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P27884 (CAC1A_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 101. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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:CACH4, CACN3, CACNL1A4
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length2424 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-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. Ref.2

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Brain specific. 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. Ref.2

Sequence similarities

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

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform BI-2 (identifier: P27884-1)

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.
Isoform BI-1 (identifier: P27884-2)

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.
Isoform CBP101 (identifier: P27884-3)

Also known as: CBP109;

The sequence of this isoform differs from the canonical sequence as follows:
     1857-1884: LYRDMYAMLRHMPPPLGLGKNCPARVAY → HYKDMYSLLRVISPPLGLGKKCPHRVAC
Isoform CBP103 (identifier: P27884-4)

The sequence of this isoform differs from the canonical sequence as follows:
     772-1120: Missing.
Isoform CBP107 (identifier: P27884-5)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24242424Voltage-dependent P/Q-type calcium channel subunit alpha-1A
PRO_0000053918

Regions

Topological domain1 – 9898Cytoplasmic Potential
Transmembrane99 – 11719Helical; Name=S1 of repeat I; Potential
Topological domain118 – 13518Extracellular Potential
Transmembrane136 – 15520Helical; Name=S2 of repeat I; Potential
Topological domain156 – 16712Cytoplasmic Potential
Transmembrane168 – 18518Helical; Name=S3 of repeat I; Potential
Topological domain186 – 1905Extracellular Potential
Transmembrane191 – 20919Helical; Name=S4 of repeat I; Potential
Topological domain210 – 22819Cytoplasmic Potential
Transmembrane229 – 24820Helical; Name=S5 of repeat I; Potential
Topological domain249 – 33587Extracellular Potential
Transmembrane336 – 36025Helical; Name=S6 of repeat I; Potential
Topological domain361 – 487127Cytoplasmic Potential
Transmembrane488 – 50619Helical; Name=S1 of repeat II; Potential
Topological domain507 – 52115Extracellular Potential
Transmembrane522 – 54120Helical; Name=S2 of repeat II; Potential
Topological domain542 – 5498Cytoplasmic Potential
Transmembrane550 – 56819Helical; Name=S3 of repeat II; Potential
Topological domain569 – 57810Extracellular Potential
Transmembrane579 – 59719Helical; Name=S4 of repeat II; Potential
Topological domain598 – 61619Cytoplasmic Potential
Transmembrane617 – 63620Helical; Name=S5 of repeat II; Potential
Topological domain637 – 68953Extracellular Potential
Transmembrane690 – 71425Helical; Name=S6 of repeat II; Potential
Topological domain715 – 1253539Cytoplasmic Potential
Transmembrane1254 – 127219Helical; Name=S1 of repeat III; Potential
Topological domain1273 – 128816Extracellular Potential
Transmembrane1289 – 130820Helical; Name=S2 of repeat III; Potential
Topological domain1309 – 132012Cytoplasmic Potential
Transmembrane1321 – 133919Helical; Name=S3 of repeat III; Potential
Topological domain1340 – 135011Extracellular Potential
Transmembrane1351 – 136919Helical; Name=S4 of repeat III; Potential
Topological domain1370 – 138819Cytoplasmic Potential
Transmembrane1389 – 140820Helical; Name=S5 of repeat III; Potential
Topological domain1409 – 149587Extracellular Potential
Transmembrane1496 – 152025Helical; Name=S6 of repeat III; Potential
Topological domain1521 – 157555Cytoplasmic Potential
Transmembrane1576 – 160429Helical; Name=S1 of repeat IV; Potential
Topological domain1605 – 16095Extracellular Potential
Transmembrane1610 – 162920Helical; Name=S2 of repeat IV; Potential
Topological domain1630 – 16378Cytoplasmic Potential
Transmembrane1638 – 165619Helical; Name=S3 of repeat IV; Potential
Topological domain1657 – 16659Extracellular Potential
Transmembrane1666 – 168419Helical; Name=S4 of repeat IV; Potential
Topological domain1685 – 170319Cytoplasmic Potential
Transmembrane1704 – 172320Helical; Name=S5 of repeat IV; Potential
Topological domain1724 – 179572Extracellular Potential
Transmembrane1796 – 182025Helical; Name=S6 of repeat IV; Potential
Topological domain1821 – 2424604Cytoplasmic Potential
Repeat85 – 363279I
Repeat473 – 717245II
Repeat1240 – 1523284III
Repeat1560 – 1823264IV
Calcium binding1849 – 186012 By similarity
Region383 – 40018Binding to the beta subunit
Compositional bias13 – 186Poly-Gly
Compositional bias727 – 7326Poly-Glu
Compositional bias1004 – 10107Poly-Gly
Compositional bias1012 – 10176Poly-Arg
Compositional bias2219 – 22279Poly-His
Compositional bias2242 – 22465Poly-Arg
Compositional bias2288 – 229710Poly-Arg
Compositional bias2298 – 23014Poly-Gly
Compositional bias2372 – 23776Poly-Pro
Compositional bias2411 – 24166Poly-Gly

Sites

Site3181Calcium ion selectivity and permeability By similarity
Site6681Calcium ion selectivity and permeability By similarity
Site14691Calcium ion selectivity and permeability By similarity
Site16581Binds to omega-Aga-IVA
Site17651Calcium ion selectivity and permeability By similarity

Amino acid modifications

Modified residue7501Phosphoserine By similarity
Modified residue18311Phosphoserine; by PKA Potential
Modified residue20371Phosphoserine By similarity
Modified residue20831Phosphotyrosine By similarity
Glycosylation2831N-linked (GlcNAc...) Potential
Glycosylation16651N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence772 – 1120349Missing in isoform CBP103.
VSP_000877
Alternative sequence772 – 1051280Missing in isoform CBP107.
VSP_000876
Alternative sequence1857 – 188428LYRDM…ARVAY → HYKDMYSLLRVISPPLGLGK KCPHRVAC in isoform CBP101.
VSP_000878
Alternative sequence2230 – 227344RGPGR…APARL → PAAADKERYGPQDRPDHGHG RARARDQRWSRSPSEGREHT THRQ in isoform BI-1.
VSP_000879
Alternative sequence2274 – 2424151Missing in isoform BI-1.
VSP_000880
Natural variant4191Missing in isoform CBP315.
Natural variant8771A → T in isoform CBS.
Natural variant11041S → N in isoform CBS.

Experimental info

Mutagenesis1881E → K: No change in inhibition by omega-Aga-IVA. Ref.3
Mutagenesis3861E → S: Reduced beta-subunit interaction. Ref.2
Mutagenesis3891L → H: Reduced beta-subunit interaction. Ref.2
Mutagenesis3921Y → S: Reduced beta-subunit interaction. Ref.2
Mutagenesis4001E → A: No effect on beta-subunit interaction. Ref.2
Mutagenesis16581E → K: Loss of inhibition by omega-Aga-IVA. Ref.3

Secondary structure

1 ... 2424
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform BI-2 (1A-2) [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: F7CC4D0AB4B45604

FASTA2,424273,231
        10         20         30         40         50         60 
MARFGDEMPA RYGGGGAGAA AGVVVGAAGG RGAGGSRQGG QPGAQRMYKQ SMAQRARTMA 

        70         80         90        100        110        120 
LYNPIPVRQN CLTVNRSLFL FSEDNVVRKY AKKITEWPPF EYMILATIIA NCIVLALEQH 

       130        140        150        160        170        180 
LPDDDKTPMS ERLDDTEPYF IGIFCFEAGI KIIALGFAFH KGSYLRNGWN VMDFVVVLTG 

       190        200        210        220        230        240 
ILATVGTEFD LRTLRAVRVL RPLKLVSGIP SLQVVLKSIM KAMIPLLQIG LLLFFAILIF 

       250        260        270        280        290        300 
AIIGLEFYMG KFHTTCFEEG TDDIQGESPA PCGTEEPART CPNGTRCQPY WEGPNNGITQ 

       310        320        330        340        350        360 
FDNILFAVLT VFQCITMEGW TDLLYNSNDA SGNTWNWLYF IPLIIIGSFF MLNLVLGVLS 

       370        380        390        400        410        420 
GEFAKERERV ENRRAFLKLR RQQQIERELN GYMEWISKAE EVILAEDETD VEQRHPFDGA 

       430        440        450        460        470        480 
LRRATIKKSK TDLLHPEEAE DQLADIASVG SPFARASIKS AKLENSSFFH KKERRMRFYI 

       490        500        510        520        530        540 
RRMVKTQAFY WTVLSLVALN TLCVAIVHYN QPEWLSDFLY YAEFIFLGLF MSEMFIKMYG 

       550        560        570        580        590        600 
LGTRPYFHSS FNCFDCGVII GSIFEVIWAV IKPGTSFGIS VLRALRLLRI FKVTKYWASL 

       610        620        630        640        650        660 
RNLVVSLLNS MKSIISLLFL LFLFIVVFAL LGMQLFGGQF NFDEGTPPTN FDTFPAAIMT 

       670        680        690        700        710        720 
VFQILTGEDW NEVMYDGIKS QGGVQGGMVF SIYFIVLTLF GNYTLLNVFL AIAVDNLANA 

       730        740        750        760        770        780 
QELTKDEQEE EEAVNQKLAL QKAKEVAEVS PLSAANMSIA MKEQQKNQKP AKSVWEQRTS 

       790        800        810        820        830        840 
EMRKQNLLAS REALYSEMDP EERWKASYAR HLRPDMKTHL DRPLVVDPQE NRNNNTNKSR 

       850        860        870        880        890        900 
VAEPTVDQRL GQQRAEDFLR KQARHHDRAR DPSAHAAAGL DARRPWAGSQ EAELSREGPY 

       910        920        930        940        950        960 
GRESDHQARE GGLEPPGFWE GEAERGKAGD PHRRHAHRQG VGGSGGSRSG SPRTGTADGE 

       970        980        990       1000       1010       1020 
PRRHRVHRRP GEDGPDDKAE RRGRHREGSR PARSGEGEAE GPDGGGGGGG ERRRRHRHGP 

      1030       1040       1050       1060       1070       1080 
PPAYDPDARR DDRERRHRRR KDTQGSGVPV SGPNLSTTRP IQQDLSRQEP PLAEDMDNLK 

      1090       1100       1110       1120       1130       1140 
NSRLATAEPV SPHENLSHAG LPQSPAKMGS STDPAGPTPA TAANPQNSTA SRRTPNNPGN 

      1150       1160       1170       1180       1190       1200 
PSNPGPPKTP ENSLIVTNPS TAQTNSAKTA RKPDHTTVEI PPACPPPLNH TVVQVNKNAN 

      1210       1220       1230       1240       1250       1260 
PDPLPKKEDE KKEEVDEGPG EDGPKPMPPY SSMFILSTTN PLRRLCHYIL NLRYFEMCIL 

      1270       1280       1290       1300       1310       1320 
MVIAMSSIAL AAEDPVQPNA PRNNVLRYFD YVFTGVFTFE MVIKMIDLGL VLHQGAYFRD 

      1330       1340       1350       1360       1370       1380 
LWNILDFIVV SGALVAFAFT GNSKGKDINT IKSLRVLRVL RPLKTIKRLP KLKAVFDCVV 

      1390       1400       1410       1420       1430       1440 
NSLKNVFNIL IVYMLFMFIF AVVAVQLFKG KFFHCTDESK EFEKDCRGKY LLYEKNEVKA 

      1450       1460       1470       1480       1490       1500 
RDREWKKYEF HYDNVLWALL TLFTVSTGEG WPQVLKHSVD ATFENQGPSP GYRMEMSIFY 

      1510       1520       1530       1540       1550       1560 
VVYFVVFPFF FVNIFVALII ITFQEQGDKM MEEYSLEKNE RACIDFAISA KPLTRHMPQN 

      1570       1580       1590       1600       1610       1620 
KQSFQYRMWQ FVVSPPFEYT IMAMIALNTI VLMMKFYGAS VAYDNALKVF NIVFTSLFSL 

      1630       1640       1650       1660       1670       1680 
ECLLKVLAFG ILNYFRDAWN IFDFVTVLGS ITDILVTEFG NNFINLSFLR LFRAARLIKL 

      1690       1700       1710       1720       1730       1740 
LRQGYTIRIL LWTFVQSFKA LPYVCLLIAM LFFIYAIIGM QVFGNIGIDM EDEDSDEDEF 

      1750       1760       1770       1780       1790       1800 
QITEHNNFRT FFQALMLLFR SATGEAWHNI MLSCLSGKPC DKNSGILTPE CGNEFAYFYF 

      1810       1820       1830       1840       1850       1860 
VSFIFLCSFL MLNLFVAVIM DNFEYLTRDS SILGPHHLDE YVRVWAEYDP AAWGRMLYRD 

      1870       1880       1890       1900       1910       1920 
MYAMLRHMPP PLGLGKNCPA RVAYKRLLRM DLPVADDNTV HFNSTLMALI RTALDIKIAK 

      1930       1940       1950       1960       1970       1980 
GGADKQQMDA ELRKEMMAIW PNLSQKTLDL LVTPHKSTDL TVGKIYAAMM IMEYYRQSKA 

      1990       2000       2010       2020       2030       2040 
KKLQAMREEQ NRTPLMFQRM EPPPDEGGAG QNALPSTQLD PAGGLMAHED GLKDSPSWVT 

      2050       2060       2070       2080       2090       2100 
QRAQEMFQKT GTWSPERAPP ADMADSQPKP QSVEMREMSQ DGYSDSEHCL PMEGQARAAS 

      2110       2120       2130       2140       2150       2160 
MPRLPAENQR RRGRPRGSDL STICDTSPMK RSASVLGPKA SRRLDDYSLE RVPPEENQRH 

      2170       2180       2190       2200       2210       2220 
HPRRRERAHR TSERSLGRYT DVDTGLGTDL SMTTQSGDLP SREREQERGR PKDRKHRPHH 

      2230       2240       2250       2260       2270       2280 
HHHHHHHPGR GPGRVSPGVS ARRRRRGPVA RVRPARAPAL AHARARARAP ARLLPELRLR 

      2290       2300       2310       2320       2330       2340 
RARRPRPRQR RRPRRRRGGG GRALRRAPGP REPLAQDSPG RGPSVCLARA ARPAGPQRLL 

      2350       2360       2370       2380       2390       2400 
PGPRTGQAPR ARLPQKPARS VQRERRGLVL SPPPPPPGEL APRAHPARTP RPGPGDSRSR 

      2410       2420 
RGGRRWTASA GKGGGGPRAS APSP

« Hide

Isoform BI-1 (1A-1) [UniParc].

Checksum: B14B3FA4E801D8D4
Show »

FASTA2,273257,351
Isoform CBP101 (CBP109) [UniParc].

Checksum: FADE1090207B5822
Show »

FASTA2,424273,179
Isoform CBP103 [UniParc].

Checksum: 7EB161F547B14151
Show »

FASTA2,075234,541
Isoform CBP107 [UniParc].

Checksum: 726B65549B57B475
Show »

FASTA2,144241,749

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X57477 mRNA. Translation: CAA40715.1.
X57689 mRNA. Translation: CAA40872.1.
X57476 mRNA. Translation: CAA40714.1.
X57688 mRNA. Translation: CAA40871.1.
PIRI46477.
I46480.
RefSeqNP_001095163.1. NM_001101693.1.
UniGeneOcu.2123.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3DVMX-ray2.60B1963-1982[»]
ProteinModelPortalP27884.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29591N.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009265.

Organism-specific databases

CTD773.

Phylogenomic databases

eggNOGCOG1226.
HOVERGENHBG050763.

Family and domain databases

InterProIPR005821. 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.
SMARTSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP27884.

Entry information

Entry nameCAC1A_RABIT
AccessionPrimary (citable) accession number: P27884
Secondary accession number(s): P27883
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: April 3, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents