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P54282 (CAC1A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
Rat brain class A
Short name=RBA-I
Voltage-gated calcium channel subunit alpha Cav2.1
Gene names
Name:Cacna1a
Synonyms:Cach4, Cacn3, Cacnl1a4
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length2212 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-1Agives 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. Interact (via C-terminal CDB motif) with CABP1 in the pre- and postsynaptic membranes.

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. Also found in heart, in kidney distal convoluted tubule (DCT), and in pituitary.

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.

Sequence similarities

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

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   Molecular functionCalcium channel
Ion channel
Voltage-gated channel
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion import

Inferred from direct assay PubMed 21611731. Source: RGD

calcium ion transport

Inferred from direct assay PubMed 9593738. Source: RGD

positive regulation of cytosolic calcium ion concentration

Inferred from sequence or structural similarity. Source: UniProtKB

sensory perception of pain

Inferred from mutant phenotype PubMed 18433788. Source: RGD

synaptic transmission

Inferred from mutant phenotype PubMed 14673106. Source: RGD

   Cellular_componentperikaryon

Inferred from direct assay PubMed 16736476. Source: RGD

plasma membrane

Inferred from direct assay PubMed 17068255PubMed 9593738. Source: RGD

protein complex

Inferred from direct assay PubMed 17068255. Source: RGD

voltage-gated calcium channel complex

Inferred from direct assay PubMed 16049183PubMed 21611731. Source: RGD

   Molecular_functioncalmodulin binding

Inferred from direct assay PubMed 15980432. Source: UniProtKB

high voltage-gated calcium channel activity

Inferred from direct assay PubMed 17068255PubMed 21611731. Source: RGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

voltage-gated calcium channel activity

Inferred from direct assay PubMed 15980432. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Rims1Q9JIR44EBI-3507416,EBI-3507436

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P54282-1)

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 2 (identifier: P54282-2)

Also known as: RKC8;

The sequence of this isoform differs from the canonical sequence as follows:
     1602-1602: G → GNP
Isoform 3 (identifier: P54282-3)

Also known as: RBA-65;

The sequence of this isoform is not available.
Isoform 4 (identifier: P54282-4)

The sequence of this isoform is not available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 22122212Voltage-dependent P/Q-type calcium channel subunit alpha-1A
PRO_0000053919

Regions

Topological domain1 – 100100Cytoplasmic Potential
Transmembrane101 – 11919Helical; Name=S1 of repeat I; Potential
Topological domain120 – 13819Extracellular Potential
Transmembrane139 – 15618Helical; Name=S2 of repeat I; Potential
Topological domain157 – 16812Cytoplasmic Potential
Transmembrane169 – 18416Helical; Name=S3 of repeat I; Potential
Topological domain185 – 1928Extracellular Potential
Transmembrane193 – 21119Helical; Name=S4 of repeat I; Potential
Topological domain212 – 23019Cytoplasmic Potential
Transmembrane231 – 25020Helical; Name=S5 of repeat I; Potential
Topological domain251 – 33787Extracellular Potential
Transmembrane338 – 36225Helical; Name=S6 of repeat I; Potential
Topological domain363 – 489127Cytoplasmic Potential
Transmembrane490 – 50920Helical; Name=S1 of repeat II; Potential
Topological domain510 – 52314Extracellular Potential
Transmembrane524 – 54320Helical; Name=S2 of repeat II; Potential
Topological domain544 – 5518Cytoplasmic Potential
Transmembrane552 – 57019Helical; Name=S3 of repeat II; Potential
Topological domain571 – 58010Extracellular Potential
Transmembrane581 – 59919Helical; Name=S4 of repeat II; Potential
Topological domain600 – 61819Cytoplasmic Potential
Transmembrane619 – 63820Helical; Name=S5 of repeat II; Potential
Topological domain639 – 69153Extracellular Potential
Transmembrane692 – 71625Helical; Name=S6 of repeat II; Potential
Topological domain717 – 1190474Cytoplasmic Potential
Transmembrane1191 – 121424Helical; Name=S1 of repeat III; Potential
Topological domain1215 – 123117Extracellular Potential
Transmembrane1232 – 125120Helical; Name=S2 of repeat III; Potential
Topological domain1252 – 12587Cytoplasmic Potential
Transmembrane1259 – 128224Helical; Name=S3 of repeat III; Potential
Topological domain1283 – 129311Extracellular Potential
Transmembrane1294 – 131118Helical; Name=S4 of repeat III; Potential
Topological domain1312 – 133019Cytoplasmic Potential
Transmembrane1331 – 135020Helical; Name=S5 of repeat III; Potential
Topological domain1351 – 143787Extracellular Potential
Transmembrane1438 – 146225Helical; Name=S6 of repeat III; Potential
Topological domain1463 – 151856Cytoplasmic Potential
Transmembrane1519 – 153719Helical; Name=S1 of repeat IV; Potential
Topological domain1538 – 155114Extracellular Potential
Transmembrane1552 – 157322Helical; Name=S2 of repeat IV; Potential
Topological domain1574 – 15807Cytoplasmic Potential
Transmembrane1581 – 160020Helical; Name=S3 of repeat IV; Potential
Topological domain1601 – 16077Extracellular Potential
Transmembrane1608 – 162619Helical; Name=S4 of repeat IV; Potential
Topological domain1627 – 164519Cytoplasmic Potential
Transmembrane1646 – 166520Helical; Name=S5 of repeat IV; Potential
Topological domain1666 – 173772Extracellular Potential
Transmembrane1738 – 176326Helical; Name=S6 of repeat IV; Potential
Topological domain1764 – 2212449Cytoplasmic Potential
Repeat87 – 365279I
Repeat475 – 719245II
Repeat1182 – 1465284III
Repeat1502 – 1765264IV
Calcium binding1791 – 180212 By similarity
Region385 – 40218Binding to the beta subunit By similarity
Compositional bias13 – 208Poly-Gly
Compositional bias729 – 7346Poly-Glu
Compositional bias1155 – 11584Poly-Glu
Compositional bias2162 – 217110Poly-His

Sites

Site3201Calcium ion selectivity and permeability By similarity
Site6701Calcium ion selectivity and permeability By similarity
Site14111Calcium ion selectivity and permeability By similarity
Site16001Binds to omega-Aga-IVA By similarity
Site17071Calcium ion selectivity and permeability By similarity

Amino acid modifications

Modified residue7921Phosphoserine By similarity
Modified residue17731Phosphoserine; by PKA Potential
Glycosylation2851N-linked (GlcNAc...) Potential
Glycosylation16071N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence16021G → GNP in isoform 2.
VSP_000881

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: DFBD7A0F553AFA52

FASTA2,212251,527
        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 LNTLWLAIVH 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 DWNEVMYDEI KSQGGVQGGM VFSIYFIVLT LFGNYTLLNV FLAIAVDNLA 

       730        740        750        760        770        780 
NAQELTKDEQ EEEEAANQKL ALQKAKEVAE VSPLSAANMS IAVKEQQKNQ KPAKSVWEQR 

       790        800        810        820        830        840 
TSEMRKQNLL ASREALYGDA AERWPTTYAR PLRPDVKTHL DRPLVVDPQE NRNNNTNKSR 

       850        860        870        880        890        900 
APEALRQTAR PRESARDPDA RRAWPSSPER APGREGPYGR ESEPQQREHA PPREHVPWDA 

       910        920        930        940        950        960 
DPERAKAGDA PRRHTHRPVA EGEPRRHRAR RRPGDEPDDR PERRPRPRDA TRPARAADGE 

       970        980        990       1000       1010       1020 
GDDGERKRRH RHGPPAHDDR ERRHRRRKES QGSGVPMSGP 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 DFHYDNVLWA 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 PCDKNSGIQK PECGNEFAYF 

      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 AQESSMKESP 

      1990       2000       2010       2020       2030       2040 
SWVTQRAQEM FQKTGTWSPE RGPPIDMPNS QPNSQSVEMR EMGTDGYSDS EHYLPMEGQT 

      2050       2060       2070       2080       2090       2100 
RAASMPRLPA ENQRRRGRPR GNNLSTISDT SPMKRSASVL GPKARRLDDY SLERVPPEEN 

      2110       2120       2130       2140       2150       2160 
QRYHQRRRDR GHRTSERSLG RYTDVDTGLG TDLSMTTQSG DLPSKDRDQD RGRPKDRKHR 

      2170       2180       2190       2200       2210 
PHHHHHHHHH HPPAPDRERY AQERPDTGRA RAREQRWSRS PSEGREHATH RQ 

« Hide

Isoform 2 (RKC8) [UniParc].

Checksum: D2ED9869D22AF77F
Show »

FASTA2,214251,739
Isoform 3 (RBA-65) (Sequence not available).
Isoform 4 (Sequence not available).

References

[1]"Primary structure of a calcium channel that is highly expressed in the rat cerebellum."
Starr T.V.B., Prystay W., Snutch T.P.
Proc. Natl. Acad. Sci. U.S.A. 88:5621-5625(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Brain.
[2]"Molecular characterization and nephron distribution of a family of transcripts encoding the pore-forming subunit of Ca2+ channels in the kidney."
Yu A.S.L., Hebert S.C., Brenner B.M., Lytton J.
Proc. Natl. Acad. Sci. U.S.A. 89:10494-10498(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1354-1659 (ISOFORM 2).
Tissue: Kidney.
[3]"Rat brain expresses a heterogeneous family of calcium channels."
Snutch T.P., Leonard J.P., Gilbert M.M., Lester H.A., Davidson N.
Proc. Natl. Acad. Sci. U.S.A. 87:3391-3395(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1435-1667 (ISOFORM 3).
[4]"Differential modulation of Ca(v)2.1 channels by calmodulin and Ca2+-binding protein 1."
Lee A., Westenbroek R.E., Haeseleer F., Palczewski K., Scheuer T., Catterall W.A.
Nat. Neurosci. 5:210-217(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CABP1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64373 mRNA. Translation: AAA40806.1.
M99222 mRNA. Translation: AAA40896.1.
PIRA41098.
RefSeqNP_037050.2. NM_012918.3.
UniGeneRn.87769.

3D structure databases

ProteinModelPortalP54282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29638N.
IntActP54282. 2 interactions.

Chemistry

BindingDBP54282.
GuidetoPHARMACOLOGY532.

Protein family/group databases

TCDB1.A.1.11.8. the voltage-gated ion channel (vic) superfamily.

PTM databases

PhosphoSiteP54282.

Proteomic databases

PaxDbP54282.
PRIDEP54282.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25398.
KEGGrno:25398.

Organism-specific databases

CTD773.
RGD2244. Cacna1a.

Phylogenomic databases

eggNOGCOG1226.
HOGENOMHOG000231530.
HOVERGENHBG050763.
KOK04344.
PhylomeDBP54282.

Gene expression databases

GenevestigatorP54282.

Family and domain databases

Gene3D1.20.120.350. 4 hits.
InterProIPR027359. Channel_four-helix_dom.
IPR005821. 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

NextBio13949997.
PROP54282.

Entry information

Entry nameCAC1A_RAT
AccessionPrimary (citable) accession number: P54282
Secondary accession number(s): Q01541
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families