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P97445 (CAC1A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Voltage-dependent P/Q-type calcium channel subunit alpha-1A
Alternative name(s):
Brain calcium channel I
Short name=BI
Calcium channel, L type, alpha-1 polypeptide isoform 4
Voltage-gated calcium channel subunit alpha Cav2.1
Gene names
Name:Cacna1a
Synonyms:Caca1a, Cach4, Cacn3, Cacnl1a4, Ccha1a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2368 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-1Agives rise to P and/or Q-type calcium currents. P/Q-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by the funnel toxin (Ftx) and by the omega-agatoxin-IVA (omega-Aga-IVA). They are however insensitive to dihydropyridines (DHP), and omega-conotoxin-GVIA (omega-CTx-GVIA).

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 with CABP1 By similarity.

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Brain specific; mainly found in the cerebellum, olfactory bulb, cerebral cortex, hippocampus, and inferior colliculus. In the hippocampus, expression occurs in pyramidal and granule neurons, as well as in interneurons. Purkinje cells contain predominantly P-type VSCC, the Q-type being a prominent calcium current in cerebellar granule cells.

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.

Involvement in disease

Defects in Cacna1a are the cause of a delayed-onset, recessive neurological disorder seen in tottering (tg) mutants, resulting in ataxia, motor seizures and behavioral absence seizures resembling petit mal epilepsy (or absence epilepsy) in humans. There are two more alleles: leaner (tg(lA)), that is characterized by severe ataxia and frequent death past weaning, but no motor seizures; and rolling Nagoya (tg(rol)), that presents an intermediary phenotype, the ataxia being somewhat more severe that with tg, but without motors seizures. Selective degeneration of cerebellar Purkinje cells has been shown for all these types of mutants.

Sequence similarities

Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family. CACNA1A subfamily. [View classification]

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentMembrane
   DiseaseDisease mutation
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   Molecular functionCalcium channel
Ion channel
Voltage-gated channel
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadult walking behavior

Inferred from mutant phenotype PubMed 10611370PubMed 11160387PubMed 11344116PubMed 12401561PubMed 13950100PubMed 16890369PubMed 4799944PubMed 4941467PubMed 8719807. Source: MGI

behavioral response to pain

Inferred from mutant phenotype PubMed 16890369. Source: MGI

calcium ion transport

Inferred from mutant phenotype PubMed 12827191PubMed 9614225PubMed 9857013. Source: MGI

calcium ion-dependent exocytosis

Inferred from mutant phenotype PubMed 12065603. Source: MGI

calcium ion-dependent exocytosis of neurotransmitter

Inferred from mutant phenotype PubMed 10670432. Source: MGI

cell death

Inferred from electronic annotation. Source: Ensembl

cell growth

Inferred from mutant phenotype PubMed 1306163. Source: MGI

cellular chloride ion homeostasis

Inferred from mutant phenotype PubMed 10899223PubMed 8565963. Source: MGI

central nervous system neuron differentiation

Inferred from mutant phenotype PubMed 6945603. Source: MGI

cerebellar Purkinje cell differentiation

Inferred from mutant phenotype PubMed 10630211PubMed 1306163PubMed 7834360. Source: MGI

cerebellar Purkinje cell layer development

Inferred from mutant phenotype PubMed 1306163. Source: MGI

cerebellar molecular layer development

Inferred from mutant phenotype PubMed 7697385. Source: MGI

cerebellum maturation

Inferred from mutant phenotype PubMed 11344116. Source: MGI

dendrite morphogenesis

Inferred from mutant phenotype PubMed 10336181PubMed 11160387PubMed 14973254. Source: MGI

gamma-aminobutyric acid secretion

Inferred from mutant phenotype PubMed 10670432. Source: MGI

gamma-aminobutyric acid signaling pathway

Inferred from mutant phenotype PubMed 8565963. Source: MGI

glucose metabolic process

Inferred from mutant phenotype PubMed 8957685. Source: MGI

hormone metabolic process

Inferred from mutant phenotype PubMed 8229069PubMed 8957685. Source: MGI

membrane depolarization

Inferred from mutant phenotype PubMed 10908603PubMed 11718712PubMed 8158221. Source: MGI

musculoskeletal movement, spinal reflex action

Inferred from mutant phenotype PubMed 11718712. Source: MGI

negative regulation of hormone biosynthetic process

Inferred from mutant phenotype PubMed 11182254. Source: MGI

negative regulation of neuron apoptotic process

Inferred from mutant phenotype PubMed 4941467Ref.2. Source: MGI

neurological system process

Inferred from mutant phenotype PubMed 1486501PubMed 6462226. Source: MGI

neuromuscular process

Inferred from mutant phenotype PubMed 11344116. Source: MGI

neuromuscular process controlling balance

Inferred from mutant phenotype PubMed 4799944. Source: MGI

neuromuscular synaptic transmission

Inferred from mutant phenotype PubMed 10686170. Source: MGI

neuron-neuron synaptic transmission

Inferred from mutant phenotype PubMed 16540584. Source: MGI

neurotransmitter metabolic process

Inferred from mutant phenotype PubMed 1686215PubMed 6167317PubMed 8100981. Source: MGI

positive regulation of cytosolic calcium ion concentration

Inferred from sequence or structural similarity. Source: UniProtKB

receptor clustering

Inferred from mutant phenotype PubMed 12624181. Source: MGI

regulation of acetylcholine secretion, neurotransmission

Inferred from mutant phenotype PubMed 10686170PubMed 12624181. Source: MGI

regulation of axonogenesis

Inferred from mutant phenotype PubMed 572084. Source: MGI

regulation of calcium ion-dependent exocytosis

Inferred from direct assay PubMed 8632762. Source: MGI

regulation of membrane potential

Inferred from mutant phenotype PubMed 10670432PubMed 12151514PubMed 12401561PubMed 1355109PubMed 1572065PubMed 9614225PubMed 9857013. Source: MGI

response to pain

Inferred from mutant phenotype PubMed 11718712. Source: MGI

rhythmic synaptic transmission

Inferred from mutant phenotype PubMed 16474392. Source: MGI

spinal cord motor neuron differentiation

Inferred from mutant phenotype PubMed 17156092. Source: MGI

sulfur amino acid metabolic process

Inferred from mutant phenotype PubMed 1485534. Source: MGI

synapse assembly

Inferred from mutant phenotype PubMed 10336181PubMed 14973254. Source: MGI

synaptic transmission

Inferred from mutant phenotype PubMed 10611370PubMed 12040045PubMed 15548652. Source: MGI

synaptic transmission, glutamatergic

Inferred from mutant phenotype PubMed 10322048PubMed 14973254. Source: MGI

transmission of nerve impulse

Inferred from mutant phenotype PubMed 1355109PubMed 1469420PubMed 1572065. Source: MGI

vestibular nucleus development

Inferred from mutant phenotype PubMed 8719615. Source: MGI

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

dendrite

Inferred from direct assay PubMed 15451373. Source: MGI

neuronal cell body

Inferred from direct assay PubMed 15451373. Source: MGI

nucleus

Inferred from electronic annotation. Source: Ensembl

voltage-gated calcium channel complex

Inferred from direct assay PubMed 10328888. Source: MGI

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

high voltage-gated calcium channel activity

Inferred from mutant phenotype PubMed 10908603PubMed 11344116PubMed 11718712PubMed 12040045PubMed 12065603PubMed 12401561PubMed 12624181PubMed 15548652PubMed 9742139. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

voltage-gated calcium channel activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 23682368Voltage-dependent P/Q-type calcium channel subunit alpha-1A
PRO_0000053917

Regions

Topological domain1 – 100100Cytoplasmic Potential
Transmembrane101 – 11919Helical; Name=S1 of repeat I; Potential
Topological domain120 – 13819Extracellular Potential
Transmembrane139 – 15618Helical; Name=S2 of repeat I; Potential
Topological domain157 – 16812Cytoplasmic Potential
Transmembrane169 – 18416Helical; Name=S3 of repeat I; Potential
Topological domain185 – 1928Extracellular Potential
Transmembrane193 – 21119Helical; Name=S4 of repeat I; Potential
Topological domain212 – 23019Cytoplasmic Potential
Transmembrane231 – 25020Helical; Name=S5 of repeat I; Potential
Topological domain251 – 33787Extracellular Potential
Transmembrane338 – 36225Helical; Name=S6 of repeat I; Potential
Topological domain363 – 489127Cytoplasmic Potential
Transmembrane490 – 50920Helical; Name=S1 of repeat II; Potential
Topological domain510 – 52314Extracellular Potential
Transmembrane524 – 54320Helical; Name=S2 of repeat II; Potential
Topological domain544 – 5518Cytoplasmic Potential
Transmembrane552 – 57019Helical; Name=S3 of repeat II; Potential
Topological domain571 – 58010Extracellular Potential
Transmembrane581 – 59919Helical; Name=S4 of repeat II; Potential
Topological domain600 – 61819Cytoplasmic Potential
Transmembrane619 – 63820Helical; Name=S5 of repeat II; Potential
Topological domain639 – 69153Extracellular Potential
Transmembrane692 – 71625Helical; Name=S6 of repeat II; Potential
Topological domain717 – 1190474Cytoplasmic Potential
Transmembrane1191 – 121424Helical; Name=S1 of repeat III; Potential
Topological domain1215 – 123117Extracellular Potential
Transmembrane1232 – 125120Helical; Name=S2 of repeat III; Potential
Topological domain1252 – 12587Cytoplasmic Potential
Transmembrane1259 – 128224Helical; Name=S3 of repeat III; Potential
Topological domain1283 – 129311Extracellular Potential
Transmembrane1294 – 131118Helical; Name=S4 of repeat III; Potential
Topological domain1312 – 133019Cytoplasmic Potential
Transmembrane1331 – 135020Helical; Name=S5 of repeat III; Potential
Topological domain1351 – 143787Extracellular Potential
Transmembrane1438 – 146225Helical; Name=S6 of repeat III; Potential
Topological domain1463 – 151856Cytoplasmic Potential
Transmembrane1519 – 153719Helical; Name=S1 of repeat IV; Potential
Topological domain1538 – 155114Extracellular Potential
Transmembrane1552 – 157322Helical; Name=S2 of repeat IV; Potential
Topological domain1574 – 15807Cytoplasmic Potential
Transmembrane1581 – 160020Helical; Name=S3 of repeat IV; Potential
Topological domain1601 – 16077Extracellular Potential
Transmembrane1608 – 162619Helical; Name=S4 of repeat IV; Potential
Topological domain1627 – 164519Cytoplasmic Potential
Transmembrane1646 – 166520Helical; Name=S5 of repeat IV; Potential
Topological domain1666 – 173772Extracellular Potential
Transmembrane1738 – 176326Helical; Name=S6 of repeat IV; Potential
Topological domain1764 – 2368605Cytoplasmic Potential
Repeat65 – 365301I
Repeat475 – 719245II
Repeat1182 – 1465284III
Repeat1502 – 1765264IV
Calcium binding1791 – 180212 By similarity
Region385 – 40218Binding to the beta subunit By similarity
Compositional bias729 – 7346Poly-Glu
Compositional bias1155 – 11584Poly-Glu

Sites

Site3201Calcium ion selectivity and permeability By similarity
Site6701Calcium ion selectivity and permeability By similarity
Site14111Calcium ion selectivity and permeability By similarity
Site16001Binds to omega-Aga-IVA By similarity
Site17071Calcium ion selectivity and permeability By similarity

Amino acid modifications

Modified residue7921Phosphoserine Ref.3
Glycosylation2851N-linked (GlcNAc...) Potential
Glycosylation16071N-linked (GlcNAc...) Potential

Natural variations

Natural variant6491P → L in tg. Ref.2

Experimental info

Sequence conflict791S → P in AAC52940. Ref.2
Sequence conflict821L → F in AAC52940. Ref.2
Sequence conflict8841P → L in AAC52940. Ref.2
Sequence conflict8881E → D in AAW56205. Ref.1
Sequence conflict10831N → D in AAC52940. Ref.2
Sequence conflict13491L → F in AAC52940. Ref.2
Sequence conflict13731L → F in AAC52940. Ref.2
Sequence conflict21611P → PH in AAW56205. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P97445 [UniParc].

Last modified February 6, 2007. Version 2.
Checksum: E7B573BA005E5CB1

FASTA2,368267,647
        10         20         30         40         50         60 
MARFGDEMPG RYGAGGGGSG PAAGVVVGAA GGRGAGGSRQ GGQPGAQRMY KQSMAQRART 

        70         80         90        100        110        120 
MALYNPIPVR QNCLTVNRSL FLFSEDNVVR KYAKKITEWP PFEYMILATI IANCIVLALE 

       130        140        150        160        170        180 
QHLPDDDKTP MSERLDDTEP YFIGIFCFEA GIKIVALGFA FHKGSYLRNG WNVMDFVVVL 

       190        200        210        220        230        240 
TGILATVGTE FDLRTLRAVR VLRPLKLVSG IPSLQVVLKS IMKAMIPLLQ IGLLLFFAIL 

       250        260        270        280        290        300 
IFAIIGLEFY MGKFHTTCFE EGTDDIQGES PAPCGTEEPA RTCPNGTKCQ PYWEGPNNGI 

       310        320        330        340        350        360 
TQFDNILFAV LTVFQCITME GWTDLLYNSN DASGNTWNWL YFIPLIIIGS FFMLNLVLGV 

       370        380        390        400        410        420 
LSGEFAKERE RVENRRAFLK LRRQQQIERE LNGYMEWISK AEEVILAEDE TDVEQRHPFD 

       430        440        450        460        470        480 
GALRRATLKK SKTDLLNPEE AEDQLADIAS VGSPFARASI KSAKLENSTF FHKKERRMRF 

       490        500        510        520        530        540 
YIRRMVKTQA FYWTVLSLVA LNTLCVAIVH YNQPEWLSDF LYYAEFIFLG LFMSEMFIKM 

       550        560        570        580        590        600 
YGLGTRPYFH SSFNCFDCGV IIGSIFEVIW AVIKPGTSFG ISVLRALRLL RIFKVTKYWA 

       610        620        630        640        650        660 
SLRNLVVSLL NSMKSIISLL FLLFLFIVVF ALLGMQLFGG QFNFDEGTPP TNFDTFPAAI 

       670        680        690        700        710        720 
MTVFQILTGE DWNEVMYDGI KSQGGVQGGM VFSIYFIVLT LFGNYTLLNV FLAIAVDNLA 

       730        740        750        760        770        780 
NAQELTKDEQ EEEEAANQKL ALQKAKEVAE VSPLSAANMS IAVKEQQKNQ KPTKSVWEQR 

       790        800        810        820        830        840 
TSEMRKQNLL ASREALYGDA AERWPTPYAR PLRPDVKTHL DRPLVVDPQE NRNNNTNKSR 

       850        860        870        880        890        900 
APEALRPTAR PRESARDPDA RRAWPGSPER APGREGPYGR ESEPQQREHA PPREHAPWDA 

       910        920        930        940        950        960 
DTERAKAGDA PRRHTHRPVA EGEPRRHRAR RRPGDEPDDR PERRPRPRDA TRPARAADGE 

       970        980        990       1000       1010       1020 
GDDGERKRRH RHGPPAHDDR ERRHRRRKEN QGSGVPVSGP NLSTTRPIQQ DLGRQDLPLA 

      1030       1040       1050       1060       1070       1080 
EDLDNMKNNK LATGEPASPH DSLGHSGLPP SPAKIGNSTN PGPALATNPQ NAASRRTPNN 

      1090       1100       1110       1120       1130       1140 
PGNPSNPGPP KTPENSLIVT NPSSTQPNSA KTARKPEHMA VEIPPACPPL NHTVVQVNKN 

      1150       1160       1170       1180       1190       1200 
ANPDPLPKKE EEKKEEEEAD PGEDGPKPMP PYSSMFILST TNPLRRLCHY ILNLRYFEMC 

      1210       1220       1230       1240       1250       1260 
ILMVIAMSSI ALAAEDPVQP NAPRNNVLRY FDYVFTGVFT FEMVIKMIDL GLVLHQGAYF 

      1270       1280       1290       1300       1310       1320 
RDLWNILDFI VVSGALVAFA FTGNSKGKDI NTIKSLRVLR VLRPLKTIKR LPKLKAVFDC 

      1330       1340       1350       1360       1370       1380 
VVNSLKNVFN ILIVYMLFMF IFAVVAVQLF KGKFFHCTDE SKEFERDCRG KYLLYEKNEV 

      1390       1400       1410       1420       1430       1440 
KARDREWKKY EFHYDNVLWA LLTLFTVSTG EGWPQVLKHS VDATFENQGP SPGYRMEMSI 

      1450       1460       1470       1480       1490       1500 
FYVVYFVVFP FFFVNIFVAL IIITFQEQGD KMMEEYSLEK NERACIDFAI SAKPLTRHMP 

      1510       1520       1530       1540       1550       1560 
QNKQSFQYRM WQFVVSPPFE YTIMAMIALN TIVLMMKFYG ASVAYENALR VFNIVFTSLF 

      1570       1580       1590       1600       1610       1620 
SLECVLKVMA FGILNYFRDA WNIFDFVTVL GSITDILVTE FGNNFINLSF LRLFRAARLI 

      1630       1640       1650       1660       1670       1680 
KLLRQGYTIR ILLWTFVQSF KALPYVCLLI AMLFFIYAII GMQVFGNIGI DGEDEDSDED 

      1690       1700       1710       1720       1730       1740 
EFQITEHNNF RTFFQALMLL FRSATGEAWH NIMLSCLSGK PCDKNSGILT ADCGNEFAYF 

      1750       1760       1770       1780       1790       1800 
YFVSFIFLCS FLMLNLFVAV IMDNFEYLTR DSSILGPHHL DEYVRVWAEY DPAACGRIHY 

      1810       1820       1830       1840       1850       1860 
KDMYSLLRVI SPPLGLGKKC PHRVACKRLL RMDLPVADDN TVHFNSTLMA LIRTALDIKI 

      1870       1880       1890       1900       1910       1920 
AKGGADKQQM DAELRKEMMA IWPNLSQKTL DLLVTPHKST DLTVGKIYAA MMIMEYYRQS 

      1930       1940       1950       1960       1970       1980 
KAKKLQAMRE EQNRTPLMFQ RMEPPSPTQE GGPSQNALPS TQLDPGGGLM AHEGGMKESP 

      1990       2000       2010       2020       2030       2040 
SWVTQRAQEM FQKTGTWSPE RGPPIDMPNS QPNSQSVEMR EMGTDGYSDS EHYLPMEGQT 

      2050       2060       2070       2080       2090       2100 
RAASMPRLPA ENQRRRGRPR GNDLSTISDT SPMKRSASVL GPKARRLDDY SLERVPPEEN 

      2110       2120       2130       2140       2150       2160 
QRYHQRRRDR GHRTSERSLG RYTDVDTGLG TDLSMTTQSG DLPSKDRDQD RGRPKDRKHR 

      2170       2180       2190       2200       2210       2220 
PHHHHHHHHH HPPAPDRDRY AQERPDTGRA RAREQRWSRS PSEGREHTTH RQGSSSVSGS 

      2230       2240       2250       2260       2270       2280 
PAPSTSGTST PRRGRRQLPQ TPCTPRPLVS YSPAPRRPAA RRMAGPAAPP GGSPRGCRRA 

      2290       2300       2310       2320       2330       2340 
PRWPAHAPEG PRPRGADYTE PDSPREPPGG AHDPAPRSPR TPRAAGCASP RHGRRLPNGY 

      2350       2360 
YAGHGAPRPR TARRGAHDAY SESEDDWC 

« Hide

References

« Hide 'large scale' references
[1]"Molecular identity of P-type calcium current in Purkinje neurons."
Richards K.S., Swensen A.M., Lipscombe D.
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Swiss Webster.
Tissue: Brain.
[2]"Absence epilepsy in tottering mutant mice is associated with calcium channel defects."
Fletcher C.F., Lutz C.M., O'Sullivan T.N., Shaughnessy J.D. Jr., Hawkes R., Frankel W.N., Copeland N.G., Jenkins N.A.
Cell 87:607-617(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 49-2212, VARIANT TG LEU-649.
Strain: DBA/2J.
[3]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-792, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[4]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain cortex.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY714490 mRNA. Translation: AAW56205.1.
U76716 mRNA. Translation: AAC52940.1.
RefSeqNP_031604.3. NM_007578.3.
UniGeneMm.334658.

3D structure databases

ProteinModelPortalP97445.
SMRP97445. Positions 102-412, 491-742, 1191-1462, 1509-1928.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198430. 4 interactions.
IntActP97445. 1 interaction.
MINTMINT-4997013.

PTM databases

PhosphoSiteP97445.

Proteomic databases

PaxDbP97445.
PRIDEP97445.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000121390; ENSMUSP00000112436; ENSMUSG00000034656.
GeneID12286.
KEGGmmu:12286.
UCSCuc009mmn.2. mouse.

Organism-specific databases

CTD773.
MGIMGI:109482. Cacna1a.

Phylogenomic databases

eggNOGCOG1226.
GeneTreeENSGT00750000117449.
HOGENOMHOG000231530.
HOVERGENHBG050763.
InParanoidP97445.
KOK04344.
OMAQPGFWEG.
OrthoDBEOG7T1RBQ.
PhylomeDBP97445.
TreeFamTF312805.

Gene expression databases

ArrayExpressP97445.
BgeeP97445.
GenevestigatorP97445.

Family and domain databases

Gene3D1.20.120.350. 4 hits.
InterProIPR017956. AT_hook_DNA-bd_motif.
IPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005448. VDCC_P/Q_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PANTHERPTHR10037:SF59. PTHR10037:SF59. 1 hit.
PfamPF08763. Ca_chan_IQ. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSPR00167. CACHANNEL.
PR01632. PQVDCCALPHA1.
SMARTSM00384. AT_hook. 1 hit.
SM01062. Ca_chan_IQ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio280756.
PROP97445.
SOURCESearch...

Entry information

Entry nameCAC1A_MOUSE
AccessionPrimary (citable) accession number: P97445
Secondary accession number(s): Q2TPN3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: February 6, 2007
Last modified: April 16, 2014
This is version 133 of the entry and version 2 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot