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Voltage-dependent N-type calcium channel subunit alpha-1B (Brain calcium channel III) (BIII) (Calcium channel, L type, alpha-1 polypeptide isoform 5) (Voltage-gated calcium channel subunit alpha Cav2.2)

 CAC1B_RAT               Reviewed;        2336 AA.
Q02294;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 149.
RecName: Full=Voltage-dependent N-type calcium channel subunit alpha-1B;
AltName: Full=Brain calcium channel III;
Short=BIII;
AltName: Full=Calcium channel, L type, alpha-1 polypeptide isoform 5;
AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.2;
Name=Cacna1b; Synonyms=Cach5, Cacnl1a5;
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=1317580; DOI=10.1073/pnas.89.11.5058;
Dubel S.J., Starr T.V.B., Hell J.W., Ahlijanian M.K., Enyeart J.J.,
Catterall W.A., Snutch T.P.;
"Molecular cloning of the alpha-1 subunit of an omega-conotoxin-
sensitive calcium channel.";
Proc. Natl. Acad. Sci. U.S.A. 89:5058-5062(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1516-1679 (CLONE RBB-10).
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).
[3]
PHOSPHORYLATION.
PubMed=8125957;
Hell J.W., Appleyard S.M., Yokoyama C.T., Warner C., Catterall W.A.;
"Differential phosphorylation of two size forms of the N-type calcium
channel alpha 1 subunit which have different COOH termini.";
J. Biol. Chem. 269:7390-7396(1994).
[4]
BETA-SUBUNIT BINDING DOMAIN.
PubMed=7509046; DOI=10.1038/368067a0;
Pragnell M., de Waard M., Mori Y., Tanabe T., Snutch T.P.,
Campbell K.P.;
"Calcium channel beta-subunit binds to a conserved motif in the I-II
cytoplasmic linker of the alpha 1-subunit.";
Nature 368:67-70(1994).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411; SER-746 AND
SER-2253, 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-1B
gives rise to N-type calcium currents. N-type calcium channels
belong to the 'high-voltage activated' (HVA) group and are blocked
by omega-conotoxin-GVIA (omega-CTx-GVIA) and by omega-agatoxin-
IIIA (omega-Aga-IIIA). They are however insensitive to
dihydropyridines (DHP), and omega-agatoxin-IVA (omega-Aga-IVA).
Calcium channels containing alpha-1B subunit may play a role in
directed migration of immature neurons.
-!- SUBUNIT: Multisubunit complex 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 RIMS1. Interacts with FMR1 (via
C-terminus); this interaction induces a deacrease in the number of
presynaptic functional CACNA1B channels at the cell surface.
{ECO:0000250|UniProtKB:O55017}.
-!- INTERACTION:
P21707:Syt1; NbExp=2; IntAct=EBI-540038, EBI-458098;
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=2 isoforms may be produced.;
Name=1;
IsoId=Q02294-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Central nervous system.
-!- 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.
-!- PTM: Phosphorylated in vitro by CaM-kinase II, PKA, PKC and CGPK.
{ECO:0000269|PubMed:8125957}.
-!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
1.A.1.11) family. CACNA1B subfamily. {ECO:0000305}.
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EMBL; M92905; AAA42014.1; -; mRNA.
PIR; B35901; B35901.
UniGene; Rn.85880; -.
PDB; 4DEX; X-ray; 2.00 A; B=358-468.
PDBsum; 4DEX; -.
ProteinModelPortal; Q02294; -.
SMR; Q02294; -.
CORUM; Q02294; -.
IntAct; Q02294; 4.
MINT; MINT-102470; -.
STRING; 10116.ENSRNOP00000006162; -.
BindingDB; Q02294; -.
ChEMBL; CHEMBL5107; -.
GuidetoPHARMACOLOGY; 533; -.
iPTMnet; Q02294; -.
PhosphoSitePlus; Q02294; -.
PaxDb; Q02294; -.
PRIDE; Q02294; -.
UCSC; RGD:628852; rat. [Q02294-1]
RGD; 628852; Cacna1b.
eggNOG; KOG2301; Eukaryota.
eggNOG; ENOG410XNP6; LUCA.
HOGENOM; HOG000231530; -.
HOVERGEN; HBG050763; -.
InParanoid; Q02294; -.
PhylomeDB; Q02294; -.
PRO; PR:Q02294; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0043679; C:axon terminus; IDA:RGD.
GO; GO:0043198; C:dendritic shaft; IDA:RGD.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; 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; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0008331; F:high voltage-gated calcium channel activity; IDA:RGD.
GO; GO:0051721; F:protein phosphatase 2A binding; IPI:RGD.
GO; GO:0005245; F:voltage-gated calcium channel activity; IMP:RGD.
GO; GO:0070509; P:calcium ion import; IMP:RGD.
GO; GO:0006816; P:calcium ion transport; IMP:RGD.
GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
GO; GO:0001956; P:positive regulation of neurotransmitter secretion; IMP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IDA:RGD.
GO; GO:0033574; P:response to testosterone; IMP:RGD.
GO; GO:0019233; P:sensory perception of pain; IMP:RGD.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR031649; GPHH_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR014873; VDCC_a1su_IQ.
InterPro; IPR005447; VDCC_N_a1su.
InterPro; IPR002077; VDCCAlpha1.
PANTHER; PTHR10037:SF161; PTHR10037:SF161; 1.
Pfam; PF08763; Ca_chan_IQ; 1.
Pfam; PF16905; GPHH; 1.
Pfam; PF00520; Ion_trans; 4.
PRINTS; PR00167; CACHANNEL.
PRINTS; PR01631; NVDCCALPHA1.
SMART; SM01062; Ca_chan_IQ; 1.
PROSITE; PS50222; EF_HAND_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Calcium;
Calcium channel; Calcium transport; Complete proteome; Disulfide bond;
Glycoprotein; Ion channel; Ion transport; Membrane; Metal-binding;
Methylation; Nucleotide-binding; Phosphoprotein; Reference proteome;
Repeat; Transmembrane; Transmembrane helix; Transport;
Voltage-gated channel.
CHAIN 1 2336 Voltage-dependent N-type calcium channel
subunit alpha-1B.
/FTId=PRO_0000053924.
TOPO_DOM 1 95 Cytoplasmic. {ECO:0000255}.
TRANSMEM 96 114 Helical; Name=S1 of repeat I.
{ECO:0000255}.
TOPO_DOM 115 133 Extracellular. {ECO:0000255}.
TRANSMEM 134 151 Helical; Name=S2 of repeat I.
{ECO:0000255}.
TOPO_DOM 152 164 Cytoplasmic. {ECO:0000255}.
TRANSMEM 165 179 Helical; Name=S3 of repeat I.
{ECO:0000255}.
TOPO_DOM 180 186 Extracellular. {ECO:0000255}.
TRANSMEM 187 205 Helical; Name=S4 of repeat I.
{ECO:0000255}.
TOPO_DOM 206 225 Cytoplasmic. {ECO:0000255}.
TRANSMEM 226 245 Helical; Name=S5 of repeat I.
{ECO:0000255}.
TOPO_DOM 246 331 Extracellular. {ECO:0000255}.
TRANSMEM 332 356 Helical; Name=S6 of repeat I.
{ECO:0000255}.
TOPO_DOM 357 483 Cytoplasmic. {ECO:0000255}.
TRANSMEM 484 503 Helical; Name=S1 of repeat II.
{ECO:0000255}.
TOPO_DOM 504 517 Extracellular. {ECO:0000255}.
TRANSMEM 518 537 Helical; Name=S2 of repeat II.
{ECO:0000255}.
TOPO_DOM 538 545 Cytoplasmic. {ECO:0000255}.
TRANSMEM 546 564 Helical; Name=S3 of repeat II.
{ECO:0000255}.
TOPO_DOM 565 575 Extracellular. {ECO:0000255}.
TRANSMEM 576 593 Helical; Name=S4 of repeat II.
{ECO:0000255}.
TOPO_DOM 594 612 Cytoplasmic. {ECO:0000255}.
TRANSMEM 613 632 Helical; Name=S5 of repeat II.
{ECO:0000255}.
TOPO_DOM 633 685 Extracellular. {ECO:0000255}.
TRANSMEM 686 710 Helical; Name=S6 of repeat II.
{ECO:0000255}.
TOPO_DOM 711 1143 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1144 1167 Helical; Name=S1 of repeat III.
{ECO:0000255}.
TOPO_DOM 1168 1184 Extracellular. {ECO:0000255}.
TRANSMEM 1185 1204 Helical; Name=S2 of repeat III.
{ECO:0000255}.
TOPO_DOM 1205 1212 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1213 1235 Helical; Name=S3 of repeat III.
{ECO:0000255}.
TOPO_DOM 1236 1250 Extracellular. {ECO:0000255}.
TRANSMEM 1251 1265 Helical; Name=S4 of repeat III.
{ECO:0000255}.
TOPO_DOM 1266 1286 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1287 1306 Helical; Name=S5 of repeat III.
{ECO:0000255}.
TOPO_DOM 1307 1392 Extracellular. {ECO:0000255}.
TRANSMEM 1393 1417 Helical; Name=S6 of repeat III.
{ECO:0000255}.
TOPO_DOM 1418 1474 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1475 1493 Helical; Name=S1 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1494 1507 Extracellular. {ECO:0000255}.
TRANSMEM 1508 1527 Helical; Name=S2 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1528 1536 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1537 1555 Helical; Name=S3 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1556 1563 Extracellular. {ECO:0000255}.
TRANSMEM 1564 1582 Helical; Name=S4 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1583 1601 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1602 1621 Helical; Name=S5 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1622 1683 Extracellular. {ECO:0000255}.
TRANSMEM 1684 1703 Helical; Name=S6 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1704 2336 Cytoplasmic. {ECO:0000255}.
REPEAT 82 359 I.
REPEAT 469 713 II.
REPEAT 1135 1421 III.
REPEAT 1458 1711 IV.
DOMAIN 1724 1759 EF-hand. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
NP_BIND 452 459 ATP. {ECO:0000255}.
CA_BIND 1737 1748 {ECO:0000255|PROSITE-ProRule:PRU00448}.
REGION 379 396 Binding to the beta subunit.
COMPBIAS 2049 2053 Poly-His.
COMPBIAS 2115 2119 Poly-Ser.
SITE 314 314 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 664 664 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1367 1367 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1655 1655 Calcium ion selectivity and permeability.
{ECO:0000250}.
MOD_RES 22 22 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:O55017}.
MOD_RES 411 411 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 746 746 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 749 749 Phosphoserine.
{ECO:0000250|UniProtKB:O55017}.
MOD_RES 784 784 Phosphoserine.
{ECO:0000250|UniProtKB:O55017}.
MOD_RES 1067 1067 Phosphoserine.
{ECO:0000250|UniProtKB:O55017}.
MOD_RES 1719 1719 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 2065 2065 Phosphoserine.
{ECO:0000250|UniProtKB:O55017}.
MOD_RES 2221 2221 Phosphoserine.
{ECO:0000250|UniProtKB:O55017}.
MOD_RES 2230 2230 Phosphoserine.
{ECO:0000250|UniProtKB:O55017}.
MOD_RES 2253 2253 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 256 256 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1563 1563 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1675 1675 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 1538 1538 N -> D (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
CONFLICT 1579 1579 C -> L (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
HELIX 364 403 {ECO:0000244|PDB:4DEX}.
SEQUENCE 2336 AA; 262256 MW; 8D50AF67834FD1BC CRC64;
MVRFGDELGG RYGGTGGGER ARGGGAGGAG GPGQGGLPPG QRVLYKQSIA QRARTMALYN
PIPVKQNCFT VNRSLFVFSE DNVVRKYAKR ITEWPPFEYM ILATIIANCI VLALEQHLPD
GDKTPMSERL DDTEPYFIGI FCFEAGIKII ALGFVFHKGS YLRNGWNVMD FVVVLTEILA
TAGTDFDLRT LRAVRVLRPL KLVSGIPSLQ VVLKSIMKAM VPLLQIGLLL FFAILMFAII
GLEFYMGKFH KACFPNSTDA EPVGDFPCGK EAPARLCDSD TECREYWPGP NFGITNFDNI
LFAILTVFQC ITMEGWTDIL YNTNDAAGNT WNWLYFIPLI IIGSFFMLNL VLGVLSGEFA
KERERVENRR AFLKLRRQQQ IERELNGYLE WIFKAEEVML AEEDKNAEEK SPLDAVLKRA
ATKKSRNDLI HAEEGEDRFV DLCAAGSPFA RASLKSGKTE SSSYFRRKEK MFRFLIRRMV
KAQSFYWVVL CVVALNTLCV AMVHYNQPQR LTTALYFAEF VFLGLFLTEM SLKMYGLGPR
SYFRSSFNCF DFGVIVGSIF EVVWAAIKPG TSFGISVLRA LRLLRIFKVT KYWNSLRNLV
VSLLNSMKSI ISLLFLLFLF IVVFALLGMQ LFGGQFNFQD ETPTTNFDTF PAAILTVFQI
LTGEDWNAVM YHGIESQGGV SKGMFSSFYF IVLTLFGNYT LLNVFLAIAV DNLANAQELT
KDEEEMEEAA NQKLALQKAK EVAEVSPMSA ANISIAARQQ NSAKARSVWE QRASQLRLQN
LRASCEALYS EMDPEERLRY ASTRHVRPDM KTHMDRPLVV EPGRDGLRGP AGNKSKPEGT
EATEGADPPR RHHRHRDRDK TSASTPAGGE QDRTDCPKAE STETGAREER ARPRRSHSKE
APGADTQVRC ERSRRHHRRG SPEEATEREP RRHRAHRHAQ DSSKEGKEGT APVLVPKGER
RARHRGPRTG PRETENSEEP TRRHRAKHKV PPTLEPPERE VAEKESNVVE GDKETRNHQP
KEPRCDLEAI AVTGVGSLHM LPSTCLQKVD EQPEDADNQR NVTRMGSQPS DPSTTVHVPV
TLTGPPGEAT VVPSANTDLE GQAEGKKEAE ADDVLRRGPR PIVPYSSMFC LSPTNLLRRF
CHYIVTMRYF EMVILVVIAL SSIALAAEDP VRTDSFRNNA LKYMDYIFTG VFTFEMVIKM
IDLGLLLHPG AYFRDLWNIL DFIVVSGALV AFAFSSFMGG SKGKDINTIK SLRVLRVLRP
LKTIKRLPKL KAVFDCVVNS LKNVLNILIV YMLFMFIFAV IAVQLFKGKF FYCTDESKEL
ERDCRGQYLD YEKEEVEAQP RQWKKYDFHY DNVLWALLTL FTVSTGEGWP MVLKHSVDAT
YEEQGPSPGF RMELSIFYVV YFVVFPFFFV NIFVALIIIT FQEQGDKVMS ECSLEKNERA
CIDFAISAKP LTRYMPQNKQ SFQYKTWTFV VSPPFEYFIM AMIALNTVVL MMKFYDAPYE
YELMLKCLNI VFTSMFSLEC ILKIIAFGVL NYFRDAWNVF DFVTVLGSIT DILVTEIANN
FINLSFLRLF RAARLIKLCR QGYTIRILLW TFVQSFKALP YVCLLIAMLF FIYAIIGMQV
FGNIALDDGT SINRHNNFRT FLQALMLLFR SATGEAWHEI MLSCLGNRAC DPHANASECG
SDFAYFYFVS FIFLCSFLML NLFVAVIMDN FEYLTRDSSI LGPHHLDEFI RVWAEYDPAA
CGRISYNDMF EMLKHMSPPL GLGKKCPARV AYKRLVRMNM PISNEDMTVH FTSTLMALIR
TALEIKLAPA GTKQHQCDAE LRKEISSVWA NLPQKTLDLL VPPHKPDEMT VGKVYAALMI
FDFYKQNKTT RDQTHQAPGG LSQMGPVSLF HPLKATLEQT QPAVLRGARV FLRQKSATSL
SNGGAIQTQE SGIKESLSWG TQRTQDVLYE ARAPLERGHS AEIPVGQPGA LAVDVQMQNM
TLRGPDGEPQ PGLESQGRAA SMPRLAAETQ PAPNASPMKR SISTLAPRPH GTQLCNTVLD
RPPPSQVSHH HHHRCHRRRD KKQRSLEKGP SLSVDTEGAP STAAGSGLPH GEGSTGCRRE
RKQERGRSQE RRQPSSSSSE KQRFYSCDRF GSREPPQPKP SLSSHPISPT AALEPGPHPQ
GSGSVNGSPL MSTSGASTPG RGGRRQLPQT PLTPRPSITY KTANSSPVHF AEGQSGLPAF
SPGRLSRGLS EHNALLQKEP LSQPLASGSR IGSDPYLGQR LDSEASAHNL PEDTLTFEEA
VATNSGRSSR TSYVSSLTSQ SHPLRRVPNG YHCTLGLSTG VRARHSYHHP DQDHWC


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EIAAB05036 Cach1,Cach1b,Cacn1,Cacna1s,Cacnl1a3,Calcium channel, L type, alpha-1 polypeptide, isoform 3, skeletal muscle,Mouse,Mus musculus,Voltage-dependent L-type calcium channel subunit alpha-1S,Voltage-gated
EIAAB05018 CACH2,CACN2,CACNA1C,CACNL1A1,Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle,CCHL1A1,Homo sapiens,Human,Voltage-dependent L-type calcium channel subunit alpha-1C,Voltage-gated
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
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
E1344c ELISA CACNA1A,CHCACHA1A,Chicken,Gallus gallus,Voltage-dependent P_Q-type calcium channel subunit alpha-1A,Voltage-gated calcium channel subunit alpha Cav2.1 96T


 

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