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P97445

- CAC1A_MOUSE

UniProt

P97445 - CAC1A_MOUSE

Protein

Voltage-dependent P/Q-type calcium channel subunit alpha-1A

Gene

Cacna1a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (06 Feb 2007)
      Previous versions | rss
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    Functioni

    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. 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).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei320 – 3201Calcium ion selectivity and permeabilityBy similarity
    Sitei670 – 6701Calcium ion selectivity and permeabilityBy similarity
    Sitei1411 – 14111Calcium ion selectivity and permeabilityBy similarity
    Sitei1600 – 16001Binds to omega-Aga-IVABy similarity
    Sitei1707 – 17071Calcium ion selectivity and permeabilityBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi1791 – 180212By similarityAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: InterPro
    2. high voltage-gated calcium channel activity Source: MGI
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: MGI
    5. voltage-gated calcium channel activity Source: UniProtKB

    GO - Biological processi

    1. adult walking behavior Source: MGI
    2. behavioral response to pain Source: MGI
    3. calcium ion-dependent exocytosis Source: MGI
    4. calcium ion-dependent exocytosis of neurotransmitter Source: MGI
    5. calcium ion import Source: RefGenome
    6. calcium ion transport Source: MGI
    7. cell death Source: Ensembl
    8. cell growth Source: MGI
    9. cellular chloride ion homeostasis Source: MGI
    10. central nervous system neuron differentiation Source: MGI
    11. cerebellar molecular layer development Source: MGI
    12. cerebellar Purkinje cell differentiation Source: MGI
    13. cerebellar Purkinje cell layer development Source: MGI
    14. cerebellum maturation Source: MGI
    15. dendrite morphogenesis Source: MGI
    16. gamma-aminobutyric acid secretion Source: MGI
    17. gamma-aminobutyric acid signaling pathway Source: MGI
    18. glucose metabolic process Source: MGI
    19. hormone metabolic process Source: MGI
    20. membrane depolarization Source: MGI
    21. membrane depolarization during action potential Source: RefGenome
    22. musculoskeletal movement, spinal reflex action Source: MGI
    23. negative regulation of hormone biosynthetic process Source: MGI
    24. negative regulation of neuron apoptotic process Source: MGI
    25. neurological system process Source: MGI
    26. neuromuscular process Source: MGI
    27. neuromuscular process controlling balance Source: MGI
    28. neuromuscular synaptic transmission Source: MGI
    29. neuron-neuron synaptic transmission Source: MGI
    30. neurotransmitter metabolic process Source: MGI
    31. positive regulation of cytosolic calcium ion concentration Source: UniProtKB
    32. receptor clustering Source: MGI
    33. regulation of acetylcholine secretion, neurotransmission Source: MGI
    34. regulation of axonogenesis Source: MGI
    35. regulation of calcium ion-dependent exocytosis Source: MGI
    36. regulation of membrane potential Source: MGI
    37. response to pain Source: MGI
    38. rhythmic synaptic transmission Source: MGI
    39. spinal cord motor neuron differentiation Source: MGI
    40. sulfur amino acid metabolic process Source: MGI
    41. synapse assembly Source: MGI
    42. synaptic transmission Source: MGI
    43. synaptic transmission, glutamatergic Source: MGI
    44. transmission of nerve impulse Source: MGI
    45. vestibular nucleus development Source: MGI

    Keywords - Molecular functioni

    Calcium channel, Ion channel, Voltage-gated channel

    Keywords - Biological processi

    Calcium transport, Ion transport, Transport

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_225645. Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:Cacna1a
    Synonyms:Caca1a, Cach4, Cacn3, Cacnl1a4, Ccha1a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:109482. Cacna1a.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. dendrite Source: MGI
    3. neuronal cell body Source: MGI
    4. nucleus Source: Ensembl
    5. voltage-gated calcium channel complex Source: MGI

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    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.

    Keywords - Diseasei

    Disease mutation

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 23682368Voltage-dependent P/Q-type calcium channel subunit alpha-1APRO_0000053917Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence Analysis
    Modified residuei792 – 7921Phosphoserine1 Publication
    Glycosylationi1607 – 16071N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP97445.
    PaxDbiP97445.
    PRIDEiP97445.

    PTM databases

    PhosphoSiteiP97445.

    Expressioni

    Tissue specificityi

    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.

    Gene expression databases

    ArrayExpressiP97445.
    BgeeiP97445.
    GenevestigatoriP97445.

    Interactioni

    Subunit structurei

    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.By similarity

    Protein-protein interaction databases

    BioGridi198430. 4 interactions.
    IntActiP97445. 1 interaction.
    MINTiMINT-4997013.

    Structurei

    3D structure databases

    ProteinModelPortaliP97445.
    SMRiP97445. Positions 102-412, 491-742, 1191-1462, 1509-1763, 1846-1923.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 100100CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini120 – 13819ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini157 – 16812CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini185 – 1928ExtracellularSequence Analysis
    Topological domaini212 – 23019CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini251 – 33787ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini363 – 489127CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini510 – 52314ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini544 – 5518CytoplasmicSequence Analysis
    Topological domaini571 – 58010ExtracellularSequence Analysis
    Topological domaini600 – 61819CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini639 – 69153ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini717 – 1190474CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1215 – 123117ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1252 – 12587CytoplasmicSequence Analysis
    Topological domaini1283 – 129311ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1312 – 133019CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1351 – 143787ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1463 – 151856CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1538 – 155114ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1574 – 15807CytoplasmicSequence Analysis
    Topological domaini1601 – 16077ExtracellularSequence Analysis
    Topological domaini1627 – 164519CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1666 – 173772ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1764 – 2368605CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei101 – 11919Helical; Name=S1 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei139 – 15618Helical; Name=S2 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei169 – 18416Helical; Name=S3 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei193 – 21119Helical; Name=S4 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei231 – 25020Helical; Name=S5 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei338 – 36225Helical; Name=S6 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei490 – 50920Helical; Name=S1 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei524 – 54320Helical; Name=S2 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei552 – 57019Helical; Name=S3 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei581 – 59919Helical; Name=S4 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei619 – 63820Helical; Name=S5 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei692 – 71625Helical; Name=S6 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei1191 – 121424Helical; Name=S1 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1232 – 125120Helical; Name=S2 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1259 – 128224Helical; Name=S3 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1294 – 131118Helical; Name=S4 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1331 – 135020Helical; Name=S5 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1438 – 146225Helical; Name=S6 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1519 – 153719Helical; Name=S1 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1552 – 157322Helical; Name=S2 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1581 – 160020Helical; Name=S3 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1608 – 162619Helical; Name=S4 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1646 – 166520Helical; Name=S5 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1738 – 176326Helical; Name=S6 of repeat IVSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati65 – 365301IAdd
    BLAST
    Repeati475 – 719245IIAdd
    BLAST
    Repeati1182 – 1465284IIIAdd
    BLAST
    Repeati1502 – 1765264IVAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni385 – 40218Binding to the beta subunitBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi729 – 7346Poly-Glu
    Compositional biasi1155 – 11584Poly-Glu

    Domaini

    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.

    Sequence similaritiesi

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1226.
    GeneTreeiENSGT00750000117449.
    HOGENOMiHOG000231530.
    HOVERGENiHBG050763.
    InParanoidiP97445.
    KOiK04344.
    OMAiQPGFWEG.
    OrthoDBiEOG7T1RBQ.
    PhylomeDBiP97445.
    TreeFamiTF312805.

    Family and domain databases

    Gene3Di1.20.120.350. 4 hits.
    InterProiIPR017956. 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]
    PANTHERiPTHR10037:SF59. PTHR10037:SF59. 1 hit.
    PfamiPF08763. Ca_chan_IQ. 1 hit.
    PF00520. Ion_trans. 4 hits.
    [Graphical view]
    PRINTSiPR00167. CACHANNEL.
    PR01632. PQVDCCALPHA1.
    SMARTiSM00384. AT_hook. 1 hit.
    SM01062. Ca_chan_IQ. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P97445-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARFGDEMPG RYGAGGGGSG PAAGVVVGAA GGRGAGGSRQ GGQPGAQRMY     50
    KQSMAQRART MALYNPIPVR QNCLTVNRSL FLFSEDNVVR KYAKKITEWP 100
    PFEYMILATI IANCIVLALE QHLPDDDKTP MSERLDDTEP YFIGIFCFEA 150
    GIKIVALGFA FHKGSYLRNG WNVMDFVVVL TGILATVGTE FDLRTLRAVR 200
    VLRPLKLVSG IPSLQVVLKS IMKAMIPLLQ IGLLLFFAIL IFAIIGLEFY 250
    MGKFHTTCFE EGTDDIQGES PAPCGTEEPA RTCPNGTKCQ PYWEGPNNGI 300
    TQFDNILFAV LTVFQCITME GWTDLLYNSN DASGNTWNWL YFIPLIIIGS 350
    FFMLNLVLGV LSGEFAKERE RVENRRAFLK LRRQQQIERE LNGYMEWISK 400
    AEEVILAEDE TDVEQRHPFD GALRRATLKK SKTDLLNPEE AEDQLADIAS 450
    VGSPFARASI KSAKLENSTF FHKKERRMRF YIRRMVKTQA FYWTVLSLVA 500
    LNTLCVAIVH YNQPEWLSDF LYYAEFIFLG LFMSEMFIKM YGLGTRPYFH 550
    SSFNCFDCGV IIGSIFEVIW AVIKPGTSFG ISVLRALRLL RIFKVTKYWA 600
    SLRNLVVSLL NSMKSIISLL FLLFLFIVVF ALLGMQLFGG QFNFDEGTPP 650
    TNFDTFPAAI MTVFQILTGE DWNEVMYDGI KSQGGVQGGM VFSIYFIVLT 700
    LFGNYTLLNV FLAIAVDNLA NAQELTKDEQ EEEEAANQKL ALQKAKEVAE 750
    VSPLSAANMS IAVKEQQKNQ KPTKSVWEQR TSEMRKQNLL ASREALYGDA 800
    AERWPTPYAR PLRPDVKTHL DRPLVVDPQE NRNNNTNKSR APEALRPTAR 850
    PRESARDPDA RRAWPGSPER APGREGPYGR ESEPQQREHA PPREHAPWDA 900
    DTERAKAGDA PRRHTHRPVA EGEPRRHRAR RRPGDEPDDR PERRPRPRDA 950
    TRPARAADGE GDDGERKRRH RHGPPAHDDR ERRHRRRKEN QGSGVPVSGP 1000
    NLSTTRPIQQ DLGRQDLPLA EDLDNMKNNK LATGEPASPH DSLGHSGLPP 1050
    SPAKIGNSTN PGPALATNPQ NAASRRTPNN PGNPSNPGPP KTPENSLIVT 1100
    NPSSTQPNSA KTARKPEHMA VEIPPACPPL NHTVVQVNKN ANPDPLPKKE 1150
    EEKKEEEEAD PGEDGPKPMP PYSSMFILST TNPLRRLCHY ILNLRYFEMC 1200
    ILMVIAMSSI ALAAEDPVQP NAPRNNVLRY FDYVFTGVFT FEMVIKMIDL 1250
    GLVLHQGAYF RDLWNILDFI VVSGALVAFA FTGNSKGKDI NTIKSLRVLR 1300
    VLRPLKTIKR LPKLKAVFDC VVNSLKNVFN ILIVYMLFMF IFAVVAVQLF 1350
    KGKFFHCTDE SKEFERDCRG KYLLYEKNEV KARDREWKKY EFHYDNVLWA 1400
    LLTLFTVSTG EGWPQVLKHS VDATFENQGP SPGYRMEMSI FYVVYFVVFP 1450
    FFFVNIFVAL IIITFQEQGD KMMEEYSLEK NERACIDFAI SAKPLTRHMP 1500
    QNKQSFQYRM WQFVVSPPFE YTIMAMIALN TIVLMMKFYG ASVAYENALR 1550
    VFNIVFTSLF SLECVLKVMA FGILNYFRDA WNIFDFVTVL GSITDILVTE 1600
    FGNNFINLSF LRLFRAARLI KLLRQGYTIR ILLWTFVQSF KALPYVCLLI 1650
    AMLFFIYAII GMQVFGNIGI DGEDEDSDED EFQITEHNNF RTFFQALMLL 1700
    FRSATGEAWH NIMLSCLSGK PCDKNSGILT ADCGNEFAYF YFVSFIFLCS 1750
    FLMLNLFVAV IMDNFEYLTR DSSILGPHHL DEYVRVWAEY DPAACGRIHY 1800
    KDMYSLLRVI SPPLGLGKKC PHRVACKRLL RMDLPVADDN TVHFNSTLMA 1850
    LIRTALDIKI AKGGADKQQM DAELRKEMMA IWPNLSQKTL DLLVTPHKST 1900
    DLTVGKIYAA MMIMEYYRQS KAKKLQAMRE EQNRTPLMFQ RMEPPSPTQE 1950
    GGPSQNALPS TQLDPGGGLM AHEGGMKESP SWVTQRAQEM FQKTGTWSPE 2000
    RGPPIDMPNS QPNSQSVEMR EMGTDGYSDS EHYLPMEGQT RAASMPRLPA 2050
    ENQRRRGRPR GNDLSTISDT SPMKRSASVL GPKARRLDDY SLERVPPEEN 2100
    QRYHQRRRDR GHRTSERSLG RYTDVDTGLG TDLSMTTQSG DLPSKDRDQD 2150
    RGRPKDRKHR PHHHHHHHHH HPPAPDRDRY AQERPDTGRA RAREQRWSRS 2200
    PSEGREHTTH RQGSSSVSGS PAPSTSGTST PRRGRRQLPQ TPCTPRPLVS 2250
    YSPAPRRPAA RRMAGPAAPP GGSPRGCRRA PRWPAHAPEG PRPRGADYTE 2300
    PDSPREPPGG AHDPAPRSPR TPRAAGCASP RHGRRLPNGY YAGHGAPRPR 2350
    TARRGAHDAY SESEDDWC 2368
    Length:2,368
    Mass (Da):267,647
    Last modified:February 6, 2007 - v2
    Checksum:iE7B573BA005E5CB1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti79 – 791S → P in AAC52940. (PubMed:8929530)Curated
    Sequence conflicti82 – 821L → F in AAC52940. (PubMed:8929530)Curated
    Sequence conflicti884 – 8841P → L in AAC52940. (PubMed:8929530)Curated
    Sequence conflicti888 – 8881E → D in AAW56205. 1 PublicationCurated
    Sequence conflicti1083 – 10831N → D in AAC52940. (PubMed:8929530)Curated
    Sequence conflicti1349 – 13491L → F in AAC52940. (PubMed:8929530)Curated
    Sequence conflicti1373 – 13731L → F in AAC52940. (PubMed:8929530)Curated
    Sequence conflicti2161 – 21611P → PH in AAW56205. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti649 – 6491P → L in tg. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY714490 mRNA. Translation: AAW56205.1.
    U76716 mRNA. Translation: AAC52940.1.
    CCDSiCCDS52618.1.
    RefSeqiNP_031604.3. NM_007578.3.
    UniGeneiMm.334658.

    Genome annotation databases

    EnsembliENSMUST00000121390; ENSMUSP00000112436; ENSMUSG00000034656.
    GeneIDi12286.
    KEGGimmu:12286.
    UCSCiuc009mmn.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY714490 mRNA. Translation: AAW56205.1 .
    U76716 mRNA. Translation: AAC52940.1 .
    CCDSi CCDS52618.1.
    RefSeqi NP_031604.3. NM_007578.3.
    UniGenei Mm.334658.

    3D structure databases

    ProteinModelPortali P97445.
    SMRi P97445. Positions 102-412, 491-742, 1191-1462, 1509-1763, 1846-1923.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198430. 4 interactions.
    IntActi P97445. 1 interaction.
    MINTi MINT-4997013.

    PTM databases

    PhosphoSitei P97445.

    Proteomic databases

    MaxQBi P97445.
    PaxDbi P97445.
    PRIDEi P97445.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000121390 ; ENSMUSP00000112436 ; ENSMUSG00000034656 .
    GeneIDi 12286.
    KEGGi mmu:12286.
    UCSCi uc009mmn.2. mouse.

    Organism-specific databases

    CTDi 773.
    MGIi MGI:109482. Cacna1a.

    Phylogenomic databases

    eggNOGi COG1226.
    GeneTreei ENSGT00750000117449.
    HOGENOMi HOG000231530.
    HOVERGENi HBG050763.
    InParanoidi P97445.
    KOi K04344.
    OMAi QPGFWEG.
    OrthoDBi EOG7T1RBQ.
    PhylomeDBi P97445.
    TreeFami TF312805.

    Enzyme and pathway databases

    Reactomei REACT_225645. Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels.

    Miscellaneous databases

    NextBioi 280756.
    PROi P97445.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P97445.
    Bgeei P97445.
    Genevestigatori P97445.

    Family and domain databases

    Gene3Di 1.20.120.350. 4 hits.
    InterProi IPR017956. 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 ]
    PANTHERi PTHR10037:SF59. PTHR10037:SF59. 1 hit.
    Pfami PF08763. Ca_chan_IQ. 1 hit.
    PF00520. Ion_trans. 4 hits.
    [Graphical view ]
    PRINTSi PR00167. CACHANNEL.
    PR01632. PQVDCCALPHA1.
    SMARTi SM00384. AT_hook. 1 hit.
    SM01062. Ca_chan_IQ. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiCAC1A_MOUSE
    AccessioniPrimary (citable) accession number: P97445
    Secondary accession number(s): Q2TPN3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 138 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3