A0A1B0GUS3 · A0A1B0GUS3_HUMAN
- ProteinVoltage-dependent P/Q-type calcium channel subunit alpha
- GeneCACNA1A
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids2495 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
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-1A gives rise to P and/or Q-type calcium currents.
Catalytic activity
- Ca2+(in) = Ca2+(out)
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | voltage-gated calcium channel complex | |
Molecular Function | metal ion binding | |
Molecular Function | voltage-gated calcium channel activity |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameVoltage-dependent P/Q-type calcium channel subunit alpha
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A1B0GUS3
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 102-119 | Helical | ||||
Sequence: YMILATIIANCIVLALEQ | ||||||
Transmembrane | 139-159 | Helical | ||||
Sequence: YFIGIFCFEAGIKIIALGFAF | ||||||
Transmembrane | 222-245 | Helical | ||||
Sequence: AMIPLLQIGLLLFFAILIFAIIGL | ||||||
Transmembrane | 337-359 | Helical | ||||
Sequence: WLYFIPLIIIGSFFMLNLVLGVL | ||||||
Transmembrane | 488-507 | Helical | ||||
Sequence: AFYWTVLSLVALNTLCVAIV | ||||||
Transmembrane | 519-539 | Helical | ||||
Sequence: LYYAEFIFLGLFMSEMFIKMY | ||||||
Transmembrane | 614-636 | Helical | ||||
Sequence: IISLLFLLFLFIVVFALLGMQLF | ||||||
Transmembrane | 690-714 | Helical | ||||
Sequence: FSIYFIVLTLFGNYTLLNVFLAIAV | ||||||
Transmembrane | 1243-1262 | Helical | ||||
Sequence: LRYFEMCILMVIAMSSIALA | ||||||
Transmembrane | 1282-1303 | Helical | ||||
Sequence: YVFTGVFTFEMVIKMIDLGLVL | ||||||
Transmembrane | 1315-1332 | Helical | ||||
Sequence: ILDFIVVSGALVAFAFTG | ||||||
Transmembrane | 1377-1399 | Helical | ||||
Sequence: VFNILIVYMLFMFIFAVVAVQLF | ||||||
Transmembrane | 1489-1514 | Helical | ||||
Sequence: IFYVVYFVVFPFFFVNIFVALIIITF | ||||||
Transmembrane | 1570-1588 | Helical | ||||
Sequence: YTIMAMIALNTIVLMMKFY | ||||||
Transmembrane | 1600-1623 | Helical | ||||
Sequence: VFNIVFTSLFSLECVLKVMAFGIL | ||||||
Transmembrane | 1691-1709 | Helical | ||||
Sequence: ALPYVCLLIAMLFFIYAII | ||||||
Transmembrane | 1787-1811 | Helical | ||||
Sequence: AYFYFVSFIFLCSFLMLNLFVAVIM |
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 908 variants from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Features
Showing features for glycosylation, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Glycosylation | 283 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 750 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2108 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Family & Domains
Features
Showing features for coiled coil, region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 710-746 | |||||
Sequence: LAIAVDNLANAQELTKDEQEEEEAANQKLALQKAKEV | ||||||
Region | 819-1221 | Disordered | ||||
Sequence: HLDRPLVVDPQENRNNNTNKSRAAEPTVDQRLGQQRAEDFLRKQARYHDRARDPSGSAGLDARRPWAGSQEAELSREGPYGRESDHHAREGSLEQPGFWEGEAERGKAGDPHRRHVHRQGGSRESRSGSPRTGADGEHRRHRAHRRPGEEGPEDKAERRARHREGSRPARGGEGEGEGPDGGERRRRHRHGAPATYEGDARREDKERRHRRRKENQGSGVPVSGPNLSTTRPIQQDLGRQDPPLAEDIDNMKNNKLATAESAAPHGSLGHAGLPQSPAKMGNSTDPGPMLAIPAMATNPQNAASRRTPNNPGNPSNPGPPKTPENSLIVTNPSGTQTNSAKTARKPDHTTVDIPPACPPPLNHTVVQVNKNANPDPLPKKEEEKKEEEEDDRGEDGPKPMPPY | ||||||
Compositional bias | 828-843 | Polar residues | ||||
Sequence: PQENRNNNTNKSRAAE | ||||||
Compositional bias | 853-875 | Basic and acidic residues | ||||
Sequence: QRAEDFLRKQARYHDRARDPSGS | ||||||
Compositional bias | 894-911 | Basic and acidic residues | ||||
Sequence: REGPYGRESDHHAREGSL | ||||||
Compositional bias | 918-1034 | Basic and acidic residues | ||||
Sequence: EGEAERGKAGDPHRRHVHRQGGSRESRSGSPRTGADGEHRRHRAHRRPGEEGPEDKAERRARHREGSRPARGGEGEGEGPDGGERRRRHRHGAPATYEGDARREDKERRHRRRKENQ | ||||||
Compositional bias | 1037-1054 | Polar residues | ||||
Sequence: GVPVSGPNLSTTRPIQQD | ||||||
Compositional bias | 1115-1129 | Polar residues | ||||
Sequence: TNPQNAASRRTPNNP | ||||||
Compositional bias | 1140-1162 | Polar residues | ||||
Sequence: TPENSLIVTNPSGTQTNSAKTAR | ||||||
Compositional bias | 1193-1215 | Basic and acidic residues | ||||
Sequence: DPLPKKEEEKKEEEEDDRGEDGP | ||||||
Domain | 1948-1982 | Voltage-dependent calcium channel alpha-1 subunit IQ | ||||
Sequence: STDLTVGKIYAAMMIMEYYRQSKAKKLQAMREEQD | ||||||
Region | 1989-2032 | Disordered | ||||
Sequence: QRMEPPSPTQEGGPGQNALPSTQLDPGGALMAHESGLKESPSWV | ||||||
Compositional bias | 2044-2067 | Polar residues | ||||
Sequence: GTWSPEQGPPTDMPNSQPNSQSVE | ||||||
Region | 2044-2495 | Disordered | ||||
Sequence: GTWSPEQGPPTDMPNSQPNSQSVEMREMGRDGYSDSEHYLPMEGQGRAASMPRLPAENQTISDTSPMKRSASVLGPKARRLDDYSLERVPPEENQRHHQRRRDRSHRASERSLGRYTDVDTGLGTDLSMTTQSGDLPSKERDQERGRPKDRKHRQHHHHHHHHHHPPPPDKDRYAQERPDHGRARARDQRWSRSPSEGREHMAHRQGSSSVSGSPAPSTSGTSTPRRGRRQLPQTPSTPRPHVSYSPVIRKAGGSGPPQQQQQQQQQQQQQAVARPGRAATSGPRRYPGPTAEPLAGDRPPTGGHSSGRSPRMERRVPGPARSESPRACRHGGARWPASGPHVSEGPPGPRHHGYYRGSDYDEADGPGSGGGEEAMAGAYDAPPPVRHASSGATGRSPRTPRASGPACASPSRHGRRLPNGYYPAHGLARPRGPGSRKGLHEPYSESDDDWC | ||||||
Compositional bias | 2098-2112 | Polar residues | ||||
Sequence: PAENQTISDTSPMKR | ||||||
Compositional bias | 2123-2142 | Basic and acidic residues | ||||
Sequence: RLDDYSLERVPPEENQRHHQ | ||||||
Compositional bias | 2193-2210 | Basic residues | ||||
Sequence: DRKHRQHHHHHHHHHHPP | ||||||
Compositional bias | 2211-2247 | Basic and acidic residues | ||||
Sequence: PPDKDRYAQERPDHGRARARDQRWSRSPSEGREHMAH | ||||||
Compositional bias | 2248-2285 | Polar residues | ||||
Sequence: RQGSSSVSGSPAPSTSGTSTPRRGRRQLPQTPSTPRPH | ||||||
Compositional bias | 2298-2319 | Polar residues | ||||
Sequence: SGPPQQQQQQQQQQQQQAVARP | ||||||
Compositional bias | 2478-2495 | Basic and acidic residues | ||||
Sequence: GSRKGLHEPYSESDDDWC |
Sequence similarities
Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family. CACNA1A subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,495
- Mass (Da)281,200
- Last updated2016-10-05 v1
- ChecksumEA547DEED3FEDA2B
Computationally mapped potential isoform sequences
There are 23 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
O00555 | CAC1A_HUMAN | CACNA1A | 2506 | ||
B5TYJ1 | B5TYJ1_HUMAN | CACNA1A | 2263 | ||
A0AAQ5BGX1 | A0AAQ5BGX1_HUMAN | CACNA1A | 184 | ||
A0AAQ5BGX9 | A0AAQ5BGX9_HUMAN | CACNA1A | 1662 | ||
K7EIF8 | K7EIF8_HUMAN | CACNA1A | 89 | ||
A0A1B0GUM7 | A0A1B0GUM7_HUMAN | CACNA1A | 2165 | ||
A0A1B0GUP3 | A0A1B0GUP3_HUMAN | CACNA1A | 1867 | ||
A0A1B0GUE5 | A0A1B0GUE5_HUMAN | CACNA1A | 1664 | ||
A0A1B0GU74 | A0A1B0GU74_HUMAN | CACNA1A | 2302 | ||
A0A1B0GTW2 | A0A1B0GTW2_HUMAN | CACNA1A | 2460 | ||
A0A1B0GU81 | A0A1B0GU81_HUMAN | CACNA1A | 2507 | ||
A0A1B0GTI4 | A0A1B0GTI4_HUMAN | CACNA1A | 2262 | ||
A0A1B0GTN7 | A0A1B0GTN7_HUMAN | CACNA1A | 2507 | ||
A0A1B0GTG6 | A0A1B0GTG6_HUMAN | CACNA1A | 212 | ||
A0A1B0GVX1 | A0A1B0GVX1_HUMAN | CACNA1A | 2508 | ||
A0A590UJK2 | A0A590UJK2_HUMAN | CACNA1A | 2328 | ||
A0A1C7CYY9 | A0A1C7CYY9_HUMAN | CACNA1A | 2508 | ||
A0A384DVW2 | A0A384DVW2_HUMAN | CACNA1A | 2261 | ||
K7EKF7 | K7EKF7_HUMAN | CACNA1A | 2496 | ||
K7EQ95 | K7EQ95_HUMAN | CACNA1A | 2494 | ||
I3L2V5 | I3L2V5_HUMAN | CACNA1A | 108 | ||
I3L391 | I3L391_HUMAN | CACNA1A | 1667 | ||
A0A087WW63 | A0A087WW63_HUMAN | CACNA1A | 2512 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 828-843 | Polar residues | ||||
Sequence: PQENRNNNTNKSRAAE | ||||||
Compositional bias | 853-875 | Basic and acidic residues | ||||
Sequence: QRAEDFLRKQARYHDRARDPSGS | ||||||
Compositional bias | 894-911 | Basic and acidic residues | ||||
Sequence: REGPYGRESDHHAREGSL | ||||||
Compositional bias | 918-1034 | Basic and acidic residues | ||||
Sequence: EGEAERGKAGDPHRRHVHRQGGSRESRSGSPRTGADGEHRRHRAHRRPGEEGPEDKAERRARHREGSRPARGGEGEGEGPDGGERRRRHRHGAPATYEGDARREDKERRHRRRKENQ | ||||||
Compositional bias | 1037-1054 | Polar residues | ||||
Sequence: GVPVSGPNLSTTRPIQQD | ||||||
Compositional bias | 1115-1129 | Polar residues | ||||
Sequence: TNPQNAASRRTPNNP | ||||||
Compositional bias | 1140-1162 | Polar residues | ||||
Sequence: TPENSLIVTNPSGTQTNSAKTAR | ||||||
Compositional bias | 1193-1215 | Basic and acidic residues | ||||
Sequence: DPLPKKEEEKKEEEEDDRGEDGP | ||||||
Compositional bias | 2044-2067 | Polar residues | ||||
Sequence: GTWSPEQGPPTDMPNSQPNSQSVE | ||||||
Compositional bias | 2098-2112 | Polar residues | ||||
Sequence: PAENQTISDTSPMKR | ||||||
Compositional bias | 2123-2142 | Basic and acidic residues | ||||
Sequence: RLDDYSLERVPPEENQRHHQ | ||||||
Compositional bias | 2193-2210 | Basic residues | ||||
Sequence: DRKHRQHHHHHHHHHHPP | ||||||
Compositional bias | 2211-2247 | Basic and acidic residues | ||||
Sequence: PPDKDRYAQERPDHGRARARDQRWSRSPSEGREHMAH | ||||||
Compositional bias | 2248-2285 | Polar residues | ||||
Sequence: RQGSSSVSGSPAPSTSGTSTPRRGRRQLPQTPSTPRPH | ||||||
Compositional bias | 2298-2319 | Polar residues | ||||
Sequence: SGPPQQQQQQQQQQQQQAVARP | ||||||
Compositional bias | 2478-2495 | Basic and acidic residues | ||||
Sequence: GSRKGLHEPYSESDDDWC |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC005305 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC005513 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC011446 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC022436 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC026805 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC093062 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC098781 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC124224 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KF456505 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |