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O73707 (CAC1C_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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):
CHCACHA1C
Voltage-gated calcium channel subunit alpha Cav1.2
Gene names
Name:CACNA1C
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length177 AA.
Sequence statusFragment.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

The isoform alpha-1Cgives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. Calcium channels containing the alpha-1C subunit play an important role in excitation-contraction coupling in the heart By similarity.

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.

Subcellular location

Membrane; Multi-pass membrane protein.

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 By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›177›177Voltage-dependent L-type calcium channel subunit alpha-1C
PRO_0000053932

Regions

Transmembrane‹1 – 13›13Helical; Name=S3 of repeat IV; Potential
Topological domain14 – 2613Extracellular Potential
Transmembrane27 – 4519Helical; Name=S4 of repeat IV; Potential
Topological domain46 – 6419Cytoplasmic Potential
Transmembrane65 – 8420Helical; Name=S5 of repeat IV; Potential
Topological domain85 – 15369Extracellular Potential
Transmembrane154 – ›177›24Helical; Name=S6 of repeat IV; Potential
Repeat‹1 – ›177›177IV
Region132 – ›177›46Dihydropyridine binding By similarity
Region146 – ›177›32Phenylalkylamine binding By similarity

Sites

Site1181Calcium ion selectivity and permeability By similarity

Amino acid modifications

Glycosylation901N-linked (GlcNAc...) Potential
Glycosylation1411N-linked (GlcNAc...) Potential

Experimental info

Non-terminal residue11
Non-terminal residue1771

Sequences

Sequence LengthMass (Da)Tools
O73707 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 84CB4656D78AAF23

FASTA17719,957
        10         20         30         40         50         60 
ALIVVGSIVD IAITEVNNAE ENSRISITFF RLFRVMRLVK LLSRGEGIRT LLWTFIKSFQ 

        70         80         90        100        110        120 
ALPYVALLIV MLFFIYAVIG MQVFGKIALN DTTEINRNNN FQTFPQAVLL LFRCATGEAW 

       130        140        150        160        170 
QEIMLACLPD KKCDPDSEPA NSTEADHSCG SSFAVFYFIS FYMLCAFLII DLFVAVI 

« Hide

References

[1]"Predominance of the alpha1D subunit in L-type voltage-gated Ca2+ channels of hair cells in the chicken's cochlea."
Kollmar R., Montgomery L.G., Fak J., Henry L.J., Hudspeth A.J.
Proc. Natl. Acad. Sci. U.S.A. 94:14883-14888(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: White leghorn.
Tissue: Basilar papilla.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF027610 mRNA. Translation: AAC08311.1.
UniGeneGga.525.

3D structure databases

ProteinModelPortalO73707.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000021218.

Proteomic databases

PaxDbO73707.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG1226.
HOGENOMHOG000231529.
PhylomeDBO73707.

Family and domain databases

InterProIPR005821. Ion_trans_dom.
IPR002077. VDCCAlpha1.
[Graphical view]
PfamPF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSPR00167. CACHANNEL.
ProtoNetSearch...

Entry information

Entry nameCAC1C_CHICK
AccessionPrimary (citable) accession number: O73707
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: August 1, 1998
Last modified: April 16, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families