22312Cytoplasmic Potential
Transmembrane224 – 24219Helical; Name=S3 of repeat I; Potential
Topological domain243 – 26220Extracellular Potential
Transmembrane263 – 28119Helical; Name=S4 of repeat I; Potential
Topological domain282 – 30019Cytoplasmic Potential
Transmembrane301 – 32020Helical; Name=S5 of repeat I; Potential
Topological domain321 – 41090Extracellular Potential
Transmembrane411 – 43525Helical; Name=S6 of repeat I; Potential
Topological domain436 – 554119Cytoplasmic Potential
Transmembrane555 – 57319Helical; Name=S1 of repeat II; Potential
Topological domain574 – 58815Extracellular Potential
Transmembrane589 – 60820Helical; Name=S2 of repeat II; Potential
Topological domain609 – 6168Cytoplasmic Potential
Transmembrane617 – 63519Helical; Name=S3 of repeat II; Potential
Topological domain636 – 64510Extracellular Potential
Transmembrane646 – 66419Helical; Name=S4 of repeat II; Potential
Topological domain665 – 68319Cytoplasmic Potential
Transmembrane684 – 70320Helical; Name=S5 of repeat II; Potential
Topological domain704 – 75855Extracellular Potential
Transmembrane759 – 78325Helical; Name=S6 of repeat II; Potential
Topological domain784 – 930147Cytoplasmic Potential
Transmembrane931 – 94919Helical; Name=S1 of repeat III; Potential
Topological domain950 – 96516Extracellular Potential
Transmembrane966 – 98520Helical; Name=S2 of repeat III; Potential
Topological domain986 – 99712Cytoplasmic Potential
Transmembrane998 – 101619Helical; Name=S3 of repeat III; Potential
Topological domain1017 – 10237Extracellular Potential
Transmembrane1024 – 104118Helical; Name=S4 of repeat III; Potential
Topological domain1042 – 106019Cytoplasmic Potential
Transmembrane1061 – 108020Helical; Name=S5 of repeat III; Potential
Topological domain1081 – 117090Extracellular Potential
Transmembrane1171 – 119525Helical; Name=S6 of repeat III; Potential
Topological domain1196 – 124853Cytoplasmic Potential
Transmembrane1249 – 126719Helical; Name=S1 of repeat IV; Potential
Topological domain1268 – 128215Extracellular Potential
Transmembrane1283 – 130220Helical; Name=S2 of repeat IV; Potential
Topological domain1303 – 13108Cytoplasmic Potential
Transmembrane1311 – 132919Helical; Name=S3 of repeat IV; Potential
Topological domain1330 – 135324Extracellular Potential
Transmembrane1354 – 137219Helical; Name=S4 of repeat IV; Potential
Topological domain1373 – 139119Cytoplasmic Potential
Transmembrane1392 – 141120Helical; Name=S5 of repeat IV; Potential
Topological domain1412 – 148069Extracellular Potential
Transmembrane1481 – 150525Helical; Name=S6 of repeat IV; Potential
Topological domain1506 – 2169664Cytoplasmic Potential
Repeat141 – 438298I
Repeat540 – 786247II
Repeat917 – 1198282III
Repeat1235 – 1508274IV
Calcium binding1534 – 154512 By similarity
Region458 – 47518Binding to the beta subunit By similarity
Region1118 – 120891Dihydropyridine binding By similarity
Region1459 – 152769Dihydropyridine binding By similarity
Region1473 – 151644Phenylalkylamine binding By similarity
Compositional bias684 – 6907Poly-Leu
Compositional bias798 – 8047Poly-Glu
Compositional bias1176 – 11827Poly-Ile

Sites

Site3931Calcium ion selectivity and permeability By similarity
Site7361Calcium ion selectivity and permeability By similarity
Site11161Calcium ion selectivity and permeability By similarity
Site14451Calcium ion selectivity and permeability By similarity

Amino acid modifications

Modified residue8451Phosphoserine By similarity
Modified residue15161Phosphoserine; by PKA Potential
Modified residue19191Phosphoserine; by PKA Potential
Modified residue19271Phosphoserine; by PKA Potential
Glycosylation1831N-linked (GlcNAc...) Potential
Glycosylation3581N-linked (GlcNAc...) Potential
Glycosylation14171N-linked (GlcNAc...) Potential
Glycosylation14681N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 4646MIRAF…YISPG → MVNENTRMYVPEENHQ in isoform 4 and isoform 5.
VSP_000908
Alternative sequence8101R → RPAR in isoform 5.
VSP_000909
Alternative sequence964 – 97916FYFDI…TIEIA → GNADYVFTSIFTLEII in isoform 4 and isoform 5.
VSP_000910
Alternative sequence1306 – 133328HYFCD…ITEVH → GYFSDPSNVFDFLIVIGSII AVILSETN in isoform 1 and isoform 4.
VSP_000911
Alternative sequence1334 – 134411Missing in isoform 3.
VSP_000912

Experimental info

Sequence conflict831L → Q in AAA18905. Ref.2
Sequence conflict831L → Q in AAA42016. Ref.2
Sequence conflict871D → G in AAA18905. Ref.2
Sequence conflict5201G → R in AAA18905. Ref.2
Sequence conflict648 – 6492CW → VL in AAA18905. Ref.2
Sequence conflict648 – 6492CW → VL in AAA42016. Ref.2
Sequence conflict6781L → V in AAA18905. Ref.2
Sequence conflict6781L → V in AAA42016. Ref.2
Sequence conflict769 – 7702SP → CG in AAA18905. Ref.2
Sequence conflict769 – 7702SP → CG in AAA42016. Ref.2
Sequence conflict7771L → V in AAA18905. Ref.2
Sequence conflict7771L → V in AAA42016. Ref.2
Sequence conflict8711D → N in AAA18905. Ref.2
Sequence conflict10371R → RA in AAA18905. Ref.2
Sequence conflict10371R → RA in AAA42016. Ref.2
Sequence conflict10981S → C in AAA18905. Ref.2
Sequence conflict10981S → C in AAA42016. Ref.2
Sequence conflict11071T → D in AAA18905. Ref.2
Sequence conflict11071T → D in AAA42016. Ref.2
Sequence conflict12291P → R in AAA18905. Ref.2
Sequence conflict12291P → R in AAA42016. Ref.2
Sequence conflict12291P → R no nucleotide entry Ref.3
Sequence conflict12291P → R in AAA89157. Ref.6
Sequence conflict13061H → D in AAB35528. Ref.5
Sequence conflict13061H → G in AAA42016. Ref.2
Sequence conflict13061H → G in AAA89157. Ref.6
Sequence conflict13291I → L in AAB35528. Ref.5
Sequence conflict14711E → K in AAA18905. Ref.2
Sequence conflict19111C → S in AAA18905. Ref.2
Sequence conflict19111C → S in AAA42016. Ref.2
Sequence conflict20841K → N in AAA18905. Ref.2
Sequence conflict21541R → Q in AAA42016. Ref.2

Secondary structure

1 ... 2169
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 (S3B) [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: D3ADBD20E4763B69

FASTA2,169243,482
        10         20         30         40         50         60 
MIRAFAQPST PPYQPLSSCL SEDTERKFKG KVVHEAQLNC FYISPGGSNY GSPRPAHANM 

        70         80         90        100        110        120 
NANAAAGLAP EHIPTPGAAL SWLAAIDAAR QAKLMGSAGN ATISTVSSTQ RKRQQYGKPK 

       130        140        150        160        170        180 
KQGGTTATRP PRALLCLTLK NPIRRACISI VEWKPFEIII LLTIFANCVA LAIYIPFPED 

       190        200        210        220        230        240 
DSNATNSNLE RVEYLFLIIF TVEAFLKVIA YGLLFHPNAY LRNGWNLLDF IIVVVGLFSA 

       250        260        270        280        290        300 
ILEQATKADG ANALGGKGAG FDVKALRAFR VLRPLRLVSG VPSLQVVLNS IIKAMVPLLH 

       310        320        330        340        350        360 
IALLVLFVII IYAIIGLELF MGKMHKTCYN QEGIIDVPAE EDPSPCALET GHGRQCQNGT 

       370        380        390        400        410        420 
VCKPGWDGPK HGITNFDNFA FAMLTVFQCI TMEGWTDVLY WMQDAMGYEL PWVYFVSLVI 

       430        440        450        460        470        480 
FGSFFVLNLV LGVLSGEFSK EREKAKARGD FQKLREKQQL EEDLKGYLDW ITQAEDIDPE 

       490        500        510        520        530        540 
NEDEGMDEDK PRNMSMPTSE TESVNTENVA GGDIEGENCG ARLAHRISKS KFSRYWRRWN 

       550        560        570        580        590        600 
RFCRRKCRAA VKSNVFYWLV IFLVFLNTLT IASEHYNQPH WLTEVQDTAN KALLALFTAE 

       610        620        630        640        650        660 
MLLKMYSLGL QAYFVSLFNR FDCFIVCGGI LETILVETKI MSPLGISCWR CVRLLRIFKI 

       670        680        690        700        710        720 
TRYWNSLSNL VASLLNSLRS IASLLLLLFL FIIIFSLLGM QLFGGKFNFD EMQTRRSTFD 

       730        740        750        760        770        780 
NFPQSLLTVF QILTGEDWNS VMYDGIMAYG GPSFPGMLVC IYFIILFISP NYILLNLFLA 

       790        800        810        820        830        840 
IAVDNLADAE SLTSAQKEEE EEKERKKLAR TASPEKKQEV MEKPAVEESK EEKIELKSIT 

       850        860        870        880        890        900 
ADGESPPTTK INMDDLQPSE NEDKSPHSNP DTAGEEDEEE PEMPVGPRPR PLSELHLKEK 

       910        920        930        940        950        960 
AVPMPEASAF FIFSPNNRFR LQCHRIVNDT IFTNLILFFI LLSSISLAAE DPVQHTSFRN 

       970        980        990       1000       1010       1020 
HILFYFDIVF TTIFTIEIAL KMTAYGAFLH KGSFCRNYFN ILDLLVVSVS LISFGIQSSA 

      1030       1040       1050       1060       1070       1080 
INVVKILRVL RVLRPLRINR AKGLKHVVQC VFVAIRTIGN IVIVTTLLQF MFACIGVQLF 

      1090       1100       1110       1120       1130       1140 
KGKLYTCSDS SKQTEAESKG NYITYKTGEV DHPIIQPRSW ENSKFDFDNV LAAMMALFTV 

      1150       1160       1170       1180       1190       1200 
STFEGWPELL YRSIDSHTED KGPIYNYRVE ISIFFIIYII IIAFFMMNIF VGFVIVTFQE 

      1210       1220       1230       1240       1250       1260 
QGEQEYKNCE LDKNQRQCVE YALKARPLPR YIPKNQHQYK VWYVVNSTYF EYLMFVLILL 

      1270       1280       1290       1300       1310       1320 
NTICLAMQHY GQSCLFKIAM NILNMLFTGL FTVEMILKLI AFKPKHYFCD AWNTFDALIV 

      1330       1340       1350       1360       1370       1380 
VGSIVDIAIT EVHPAEHTQC SPSMSAEENS RISITFFRLF RVMRLVKLLS RGEGIRTLLW 

      1390       1400       1410       1420       1430       1440 
TFIKSFQALP YVALLIVMLF FIYAVIGMQV FGKIALNDTT EINRNNNFQT FPQAVLLLFR 

      1450       1460       1470       1480       1490       1500 
CATGEAWQDI MLACMPGKKC APESEPSNST EGETPCGSSF AVFYFISFYM LCAFLIINLF 

      1510       1520       1530       1540       1550       1560 
VAVIMDNFDY LTRDWSILGP HHLDEFKRIW AEYDPEAKGR IKHLDVVTLL RRIQPPLGFG 

      1570       1580       1590       1600       1610       1620 
KLCPHRVACK RLVSMNMPLN SDGTVMFNAT LFALVRTALR IKTEGNLEQA NEELRAIIKK 

      1630       1640       1650       1660       1670       1680 
IWKRTSMKLL DQVVPPAGDD EVTVGKFYAT FLIQEYFRKF KKRKEQGLVG KPSQRNALSL 

      1690       1700       1710       1720       1730       1740 
QAGLRTLHDI GPEIRRAISG DLTAEEELDK AMKEAVSAAS EDDIFRRAGG LFGNHVSYYQ 

      1750       1760       1770       1780       1790       1800 
SDSRSNFPQT FATQRPLHIN KTGNNQADTE SPSHEKLVDS TFTPSSYSST GSNANINNAN 

      1810       1820       1830       1840       1850       1860 
NTALGRFPHP AGYSSTVSTV EGHGPPLSPA VRVQEAAWKL SSKRCHSRES QGATVSQDMF 

      1870       1880       1890       1900       1910       1920 
PDETRSSVRL SEEVEYCSEP SLLSTDILSY QDDENRQLTC LEEDKREIQP CPKRSFLRSA 

      1930       1940       1950       1960       1970       1980 
SLGRRASFHL ECLKRQKDQG GDISQKTALP LHLVHHQALA VAGLSPLLQR SHSPSTFPRP 

      1990       2000       2010       2020       2030       2040 
RPTPPVTPGS RGRPLQPIPT LRLEGAESSE KLNSSFPSIH CSSWSEETTA CSGGSSMARR 

      2050       2060       2070       2080       2090       2100 
ARPVSLTVPS QAGAPGRQFH GSASSLVEAV LISEGLGQFA QDPKFIEVTT QELADACDMT 

      2110       2120       2130       2140       2150       2160 
IEEMENAADN ILSGGAQQSP NGTLLPFVNC RDPGQDRAVV PEDESCVYAL GRGRSEEALP 


DSRSYVSNL

« Hide

Isoform 1 (S3A) [UniParc].

Checksum: 1539479E670D0D2A
Show »

FASTA2,169243,364
Isoform 3 (D1) (ROB2) [UniParc].

Checksum: 498718087DA7DC10
Show »

FASTA2,158242,313
Isoform 4 (rbC-I) [UniParc].

Checksum: 8A3C3354E8BDB60D
Show »

FASTA2,139240,045
Isoform 5 (rbC-II) [UniParc].

Checksum: 4207AD0217F19CB2
Show »

FASTA2,142240,488

References

[1]"cDNA cloning of a dihydropyridine-sensitive calcium channel from rat aorta. Evidence for the existence of alternatively spliced forms."
Koch W.J., Ellinor P.T., Schwartz A.
J. Biol. Chem. 265:17786-17791(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Aorta.
[2]"Distinct calcium channels are generated by alternative splicing and are differentially expressed in the mammalian CNS."
Snutch T.P., Tomlinson W.J., Leonard J.P., Gilbert M.M.
Neuron 7:45-57(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5).
Tissue: Brain.
[3]"Rat brain expresses a heterogeneous family of calcium channels."
Snutch T.P., Leonard J.P., Gilbert M.M., Lester H.A., Davidson N.
Proc. Natl. Acad. Sci. U.S.A. 87:3391-3395(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1168-1413 (ISOFORM 1).
[4]"Mutually exclusive exon splicing of the cardiac calcium channel a1 subunit generates developmentally regulated isoforms in the rat heart."
Diebold R.J., Koch W.J., Ellinor P.T., Wang J.-J., Muthuchamy M., Wieczorek D.F., Schwartz A.
Proc. Natl. Acad. Sci. U.S.A. 89:1497-1501(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1269-1415 (ISOFORMS 1; 2 AND 3).
[5]"Changes in transcripts encoding calcium channel subunits of rat myometrium during pregnancy."
Tezuka N., Ali M., Chwalisz K., Garfield R.E.
Am. J. Physiol. 269:C1008-C1017(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1269-1387.
Tissue: Myometrium.
[6]"Multiple calcium channel transcripts in rat osteosarcoma cells: selective activation of alpha 1D isoform by parathyroid hormone."
Barry E.L.R., Gesek F.A., Froehner S.C., Friedman P.A.
Proc. Natl. Acad. Sci. U.S.A. 92:10914-10918(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1202-1495 (ISOFORM 3).
Tissue: Osteosarcoma.
[7]"Differential phosphorylation of two size forms of the neuronal class C L-type calcium channel alpha 1 subunit."
Hell J.W., Yokoyama C.T., Wong S.T., Warner C., Snutch T.P., Catterall W.A.
J. Biol. Chem. 268:19451-19457(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[8]"Ca2+-binding protein-1 facilitates and forms a postsynaptic complex with Cav1.2 (L-type) Ca2+ channels."
Zhou H., Kim S.-A., Kirk E.A., Tippens A.L., Sun H., Haeseleer F., Lee A.
J. Neurosci. 24:4698-4708(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CABP1.
[9]"Structural basis of the alpha1-beta subunit interaction of voltage-gated Ca2+ channels."
Chen Y.H., Li M.H., Zhang Y., He L.L., Yamada Y., Fitzmaurice A., Shen Y., Zhang H., Tong L., Yang J.
Nature 429:675-680(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 452-476.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M59786 mRNA. Translation: AAA85463.1.
M67515 mRNA. Translation: AAA18905.1.
M67516 mRNA. Translation: AAA42016.1.
M91242 expand/collapse EMBL AC list , M91240, M89924, M91241 Genomic DNA. Translation: AAA41460.1.
S80558 mRNA. Translation: AAB35528.1.
U31815 mRNA. Translation: AAA89157.1.
IPIIPI00231323.
IPI00392650.
IPI00476992.
IPI00948183.
IPI00949968.
RefSeqNP_036649.2. NM_012517.2.
UniGeneRn.9827.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VYTX-ray2.60E/F452-476[»]
ProteinModelPortalP22002.
SMRP22002. Positions 1641-1669.
ModBaseSearch...

Protein-protein interaction databases

IntActP22002. 2 interactions.

PTM databases

PhosphoSiteP22002.

Proteomic databases

PaxDbP22002.
PRIDEP22002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID24239.
KEGGrno:24239.
UCSCRGD:2245. rat.

Organism-specific databases

CTD775.
RGD2245. Cacna1c.

Phylogenomic databases

eggNOGCOG1226.
HOVERGENHBG050763.
InParanoidP22002.
KOK04850.

Enzyme and pathway databases

ReactomeREACT_113568. Metabolism.

Gene expression databases

ArrayExpressP22002.
GenevestigatorP22002.
GermOnlineENSRNOG00000007090. Rattus norvegicus.

Family and domain databases

InterProIPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005451. VDCC_L_a1csu.
IPR005446. VDCC_L_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PANTHERPTHR10037:SF47. PTHR10037:SF47. 1 hit.
PfamPF08763. Ca_chan_IQ. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSPR00167. CACHANNEL.
PR01630. LVDCCALPHA1.
PR01635. LVDCCALPHA1C.
SMARTSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP22002.
ChEMBLCHEMBL3762.
EvolutionaryTraceP22002.
NextBio602705.

Entry information

Entry nameCAC1C_RAT
AccessionPrimary (citable) accession number: P22002
Secondary accession number(s): P27733 expand/collapse secondary AC list , P27734, Q62816, Q63271, Q64178
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: April 3, 2013
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents