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Voltage-dependent P/Q-type calcium channel subunit alpha-1A (Brain calcium channel I) (BI) (Calcium channel, L type, alpha-1 polypeptide, isoform 4) (Rat brain class A) (RBA-I) (Voltage-gated calcium channel subunit alpha Cav2.1)

 CAC1A_RAT               Reviewed;        2212 AA.
P54282; Q01541;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
27-SEP-2017, entry version 146.
RecName: Full=Voltage-dependent P/Q-type calcium channel subunit alpha-1A;
AltName: Full=Brain calcium channel I;
Short=BI;
AltName: Full=Calcium channel, L type, alpha-1 polypeptide, isoform 4;
AltName: Full=Rat brain class A;
Short=RBA-I;
AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.1;
Name=Cacna1a; Synonyms=Cach4, Cacn3, Cacnl1a4;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=1648226; DOI=10.1073/pnas.88.13.5621;
Starr T.V.B., Prystay W., Snutch T.P.;
"Primary structure of a calcium channel that is highly expressed in
the rat cerebellum.";
Proc. Natl. Acad. Sci. U.S.A. 88:5621-5625(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1354-1659 (ISOFORM 2).
TISSUE=Kidney;
PubMed=1279681; DOI=10.1073/pnas.89.21.10494;
Yu A.S.L., Hebert S.C., Brenner B.M., Lytton J.;
"Molecular characterization and nephron distribution of a family of
transcripts encoding the pore-forming subunit of Ca2+ channels in the
kidney.";
Proc. Natl. Acad. Sci. U.S.A. 89:10494-10498(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1435-1667 (ISOFORM 3).
PubMed=1692134; DOI=10.1073/pnas.87.9.3391;
Snutch T.P., Leonard J.P., Gilbert M.M., Lester H.A., Davidson N.;
"Rat brain expresses a heterogeneous family of calcium channels.";
Proc. Natl. Acad. Sci. U.S.A. 87:3391-3395(1990).
[4]
INTERACTION WITH CABP1.
PubMed=11865310; DOI=10.1038/nn805;
Lee A., Westenbroek R.E., Haeseleer F., Palczewski K., Scheuer T.,
Catterall W.A.;
"Differential modulation of Ca(v)2.1 channels by calmodulin and Ca2+-
binding protein 1.";
Nat. Neurosci. 5:210-217(2002).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453; SER-752; SER-755;
SER-1998; SER-2028; SER-2030; SER-2071 AND SER-2091, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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).
{ECO:0000250|UniProtKB:O00555}.
-!- SUBUNIT: 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.
-!- INTERACTION:
Q9JIR4:Rims1; NbExp=4; IntAct=EBI-3507416, EBI-3507436;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:O00555}; Multi-pass membrane protein
{ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=P54282-1; Sequence=Displayed;
Name=2; Synonyms=RKC8;
IsoId=P54282-2; Sequence=VSP_000881;
Name=3; Synonyms=RBA-65;
IsoId=P54282-3; Sequence=Not described;
Name=4;
IsoId=P54282-4; Sequence=Not described;
-!- 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.
-!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
1.A.1.11) family. CACNA1A subfamily. {ECO:0000305}.
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EMBL; M64373; AAA40806.1; -; mRNA.
EMBL; M99222; AAA40896.1; -; mRNA.
PIR; A41098; A41098.
RefSeq; NP_037050.2; NM_012918.3.
UniGene; Rn.87769; -.
ProteinModelPortal; P54282; -.
BioGrid; 247433; 4.
CORUM; P54282; -.
DIP; DIP-29638N; -.
IntAct; P54282; 2.
STRING; 10116.ENSRNOP00000059641; -.
GuidetoPHARMACOLOGY; 532; -.
TCDB; 1.A.1.11.8; the voltage-gated ion channel (vic) superfamily.
iPTMnet; P54282; -.
PhosphoSitePlus; P54282; -.
PaxDb; P54282; -.
PRIDE; P54282; -.
GeneID; 25398; -.
KEGG; rno:25398; -.
CTD; 773; -.
RGD; 2244; Cacna1a.
eggNOG; KOG2301; Eukaryota.
eggNOG; ENOG410XNP6; LUCA.
HOGENOM; HOG000231530; -.
HOVERGEN; HBG050763; -.
InParanoid; P54282; -.
KO; K04344; -.
PhylomeDB; P54282; -.
PRO; PR:P54282; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
GO; GO:0043204; C:perikaryon; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:RGD.
GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
GO; GO:0008331; F:high voltage-gated calcium channel activity; IDA:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:UniProtKB.
GO; GO:0070509; P:calcium ion import; IDA:RGD.
GO; GO:0006816; P:calcium ion transport; IDA:RGD.
GO; GO:0007268; P:chemical synaptic transmission; IMP:RGD.
GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; IMP:RGD.
GO; GO:0019233; P:sensory perception of pain; IMP:RGD.
InterPro; IPR005448; CACNA1A.
InterPro; IPR031649; GPHH_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR014873; VDCC_a1su_IQ.
InterPro; IPR002077; VDCCAlpha1.
PANTHER; PTHR10037:SF249; PTHR10037:SF249; 1.
Pfam; PF08763; Ca_chan_IQ; 1.
Pfam; PF16905; GPHH; 1.
Pfam; PF00520; Ion_trans; 4.
PRINTS; PR00167; CACHANNEL.
PRINTS; PR01632; PQVDCCALPHA1.
SMART; SM01062; Ca_chan_IQ; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Calcium channel; Calcium transport;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
Ion channel; Ion transport; Membrane; Metal-binding; Phosphoprotein;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport; Voltage-gated channel.
CHAIN 1 2212 Voltage-dependent P/Q-type calcium
channel subunit alpha-1A.
/FTId=PRO_0000053919.
TOPO_DOM 1 100 Cytoplasmic. {ECO:0000255}.
TRANSMEM 101 119 Helical; Name=S1 of repeat I.
{ECO:0000255}.
TOPO_DOM 120 138 Extracellular. {ECO:0000255}.
TRANSMEM 139 156 Helical; Name=S2 of repeat I.
{ECO:0000255}.
TOPO_DOM 157 168 Cytoplasmic. {ECO:0000255}.
TRANSMEM 169 184 Helical; Name=S3 of repeat I.
{ECO:0000255}.
TOPO_DOM 185 192 Extracellular. {ECO:0000255}.
TRANSMEM 193 211 Helical; Name=S4 of repeat I.
{ECO:0000255}.
TOPO_DOM 212 230 Cytoplasmic. {ECO:0000255}.
TRANSMEM 231 250 Helical; Name=S5 of repeat I.
{ECO:0000255}.
TOPO_DOM 251 337 Extracellular. {ECO:0000255}.
TRANSMEM 338 362 Helical; Name=S6 of repeat I.
{ECO:0000255}.
TOPO_DOM 363 489 Cytoplasmic. {ECO:0000255}.
TRANSMEM 490 509 Helical; Name=S1 of repeat II.
{ECO:0000255}.
TOPO_DOM 510 523 Extracellular. {ECO:0000255}.
TRANSMEM 524 543 Helical; Name=S2 of repeat II.
{ECO:0000255}.
TOPO_DOM 544 551 Cytoplasmic. {ECO:0000255}.
TRANSMEM 552 570 Helical; Name=S3 of repeat II.
{ECO:0000255}.
TOPO_DOM 571 580 Extracellular. {ECO:0000255}.
TRANSMEM 581 599 Helical; Name=S4 of repeat II.
{ECO:0000255}.
TOPO_DOM 600 618 Cytoplasmic. {ECO:0000255}.
TRANSMEM 619 638 Helical; Name=S5 of repeat II.
{ECO:0000255}.
TOPO_DOM 639 691 Extracellular. {ECO:0000255}.
TRANSMEM 692 716 Helical; Name=S6 of repeat II.
{ECO:0000255}.
TOPO_DOM 717 1190 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1191 1214 Helical; Name=S1 of repeat III.
{ECO:0000255}.
TOPO_DOM 1215 1231 Extracellular. {ECO:0000255}.
TRANSMEM 1232 1251 Helical; Name=S2 of repeat III.
{ECO:0000255}.
TOPO_DOM 1252 1258 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1259 1282 Helical; Name=S3 of repeat III.
{ECO:0000255}.
TOPO_DOM 1283 1293 Extracellular. {ECO:0000255}.
TRANSMEM 1294 1311 Helical; Name=S4 of repeat III.
{ECO:0000255}.
TOPO_DOM 1312 1330 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1331 1350 Helical; Name=S5 of repeat III.
{ECO:0000255}.
TOPO_DOM 1351 1437 Extracellular. {ECO:0000255}.
TRANSMEM 1438 1462 Helical; Name=S6 of repeat III.
{ECO:0000255}.
TOPO_DOM 1463 1518 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1519 1537 Helical; Name=S1 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1538 1551 Extracellular. {ECO:0000255}.
TRANSMEM 1552 1573 Helical; Name=S2 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1574 1580 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1581 1600 Helical; Name=S3 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1601 1607 Extracellular. {ECO:0000255}.
TRANSMEM 1608 1626 Helical; Name=S4 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1627 1645 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1646 1665 Helical; Name=S5 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1666 1737 Extracellular. {ECO:0000255}.
TRANSMEM 1738 1763 Helical; Name=S6 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1764 2212 Cytoplasmic. {ECO:0000255}.
REPEAT 87 365 I.
REPEAT 475 719 II.
REPEAT 1182 1465 III.
REPEAT 1502 1765 IV.
CA_BIND 1791 1802 {ECO:0000250}.
REGION 385 402 Binding to the beta subunit.
{ECO:0000250}.
COMPBIAS 13 20 Poly-Gly.
COMPBIAS 729 734 Poly-Glu.
COMPBIAS 1155 1158 Poly-Glu.
COMPBIAS 2162 2171 Poly-His.
SITE 320 320 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 670 670 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1411 1411 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1600 1600 Binds to omega-Aga-IVA. {ECO:0000250}.
SITE 1707 1707 Calcium ion selectivity and permeability.
{ECO:0000250}.
MOD_RES 411 411 Phosphothreonine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 450 450 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 453 453 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 752 752 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 755 755 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 792 792 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 1038 1038 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 1042 1042 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 1051 1051 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 1773 1773 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 1935 1935 Phosphothreonine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 1998 1998 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 2016 2016 Phosphoserine.
{ECO:0000250|UniProtKB:P97445}.
MOD_RES 2028 2028 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 2030 2030 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 2071 2071 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 2091 2091 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 285 285 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1607 1607 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1602 1602 G -> GNP (in isoform 2).
{ECO:0000303|PubMed:1279681}.
/FTId=VSP_000881.
SEQUENCE 2212 AA; 251527 MW; DFBD7A0F553AFA52 CRC64;
MARFGDEMPG RYGAGGGGSG PAAGVVVGAA GGRGAGGSRQ GGQPGAQRMY KQSMAQRART
MALYNPIPVR QNCLTVNRSL FLFSEDNVVR KYAKKITEWP PFEYMILATI IANCIVLALE
QHLPDDDKTP MSERLDDTEP YFIGIFCFEA GIKIVALGFA FHKGSYLRNG WNVMDFVVVL
TGILATVGTE FDLRTLRAVR VLRPLKLVSG IPSLQVVLKS IMKAMIPLLQ IGLLLFFAIL
IFAIIGLEFY MGKFHTTCFE EGTDDIQGES PAPCGTEEPA RTCPNGTKCQ PYWEGPNNGI
TQFDNILFAV LTVFQCITME GWTDLLYNSN DASGNTWNWL YFIPLIIIGS FFMLNLVLGV
LSGEFAKERE RVENRRAFLK LRRQQQIERE LNGYMEWISK AEEVILAEDE TDVEQRHPFD
GALRRATLKK SKTDLLNPEE AEDQLADIAS VGSPFARASI KSAKLENSTF FHKKERRMRF
YIRRMVKTQA FYWTVLSLVA LNTLWLAIVH YNQPEWLSDF LYYAEFIFLG LFMSEMFIKM
YGLGTRPYFH SSFNCFDCGV IIGSIFEVIW AVIKPGTSFG ISVLRALRLL RIFKVTKYWA
SLRNLVVSLL NSMKSIISLL FLLFLFIVVF ALLGMQLFGG QFNFDEGTPP TNFDTFPAAI
MTVFQILTGE DWNEVMYDEI KSQGGVQGGM VFSIYFIVLT LFGNYTLLNV FLAIAVDNLA
NAQELTKDEQ EEEEAANQKL ALQKAKEVAE VSPLSAANMS IAVKEQQKNQ KPAKSVWEQR
TSEMRKQNLL ASREALYGDA AERWPTTYAR PLRPDVKTHL DRPLVVDPQE NRNNNTNKSR
APEALRQTAR PRESARDPDA RRAWPSSPER APGREGPYGR ESEPQQREHA PPREHVPWDA
DPERAKAGDA PRRHTHRPVA EGEPRRHRAR RRPGDEPDDR PERRPRPRDA TRPARAADGE
GDDGERKRRH RHGPPAHDDR ERRHRRRKES QGSGVPMSGP NLSTTRPIQQ DLGRQDLPLA
EDLDNMKNNK LATGEPASPH DSLGHSGLPP SPAKIGNSTN PGPALATNPQ NAASRRTPNN
PGNPSNPGPP KTPENSLIVT NPSSTQPNSA KTARKPEHMA VEIPPACPPL NHTVVQVNKN
ANPDPLPKKE EEKKEEEEAD PGEDGPKPMP PYSSMFILST TNPLRRLCHY ILNLRYFEMC
ILMVIAMSSI ALAAEDPVQP NAPRNNVLRY FDYVFTGVFT FEMVIKMIDL GLVLHQGAYF
RDLWNILDFI VVSGALVAFA FTGNSKGKDI NTIKSLRVLR VLRPLKTIKR LPKLKAVFDC
VVNSLKNVFN ILIVYMLFMF IFAVVAVQLF KGKFFHCTDE SKEFERDCRG KYLLYEKNEV
KARDREWKKY DFHYDNVLWA LLTLFTVSTG EGWPQVLKHS VDATFENQGP SPGYRMEMSI
FYVVYFVVFP FFFVNIFVAL IIITFQEQGD KMMEEYSLEK NERACIDFAI SAKPLTRHMP
QNKQSFQYRM WQFVVSPPFE YTIMAMIALN TIVLMMKFYG ASVAYENALR VFNIVFTSLF
SLECVLKVMA FGILNYFRDA WNIFDFVTVL GSITDILVTE FGNNFINLSF LRLFRAARLI
KLLRQGYTIR ILLWTFVQSF KALPYVCLLI AMLFFIYAII GMQVFGNIGI DGEDEDSDED
EFQITEHNNF RTFFQALMLL FRSATGEAWH NIMLSCLSGK PCDKNSGIQK PECGNEFAYF
YFVSFIFLCS FLMLNLFVAV IMDNFEYLTR DSSILGPHHL DEYVRVWAEY DPAACGRIHY
KDMYSLLRVI SPPLGLGKKC PHRVACKRLL RMDLPVADDN TVHFNSTLMA LIRTALDIKI
AKGGADKQQM DAELRKEMMA IWPNLSQKTL DLLVTPHKST DLTVGKIYAA MMIMEYYRQS
KAKKLQAMRE EQNRTPLMFQ RMEPPSPTQE GGPSQNALPS TQLDPGGGLM AQESSMKESP
SWVTQRAQEM FQKTGTWSPE RGPPIDMPNS QPNSQSVEMR EMGTDGYSDS EHYLPMEGQT
RAASMPRLPA ENQRRRGRPR GNNLSTISDT SPMKRSASVL GPKARRLDDY SLERVPPEEN
QRYHQRRRDR GHRTSERSLG RYTDVDTGLG TDLSMTTQSG DLPSKDRDQD RGRPKDRKHR
PHHHHHHHHH HPPAPDRERY AQERPDTGRA RAREQRWSRS PSEGREHATH RQ


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U1344r CLIA BI,Brain calcium channel I,Cach4,Cacn3,Cacna1a,Cacnl1a4,Calcium channel, L type, alpha-1 polypeptide, isoform 4,Rat,Rat brain class A,Rattus norvegicus,RBA-I,Voltage-dependent P_Q-type calcium ch 96T
E1344r ELISA BI,Brain calcium channel I,Cach4,Cacn3,Cacna1a,Cacnl1a4,Calcium channel, L type, alpha-1 polypeptide, isoform 4,Rat,Rat brain class A,Rattus norvegicus,RBA-I,Voltage-dependent P_Q-type calcium c 96T
EIAAB05037 CACH1,CACNA1S,CACNL1A3,Calcium channel, L type, alpha-1 polypeptide, isoform 3, skeletal muscle,Oryctolagus cuniculus,Rabbit,Voltage-dependent L-type calcium channel subunit alpha-1S,Voltage-gated cal
E1344Rb ELISA kit BI,Brain calcium channel I,CACH4,CACN3,CACNA1A,CACNL1A4,Calcium channel, L type, alpha-1 polypeptide isoform 4,Oryctolagus cuniculus,Rabbit,Voltage-dependent P_Q-type calcium channel subuni 96T
E1344m ELISA kit BI,Brain calcium channel I,Caca1a,Cach4,Cacn3,Cacna1a,Cacnl1a4,Calcium channel, L type, alpha-1 polypeptide isoform 4,Ccha1a,Mouse,Mus musculus,Voltage-dependent P_Q-type calcium channel su 96T


 

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