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P97445

- CAC1A_MOUSE

UniProt

P97445 - CAC1A_MOUSE

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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

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. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP97445.
ExpressionAtlasiP97445. baseline and differential.
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.
GeneTreeiENSGT00760000119135.
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

        10         20         30         40         50
MARFGDEMPG RYGAGGGGSG PAAGVVVGAA GGRGAGGSRQ GGQPGAQRMY
60 70 80 90 100
KQSMAQRART MALYNPIPVR QNCLTVNRSL FLFSEDNVVR KYAKKITEWP
110 120 130 140 150
PFEYMILATI IANCIVLALE QHLPDDDKTP MSERLDDTEP YFIGIFCFEA
160 170 180 190 200
GIKIVALGFA FHKGSYLRNG WNVMDFVVVL TGILATVGTE FDLRTLRAVR
210 220 230 240 250
VLRPLKLVSG IPSLQVVLKS IMKAMIPLLQ IGLLLFFAIL IFAIIGLEFY
260 270 280 290 300
MGKFHTTCFE EGTDDIQGES PAPCGTEEPA RTCPNGTKCQ PYWEGPNNGI
310 320 330 340 350
TQFDNILFAV LTVFQCITME GWTDLLYNSN DASGNTWNWL YFIPLIIIGS
360 370 380 390 400
FFMLNLVLGV LSGEFAKERE RVENRRAFLK LRRQQQIERE LNGYMEWISK
410 420 430 440 450
AEEVILAEDE TDVEQRHPFD GALRRATLKK SKTDLLNPEE AEDQLADIAS
460 470 480 490 500
VGSPFARASI KSAKLENSTF FHKKERRMRF YIRRMVKTQA FYWTVLSLVA
510 520 530 540 550
LNTLCVAIVH YNQPEWLSDF LYYAEFIFLG LFMSEMFIKM YGLGTRPYFH
560 570 580 590 600
SSFNCFDCGV IIGSIFEVIW AVIKPGTSFG ISVLRALRLL RIFKVTKYWA
610 620 630 640 650
SLRNLVVSLL NSMKSIISLL FLLFLFIVVF ALLGMQLFGG QFNFDEGTPP
660 670 680 690 700
TNFDTFPAAI MTVFQILTGE DWNEVMYDGI KSQGGVQGGM VFSIYFIVLT
710 720 730 740 750
LFGNYTLLNV FLAIAVDNLA NAQELTKDEQ EEEEAANQKL ALQKAKEVAE
760 770 780 790 800
VSPLSAANMS IAVKEQQKNQ KPTKSVWEQR TSEMRKQNLL ASREALYGDA
810 820 830 840 850
AERWPTPYAR PLRPDVKTHL DRPLVVDPQE NRNNNTNKSR APEALRPTAR
860 870 880 890 900
PRESARDPDA RRAWPGSPER APGREGPYGR ESEPQQREHA PPREHAPWDA
910 920 930 940 950
DTERAKAGDA PRRHTHRPVA EGEPRRHRAR RRPGDEPDDR PERRPRPRDA
960 970 980 990 1000
TRPARAADGE GDDGERKRRH RHGPPAHDDR ERRHRRRKEN QGSGVPVSGP
1010 1020 1030 1040 1050
NLSTTRPIQQ DLGRQDLPLA EDLDNMKNNK LATGEPASPH DSLGHSGLPP
1060 1070 1080 1090 1100
SPAKIGNSTN PGPALATNPQ NAASRRTPNN PGNPSNPGPP KTPENSLIVT
1110 1120 1130 1140 1150
NPSSTQPNSA KTARKPEHMA VEIPPACPPL NHTVVQVNKN ANPDPLPKKE
1160 1170 1180 1190 1200
EEKKEEEEAD PGEDGPKPMP PYSSMFILST TNPLRRLCHY ILNLRYFEMC
1210 1220 1230 1240 1250
ILMVIAMSSI ALAAEDPVQP NAPRNNVLRY FDYVFTGVFT FEMVIKMIDL
1260 1270 1280 1290 1300
GLVLHQGAYF RDLWNILDFI VVSGALVAFA FTGNSKGKDI NTIKSLRVLR
1310 1320 1330 1340 1350
VLRPLKTIKR LPKLKAVFDC VVNSLKNVFN ILIVYMLFMF IFAVVAVQLF
1360 1370 1380 1390 1400
KGKFFHCTDE SKEFERDCRG KYLLYEKNEV KARDREWKKY EFHYDNVLWA
1410 1420 1430 1440 1450
LLTLFTVSTG EGWPQVLKHS VDATFENQGP SPGYRMEMSI FYVVYFVVFP
1460 1470 1480 1490 1500
FFFVNIFVAL IIITFQEQGD KMMEEYSLEK NERACIDFAI SAKPLTRHMP
1510 1520 1530 1540 1550
QNKQSFQYRM WQFVVSPPFE YTIMAMIALN TIVLMMKFYG ASVAYENALR
1560 1570 1580 1590 1600
VFNIVFTSLF SLECVLKVMA FGILNYFRDA WNIFDFVTVL GSITDILVTE
1610 1620 1630 1640 1650
FGNNFINLSF LRLFRAARLI KLLRQGYTIR ILLWTFVQSF KALPYVCLLI
1660 1670 1680 1690 1700
AMLFFIYAII GMQVFGNIGI DGEDEDSDED EFQITEHNNF RTFFQALMLL
1710 1720 1730 1740 1750
FRSATGEAWH NIMLSCLSGK PCDKNSGILT ADCGNEFAYF YFVSFIFLCS
1760 1770 1780 1790 1800
FLMLNLFVAV IMDNFEYLTR DSSILGPHHL DEYVRVWAEY DPAACGRIHY
1810 1820 1830 1840 1850
KDMYSLLRVI SPPLGLGKKC PHRVACKRLL RMDLPVADDN TVHFNSTLMA
1860 1870 1880 1890 1900
LIRTALDIKI AKGGADKQQM DAELRKEMMA IWPNLSQKTL DLLVTPHKST
1910 1920 1930 1940 1950
DLTVGKIYAA MMIMEYYRQS KAKKLQAMRE EQNRTPLMFQ RMEPPSPTQE
1960 1970 1980 1990 2000
GGPSQNALPS TQLDPGGGLM AHEGGMKESP SWVTQRAQEM FQKTGTWSPE
2010 2020 2030 2040 2050
RGPPIDMPNS QPNSQSVEMR EMGTDGYSDS EHYLPMEGQT RAASMPRLPA
2060 2070 2080 2090 2100
ENQRRRGRPR GNDLSTISDT SPMKRSASVL GPKARRLDDY SLERVPPEEN
2110 2120 2130 2140 2150
QRYHQRRRDR GHRTSERSLG RYTDVDTGLG TDLSMTTQSG DLPSKDRDQD
2160 2170 2180 2190 2200
RGRPKDRKHR PHHHHHHHHH HPPAPDRDRY AQERPDTGRA RAREQRWSRS
2210 2220 2230 2240 2250
PSEGREHTTH RQGSSSVSGS PAPSTSGTST PRRGRRQLPQ TPCTPRPLVS
2260 2270 2280 2290 2300
YSPAPRRPAA RRMAGPAAPP GGSPRGCRRA PRWPAHAPEG PRPRGADYTE
2310 2320 2330 2340 2350
PDSPREPPGG AHDPAPRSPR TPRAAGCASP RHGRRLPNGY YAGHGAPRPR
2360
TARRGAHDAY SESEDDWC
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 ENSGT00760000119135.
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

Bgeei P97445.
ExpressionAtlasi P97445. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 139 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