P97445 (CAC1A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Cacna1a
Synonyms:	Caca1a, Cach4, Cacn3, Cacnl1a4, Ccha1a

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	2368 AA.
Sequence status	Complete.
Protein existence	Evidence 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-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).
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 process	Calcium transport Ion transport Transport
Cellular component	Membrane
Disease	Disease mutation
Domain	Repeat Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding
Molecular function	Calcium channel Ion channel Voltage-gated channel
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adult 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-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 growth Inferred from mutant phenotype PubMed 1306163. Source: MGI cellular chloride ion homeostasis Inferred from mutant phenotype PubMed 10899223PubMed 8565963. Source: MGI cerebellar Purkinje cell differentiation Inferred from mutant phenotype PubMed 10630211PubMed 1306163PubMed 7834360. 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 elevation of cytosolic calcium ion concentration Inferred from sequence or structural similarity. Source: UniProtKB 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 neuromuscular process controlling balance Inferred from mutant phenotype PubMed 4799944. Source: MGI neuromuscular synaptic transmission Inferred from mutant phenotype PubMed 10686170. Source: MGI neurotransmitter metabolic process Inferred from mutant phenotype PubMed 1686215PubMed 6167317PubMed 8100981. Source: MGI receptor clustering Inferred from mutant phenotype PubMed 12624181. Source: MGI regulation of acetylcholine secretion 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 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, glutamatergic Inferred from mutant phenotype PubMed 10322048PubMed 14973254. Source: MGI vestibular nucleus development Inferred from mutant phenotype PubMed 8719615. Source: MGI
Cellular_component	dendrite Inferred from direct assay PubMed 15451373. Source: MGI neuronal cell body Inferred from direct assay PubMed 15451373. Source: MGI voltage-gated calcium channel complex Inferred from direct assay PubMed 10328888. Source: MGI
Molecular_function	DNA 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2368	2368	Voltage-dependent P/Q-type calcium channel subunit alpha-1A		PRO_0000053917
Regions
	Topological domain	1 – 100	100	Cytoplasmic Potential
	Transmembrane	101 – 119	19	Helical; Name=S1 of repeat I; Potential
	Topological domain	120 – 138	19	Extracellular Potential
	Transmembrane	139 – 156	18	Helical; Name=S2 of repeat I; Potential
	Topological domain	157 – 168	12	Cytoplasmic Potential
	Transmembrane	169 – 184	16	Helical; Name=S3 of repeat I; Potential
	Topological domain	185 – 192	8	Extracellular Potential
	Transmembrane	193 – 211	19	Helical; Name=S4 of repeat I; Potential
	Topological domain	212 – 230	19	Cytoplasmic Potential
	Transmembrane	231 – 250	20	Helical; Name=S5 of repeat I; Potential
	Topological domain	251 – 337	87	Extracellular Potential
	Transmembrane	338 – 362	25	Helical; Name=S6 of repeat I; Potential
	Topological domain	363 – 489	127	Cytoplasmic Potential
	Transmembrane	490 – 509	20	Helical; Name=S1 of repeat II; Potential
	Topological domain	510 – 523	14	Extracellular Potential
	Transmembrane	524 – 543	20	Helical; Name=S2 of repeat II; Potential
	Topological domain	544 – 551	8	Cytoplasmic Potential
	Transmembrane	552 – 570	19	Helical; Name=S3 of repeat II; Potential
	Topological domain	571 – 580	10	Extracellular Potential
	Transmembrane	581 – 599	19	Helical; Name=S4 of repeat II; Potential
	Topological domain	600 – 618	19	Cytoplasmic Potential
	Transmembrane	619 – 638	20	Helical; Name=S5 of repeat II; Potential
	Topological domain	639 – 691	53	Extracellular Potential
	Transmembrane	692 – 716	25	Helical; Name=S6 of repeat II; Potential
	Topological domain	717 – 1190	474	Cytoplasmic Potential
	Transmembrane	1191 – 1214	24	Helical; Name=S1 of repeat III; Potential
	Topological domain	1215 – 1231	17	Extracellular Potential
	Transmembrane	1232 – 1251	20	Helical; Name=S2 of repeat III; Potential
	Topological domain	1252 – 1258	7	Cytoplasmic Potential
	Transmembrane	1259 – 1282	24	Helical; Name=S3 of repeat III; Potential
	Topological domain	1283 – 1293	11	Extracellular Potential
	Transmembrane	1294 – 1311	18	Helical; Name=S4 of repeat III; Potential
	Topological domain	1312 – 1330	19	Cytoplasmic Potential
	Transmembrane	1331 – 1350	20	Helical; Name=S5 of repeat III; Potential
	Topological domain	1351 – 1437	87	Extracellular Potential
	Transmembrane	1438 – 1462	25	Helical; Name=S6 of repeat III; Potential
	Topological domain	1463 – 1518	56	Cytoplasmic Potential
	Transmembrane	1519 – 1537	19	Helical; Name=S1 of repeat IV; Potential
	Topological domain	1538 – 1551	14	Extracellular Potential
	Transmembrane	1552 – 1573	22	Helical; Name=S2 of repeat IV; Potential
	Topological domain	1574 – 1580	7	Cytoplasmic Potential
	Transmembrane	1581 – 1600	20	Helical; Name=S3 of repeat IV; Potential
	Topological domain	1601 – 1607	7	Extracellular Potential
	Transmembrane	1608 – 1626	19	Helical; Name=S4 of repeat IV; Potential
	Topological domain	1627 – 1645	19	Cytoplasmic Potential
	Transmembrane	1646 – 1665	20	Helical; Name=S5 of repeat IV; Potential
	Topological domain	1666 – 1737	72	Extracellular Potential
	Transmembrane	1738 – 1763	26	Helical; Name=S6 of repeat IV; Potential
	Topological domain	1764 – 2368	605	Cytoplasmic Potential
	Repeat	65 – 365	301	I
	Repeat	475 – 719	245	II
	Repeat	1182 – 1465	284	III
	Repeat	1502 – 1765	264	IV
	Calcium binding	1791 – 1802	12	By similarity
	Region	385 – 402	18	Binding to the beta subunit By similarity
	Compositional bias	729 – 734	6	Poly-Glu
	Compositional bias	1155 – 1158	4	Poly-Glu
Sites
	Site	320	1	Calcium ion selectivity and permeability By similarity
	Site	670	1	Calcium ion selectivity and permeability By similarity
	Site	1411	1	Calcium ion selectivity and permeability By similarity
	Site	1600	1	Binds to omega-Aga-IVA By similarity
	Site	1707	1	Calcium ion selectivity and permeability By similarity
Amino acid modifications
	Modified residue	752	1	Phosphoserine Ref.3
	Modified residue	1981	1	Phosphoserine Ref.3
	Modified residue	2027	1	Phosphotyrosine Ref.3
	Modified residue	2220	1	Phosphoserine Ref.3
	Modified residue	2273	1	Phosphoserine Ref.3
	Glycosylation	285	1	N-linked (GlcNAc...) Potential
	Glycosylation	1607	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	649	1	P → L in tg. Ref.2
Experimental info
	Sequence conflict	79	1	S → P in AAC52940. Ref.2
	Sequence conflict	82	1	L → F in AAC52940. Ref.2
	Sequence conflict	884	1	P → L in AAC52940. Ref.2
	Sequence conflict	888	1	E → D in AAW56205. Ref.1
	Sequence conflict	1083	1	N → D in AAC52940. Ref.2
	Sequence conflict	1349	1	L → F in AAC52940. Ref.2
	Sequence conflict	1373	1	L → F in AAC52940. Ref.2
	Sequence conflict	2161	1	P → PH in AAW56205. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P97445 [UniParc]. Last modified February 6, 2007. Version 2. Checksum: E7B573BA005E5CB1	FASTA	2,368	267,647
	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

References

	« Hide 'large scale' referencesShow '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]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-752; SER-1981; TYR-2027; SER-2220 AND SER-2273, MASS SPECTROMETRY. Tissue: Brain cortex.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY714490 mRNA. Translation: AAW56205.1. U76716 mRNA. Translation: AAC52940.1.
IPI	IPI00408646.
RefSeq	NP_031604.3. NM_007578.3.
UniGene	Mm.334658.
3D structure databases
ProteinModelPortal	P97445.
SMR	P97445. Positions 96-361, 369-412, 491-717, 1191-1462, 1509-1763, 1846-1923.
ModBase	Search...
Protein-protein interaction databases
IntAct	P97445. 1 interaction.
MINT	MINT-4997013.
PTM databases
PhosphoSite	P97445.
Proteomic databases
PaxDb	P97445.
PRIDE	P97445.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000121390; ENSMUSP00000112436; ENSMUSG00000034656.
GeneID	12286.
KEGG	mmu:12286.
UCSC	uc009mmn.2. mouse.
Organism-specific databases
CTD	773.
MGI	MGI:109482. Cacna1a.
Phylogenomic databases
eggNOG	COG1226.
GeneTree	ENSGT00680000099892.
HOGENOM	HOG000231530.
HOVERGEN	HBG050763.
InParanoid	P97445.
KO	K04344.
OMA	QPGFWEG.
OrthoDB	EOG48KR9C.
Gene expression databases
ArrayExpress	P97445.
Bgee	P97445.
Genevestigator	P97445.
GermOnline	ENSMUSG00000034656. Mus musculus.
Family and domain databases
Gene3D	1.20.120.350. 4 hits.
InterPro	IPR017956. AT_hook_DNA-bd_motif. IPR005821. Ion_trans_dom. IPR027359. K_channel_four-helix_dom. IPR014873. VDCC_a1su_IQ. IPR005448. VDCC_P/Q_a1su. IPR002077. VDCCAlpha1. [Graphical view]
PANTHER	PTHR10037:SF59. PTHR10037:SF59. 1 hit.
Pfam	PF08763. Ca_chan_IQ. 1 hit. PF00520. Ion_trans. 4 hits. [Graphical view]
PRINTS	PR00167. CACHANNEL. PR01632. PQVDCCALPHA1.
SMART	SM00384. AT_hook. 1 hit. SM01062. Ca_chan_IQ. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	280756.
SOURCE	Search...

Entry information

Entry name

CAC1A_MOUSE

Accession

Primary (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:	May 29, 2013
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program