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Protein

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

Gene

CACNA1A

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: 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
Sitei318 – 3181Calcium ion selectivity and permeabilityBy similarity
Sitei668 – 6681Calcium ion selectivity and permeabilityBy similarity
Sitei1469 – 14691Calcium ion selectivity and permeabilityBy similarity
Sitei1658 – 16581Binds to omega-Aga-IVA
Sitei1765 – 17651Calcium ion selectivity and permeabilityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi1849 – 186012By similarityAdd
BLAST

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • protein C-terminus binding Source: UniProtKB
  • voltage-gated calcium channel activity Source: UniProtKB

GO - Biological processi

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

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:CACH4, CACN3, CACNL1A4
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 9898CytoplasmicSequence analysisAdd
BLAST
Transmembranei99 – 11719Helical; Name=S1 of repeat ISequence analysisAdd
BLAST
Topological domaini118 – 13518ExtracellularSequence analysisAdd
BLAST
Transmembranei136 – 15520Helical; Name=S2 of repeat ISequence analysisAdd
BLAST
Topological domaini156 – 16712CytoplasmicSequence analysisAdd
BLAST
Transmembranei168 – 18518Helical; Name=S3 of repeat ISequence analysisAdd
BLAST
Topological domaini186 – 1905ExtracellularSequence analysis
Transmembranei191 – 20919Helical; Name=S4 of repeat ISequence analysisAdd
BLAST
Topological domaini210 – 22819CytoplasmicSequence analysisAdd
BLAST
Transmembranei229 – 24820Helical; Name=S5 of repeat ISequence analysisAdd
BLAST
Topological domaini249 – 33587ExtracellularSequence analysisAdd
BLAST
Transmembranei336 – 36025Helical; Name=S6 of repeat ISequence analysisAdd
BLAST
Topological domaini361 – 487127CytoplasmicSequence analysisAdd
BLAST
Transmembranei488 – 50619Helical; Name=S1 of repeat IISequence analysisAdd
BLAST
Topological domaini507 – 52115ExtracellularSequence analysisAdd
BLAST
Transmembranei522 – 54120Helical; Name=S2 of repeat IISequence analysisAdd
BLAST
Topological domaini542 – 5498CytoplasmicSequence analysis
Transmembranei550 – 56819Helical; Name=S3 of repeat IISequence analysisAdd
BLAST
Topological domaini569 – 57810ExtracellularSequence analysis
Transmembranei579 – 59719Helical; Name=S4 of repeat IISequence analysisAdd
BLAST
Topological domaini598 – 61619CytoplasmicSequence analysisAdd
BLAST
Transmembranei617 – 63620Helical; Name=S5 of repeat IISequence analysisAdd
BLAST
Topological domaini637 – 68953ExtracellularSequence analysisAdd
BLAST
Transmembranei690 – 71425Helical; Name=S6 of repeat IISequence analysisAdd
BLAST
Topological domaini715 – 1253539CytoplasmicSequence analysisAdd
BLAST
Transmembranei1254 – 127219Helical; Name=S1 of repeat IIISequence analysisAdd
BLAST
Topological domaini1273 – 128816ExtracellularSequence analysisAdd
BLAST
Transmembranei1289 – 130820Helical; Name=S2 of repeat IIISequence analysisAdd
BLAST
Topological domaini1309 – 132012CytoplasmicSequence analysisAdd
BLAST
Transmembranei1321 – 133919Helical; Name=S3 of repeat IIISequence analysisAdd
BLAST
Topological domaini1340 – 135011ExtracellularSequence analysisAdd
BLAST
Transmembranei1351 – 136919Helical; Name=S4 of repeat IIISequence analysisAdd
BLAST
Topological domaini1370 – 138819CytoplasmicSequence analysisAdd
BLAST
Transmembranei1389 – 140820Helical; Name=S5 of repeat IIISequence analysisAdd
BLAST
Topological domaini1409 – 149587ExtracellularSequence analysisAdd
BLAST
Transmembranei1496 – 152025Helical; Name=S6 of repeat IIISequence analysisAdd
BLAST
Topological domaini1521 – 157555CytoplasmicSequence analysisAdd
BLAST
Transmembranei1576 – 160429Helical; Name=S1 of repeat IVSequence analysisAdd
BLAST
Topological domaini1605 – 16095ExtracellularSequence analysis
Transmembranei1610 – 162920Helical; Name=S2 of repeat IVSequence analysisAdd
BLAST
Topological domaini1630 – 16378CytoplasmicSequence analysis
Transmembranei1638 – 165619Helical; Name=S3 of repeat IVSequence analysisAdd
BLAST
Topological domaini1657 – 16659ExtracellularSequence analysis
Transmembranei1666 – 168419Helical; Name=S4 of repeat IVSequence analysisAdd
BLAST
Topological domaini1685 – 170319CytoplasmicSequence analysisAdd
BLAST
Transmembranei1704 – 172320Helical; Name=S5 of repeat IVSequence analysisAdd
BLAST
Topological domaini1724 – 179572ExtracellularSequence analysisAdd
BLAST
Transmembranei1796 – 182025Helical; Name=S6 of repeat IVSequence analysisAdd
BLAST
Topological domaini1821 – 2424604CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • voltage-gated calcium channel complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi188 – 1881E → K: No change in inhibition by omega-Aga-IVA. 1 Publication
Mutagenesisi386 – 3861E → S: Reduced beta-subunit interaction. 1 Publication
Mutagenesisi389 – 3891L → H: Reduced beta-subunit interaction. 1 Publication
Mutagenesisi392 – 3921Y → S: Reduced beta-subunit interaction. 1 Publication
Mutagenesisi400 – 4001E → A: No effect on beta-subunit interaction. 1 Publication
Mutagenesisi1658 – 16581E → K: Loss of inhibition by omega-Aga-IVA. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24242424Voltage-dependent P/Q-type calcium channel subunit alpha-1APRO_0000053918Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi283 – 2831N-linked (GlcNAc...)Sequence analysis
Modified residuei409 – 4091PhosphothreonineBy similarity
Modified residuei448 – 4481PhosphoserineBy similarity
Modified residuei451 – 4511PhosphoserineBy similarity
Modified residuei750 – 7501PhosphoserineBy similarity
Modified residuei753 – 7531PhosphoserineBy similarity
Modified residuei790 – 7901PhosphoserineBy similarity
Modified residuei1091 – 10911PhosphoserineBy similarity
Modified residuei1104 – 11041PhosphoserineBy similarity
Glycosylationi1665 – 16651N-linked (GlcNAc...)Sequence analysis
Modified residuei1831 – 18311Phosphoserine; by PKASequence analysis
Modified residuei1993 – 19931PhosphothreonineBy similarity
Modified residuei2054 – 20541PhosphoserineBy similarity
Modified residuei2072 – 20721PhosphoserineBy similarity
Modified residuei2084 – 20841PhosphoserineBy similarity
Modified residuei2086 – 20861PhosphoserineBy similarity
Modified residuei2127 – 21271PhosphoserineBy similarity
Modified residuei2148 – 21481PhosphoserineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Expressioni

Tissue specificityi

Brain specific. Purkinje cells contain predominantly P-type VSCC, the Q-type being a prominent calcium current in cerebellar granule cells.

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

GO - Molecular functioni

  • protein C-terminus binding Source: UniProtKB

Protein-protein interaction databases

DIPiDIP-29591N.

Structurei

Secondary structure

1
2424
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1963 – 197917Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DVMX-ray2.60B1963-1982[»]
ProteinModelPortaliP27884.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27884.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati85 – 363279IAdd
BLAST
Repeati473 – 717245IIAdd
BLAST
Repeati1240 – 1523284IIIAdd
BLAST
Repeati1560 – 1823264IVAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni383 – 40018Binding to the beta subunitAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi13 – 186Poly-Gly
Compositional biasi727 – 7326Poly-Glu
Compositional biasi1004 – 10107Poly-Gly
Compositional biasi1012 – 10176Poly-Arg
Compositional biasi2219 – 22279Poly-His
Compositional biasi2242 – 22465Poly-Arg
Compositional biasi2288 – 229710Poly-Arg
Compositional biasi2298 – 23014Poly-Gly
Compositional biasi2372 – 23776Poly-Pro
Compositional biasi2411 – 24166Poly-Gly

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

HOVERGENiHBG050763.
InParanoidiP27884.
KOiK04344.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR005448. CACNA1A.
IPR027359. Channel_four-helix_dom.
IPR031649. GPHH_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR002077. VDCCAlpha1.
[Graphical view]
PANTHERiPTHR10037:SF59. PTHR10037:SF59. 4 hits.
PfamiPF08763. Ca_chan_IQ. 1 hit.
PF16905. GPHH. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSiPR00167. CACHANNEL.
PR01632. PQVDCCALPHA1.
SMARTiSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform BI-2 (identifier: P27884-1) [UniParc]FASTAAdd to basket

Also known as: 1A-2

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MARFGDEMPA RYGGGGAGAA AGVVVGAAGG RGAGGSRQGG QPGAQRMYKQ
60 70 80 90 100
SMAQRARTMA LYNPIPVRQN CLTVNRSLFL FSEDNVVRKY AKKITEWPPF
110 120 130 140 150
EYMILATIIA NCIVLALEQH LPDDDKTPMS ERLDDTEPYF IGIFCFEAGI
160 170 180 190 200
KIIALGFAFH KGSYLRNGWN VMDFVVVLTG ILATVGTEFD LRTLRAVRVL
210 220 230 240 250
RPLKLVSGIP SLQVVLKSIM KAMIPLLQIG LLLFFAILIF AIIGLEFYMG
260 270 280 290 300
KFHTTCFEEG TDDIQGESPA PCGTEEPART CPNGTRCQPY WEGPNNGITQ
310 320 330 340 350
FDNILFAVLT VFQCITMEGW TDLLYNSNDA SGNTWNWLYF IPLIIIGSFF
360 370 380 390 400
MLNLVLGVLS GEFAKERERV ENRRAFLKLR RQQQIERELN GYMEWISKAE
410 420 430 440 450
EVILAEDETD VEQRHPFDGA LRRATIKKSK TDLLHPEEAE DQLADIASVG
460 470 480 490 500
SPFARASIKS AKLENSSFFH KKERRMRFYI RRMVKTQAFY WTVLSLVALN
510 520 530 540 550
TLCVAIVHYN QPEWLSDFLY YAEFIFLGLF MSEMFIKMYG LGTRPYFHSS
560 570 580 590 600
FNCFDCGVII GSIFEVIWAV IKPGTSFGIS VLRALRLLRI FKVTKYWASL
610 620 630 640 650
RNLVVSLLNS MKSIISLLFL LFLFIVVFAL LGMQLFGGQF NFDEGTPPTN
660 670 680 690 700
FDTFPAAIMT VFQILTGEDW NEVMYDGIKS QGGVQGGMVF SIYFIVLTLF
710 720 730 740 750
GNYTLLNVFL AIAVDNLANA QELTKDEQEE EEAVNQKLAL QKAKEVAEVS
760 770 780 790 800
PLSAANMSIA MKEQQKNQKP AKSVWEQRTS EMRKQNLLAS REALYSEMDP
810 820 830 840 850
EERWKASYAR HLRPDMKTHL DRPLVVDPQE NRNNNTNKSR VAEPTVDQRL
860 870 880 890 900
GQQRAEDFLR KQARHHDRAR DPSAHAAAGL DARRPWAGSQ EAELSREGPY
910 920 930 940 950
GRESDHQARE GGLEPPGFWE GEAERGKAGD PHRRHAHRQG VGGSGGSRSG
960 970 980 990 1000
SPRTGTADGE PRRHRVHRRP GEDGPDDKAE RRGRHREGSR PARSGEGEAE
1010 1020 1030 1040 1050
GPDGGGGGGG ERRRRHRHGP PPAYDPDARR DDRERRHRRR KDTQGSGVPV
1060 1070 1080 1090 1100
SGPNLSTTRP IQQDLSRQEP PLAEDMDNLK NSRLATAEPV SPHENLSHAG
1110 1120 1130 1140 1150
LPQSPAKMGS STDPAGPTPA TAANPQNSTA SRRTPNNPGN PSNPGPPKTP
1160 1170 1180 1190 1200
ENSLIVTNPS TAQTNSAKTA RKPDHTTVEI PPACPPPLNH TVVQVNKNAN
1210 1220 1230 1240 1250
PDPLPKKEDE KKEEVDEGPG EDGPKPMPPY SSMFILSTTN PLRRLCHYIL
1260 1270 1280 1290 1300
NLRYFEMCIL MVIAMSSIAL AAEDPVQPNA PRNNVLRYFD YVFTGVFTFE
1310 1320 1330 1340 1350
MVIKMIDLGL VLHQGAYFRD LWNILDFIVV SGALVAFAFT GNSKGKDINT
1360 1370 1380 1390 1400
IKSLRVLRVL RPLKTIKRLP KLKAVFDCVV NSLKNVFNIL IVYMLFMFIF
1410 1420 1430 1440 1450
AVVAVQLFKG KFFHCTDESK EFEKDCRGKY LLYEKNEVKA RDREWKKYEF
1460 1470 1480 1490 1500
HYDNVLWALL TLFTVSTGEG WPQVLKHSVD ATFENQGPSP GYRMEMSIFY
1510 1520 1530 1540 1550
VVYFVVFPFF FVNIFVALII ITFQEQGDKM MEEYSLEKNE RACIDFAISA
1560 1570 1580 1590 1600
KPLTRHMPQN KQSFQYRMWQ FVVSPPFEYT IMAMIALNTI VLMMKFYGAS
1610 1620 1630 1640 1650
VAYDNALKVF NIVFTSLFSL ECLLKVLAFG ILNYFRDAWN IFDFVTVLGS
1660 1670 1680 1690 1700
ITDILVTEFG NNFINLSFLR LFRAARLIKL LRQGYTIRIL LWTFVQSFKA
1710 1720 1730 1740 1750
LPYVCLLIAM LFFIYAIIGM QVFGNIGIDM EDEDSDEDEF QITEHNNFRT
1760 1770 1780 1790 1800
FFQALMLLFR SATGEAWHNI MLSCLSGKPC DKNSGILTPE CGNEFAYFYF
1810 1820 1830 1840 1850
VSFIFLCSFL MLNLFVAVIM DNFEYLTRDS SILGPHHLDE YVRVWAEYDP
1860 1870 1880 1890 1900
AAWGRMLYRD MYAMLRHMPP PLGLGKNCPA RVAYKRLLRM DLPVADDNTV
1910 1920 1930 1940 1950
HFNSTLMALI RTALDIKIAK GGADKQQMDA ELRKEMMAIW PNLSQKTLDL
1960 1970 1980 1990 2000
LVTPHKSTDL TVGKIYAAMM IMEYYRQSKA KKLQAMREEQ NRTPLMFQRM
2010 2020 2030 2040 2050
EPPPDEGGAG QNALPSTQLD PAGGLMAHED GLKDSPSWVT QRAQEMFQKT
2060 2070 2080 2090 2100
GTWSPERAPP ADMADSQPKP QSVEMREMSQ DGYSDSEHCL PMEGQARAAS
2110 2120 2130 2140 2150
MPRLPAENQR RRGRPRGSDL STICDTSPMK RSASVLGPKA SRRLDDYSLE
2160 2170 2180 2190 2200
RVPPEENQRH HPRRRERAHR TSERSLGRYT DVDTGLGTDL SMTTQSGDLP
2210 2220 2230 2240 2250
SREREQERGR PKDRKHRPHH HHHHHHHPGR GPGRVSPGVS ARRRRRGPVA
2260 2270 2280 2290 2300
RVRPARAPAL AHARARARAP ARLLPELRLR RARRPRPRQR RRPRRRRGGG
2310 2320 2330 2340 2350
GRALRRAPGP REPLAQDSPG RGPSVCLARA ARPAGPQRLL PGPRTGQAPR
2360 2370 2380 2390 2400
ARLPQKPARS VQRERRGLVL SPPPPPPGEL APRAHPARTP RPGPGDSRSR
2410 2420
RGGRRWTASA GKGGGGPRAS APSP
Length:2,424
Mass (Da):273,231
Last modified:July 1, 1993 - v1
Checksum:iF7CC4D0AB4B45604
GO
Isoform BI-1 (identifier: P27884-2) [UniParc]FASTAAdd to basket

Also known as: 1A-1

The sequence of this isoform differs from the canonical sequence as follows:
     2230-2273: RGPGRVSPGV...RARARAPARL → PAAADKERYG...EGREHTTHRQ
     2274-2424: Missing.

Show »
Length:2,273
Mass (Da):257,351
Checksum:iB14B3FA4E801D8D4
GO
Isoform CBP101 (identifier: P27884-3) [UniParc]FASTAAdd to basket

Also known as: CBP109

The sequence of this isoform differs from the canonical sequence as follows:
     1857-1884: LYRDMYAMLRHMPPPLGLGKNCPARVAY → HYKDMYSLLRVISPPLGLGKKCPHRVAC

Show »
Length:2,424
Mass (Da):273,179
Checksum:iFADE1090207B5822
GO
Isoform CBP103 (identifier: P27884-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     772-1120: Missing.

Show »
Length:2,075
Mass (Da):234,541
Checksum:i7EB161F547B14151
GO
Isoform CBP107 (identifier: P27884-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     772-1051: Missing.

Show »
Length:2,144
Mass (Da):241,749
Checksum:i726B65549B57B475
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti419 – 4191Missing in isoform CBP315.
Natural varianti877 – 8771A → T in isoform CBS.
Natural varianti1104 – 11041S → N in isoform CBS.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei772 – 1120349Missing in isoform CBP103. CuratedVSP_000877Add
BLAST
Alternative sequencei772 – 1051280Missing in isoform CBP107. CuratedVSP_000876Add
BLAST
Alternative sequencei1857 – 188428LYRDM…ARVAY → HYKDMYSLLRVISPPLGLGK KCPHRVAC in isoform CBP101. CuratedVSP_000878Add
BLAST
Alternative sequencei2230 – 227344RGPGR…APARL → PAAADKERYGPQDRPDHGHG RARARDQRWSRSPSEGREHT THRQ in isoform BI-1. CuratedVSP_000879Add
BLAST
Alternative sequencei2274 – 2424151Missing in isoform BI-1. CuratedVSP_000880Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57477 mRNA. Translation: CAA40715.1.
X57689 mRNA. Translation: CAA40872.1.
X57476 mRNA. Translation: CAA40714.1.
X57688 mRNA. Translation: CAA40871.1.
PIRiI46477.
I46480.
RefSeqiNP_001095163.1. NM_001101693.1. [P27884-2]
UniGeneiOcu.2123.

Genome annotation databases

GeneIDi100009265.
KEGGiocu:100009265.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57477 mRNA. Translation: CAA40715.1.
X57689 mRNA. Translation: CAA40872.1.
X57476 mRNA. Translation: CAA40714.1.
X57688 mRNA. Translation: CAA40871.1.
PIRiI46477.
I46480.
RefSeqiNP_001095163.1. NM_001101693.1. [P27884-2]
UniGeneiOcu.2123.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DVMX-ray2.60B1963-1982[»]
ProteinModelPortaliP27884.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29591N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009265.
KEGGiocu:100009265.

Organism-specific databases

CTDi773.

Phylogenomic databases

HOVERGENiHBG050763.
InParanoidiP27884.
KOiK04344.

Miscellaneous databases

EvolutionaryTraceiP27884.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR005448. CACNA1A.
IPR027359. Channel_four-helix_dom.
IPR031649. GPHH_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR002077. VDCCAlpha1.
[Graphical view]
PANTHERiPTHR10037:SF59. PTHR10037:SF59. 4 hits.
PfamiPF08763. Ca_chan_IQ. 1 hit.
PF16905. GPHH. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSiPR00167. CACHANNEL.
PR01632. PQVDCCALPHA1.
SMARTiSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Primary structure and functional expression from complementary DNA of a brain calcium channel."
    Mori Y., Friedrich T., Kim M.-S., Mikami A., Nakai J., Ruth P., Bosse E., Hofmann F., Flockerzi V., Furuichi T., Mikoshiba K., Imoto K., Tanabe T., Numa S.
    Nature 350:398-402(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
    Tissue: Brain.
  2. "Calcium channel beta-subunit binds to a conserved motif in the I-II cytoplasmic linker of the alpha 1-subunit."
    Pragnell M., de Waard M., Mori Y., Tanabe T., Snutch T.P., Campbell K.P.
    Nature 368:67-70(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: BETA-SUBUNIT BINDING DOMAIN, MUTAGENESIS OF GLU-386; LEU-389; TYR-392 AND GLU-400.
  3. "A hot spot for the interaction of gating modifier toxins with voltage-dependent ion channels."
    Winterfield J.R., Swartz K.J.
    J. Gen. Physiol. 116:637-644(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLU-188 AND GLU-1658.

Entry informationi

Entry nameiCAC1A_RABIT
AccessioniPrimary (citable) accession number: P27884
Secondary accession number(s): P27883
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: July 6, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.