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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_RABIT             Reviewed;        2339 AA.
Q05152;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 121.
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;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=8386525; DOI=10.1016/0896-6273(93)90162-K;
Fujita Y., Mynlieff M., Dirksen R.T., Kim M.-S., Niidome T., Nakai J.,
Friedrich T., Iwabe N., Miyata T., Furuichi T., Furutama D.,
Mikoshiba K., Mori Y., Beam K.G.;
"Primary structure and functional expression of the omega-conotoxin-
sensitive N-type calcium channel from rabbit brain.";
Neuron 10:585-598(1993).
-!- 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:
P62158:CALM3 (xeno); NbExp=2; IntAct=EBI-15685496, EBI-397435;
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- TISSUE SPECIFICITY: Widespread expression throughout the brain.
Highest levels in corpus striatum and midbrain.
-!- 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:0000250}.
-!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
1.A.1.11) family. CACNA1B subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D14157; BAA03202.1; -; mRNA.
RefSeq; NP_001075660.1; NM_001082191.1.
UniGene; Ocu.2138; -.
PDB; 3DVE; X-ray; 2.35 A; B=1855-1875.
PDB; 3DVJ; X-ray; 2.80 A; B=1853-1873.
PDBsum; 3DVE; -.
PDBsum; 3DVJ; -.
ProteinModelPortal; Q05152; -.
SMR; Q05152; -.
DIP; DIP-29592N; -.
IntAct; Q05152; 2.
STRING; 9986.ENSOCUP00000010930; -.
iPTMnet; Q05152; -.
GeneID; 100008979; -.
KEGG; ocu:100008979; -.
CTD; 774; -.
eggNOG; KOG2301; Eukaryota.
eggNOG; ENOG410XNP6; LUCA.
HOVERGEN; HBG050763; -.
InParanoid; Q05152; -.
KO; K04849; -.
EvolutionaryTrace; Q05152; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
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; 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 2339 Voltage-dependent N-type calcium channel
subunit alpha-1B.
/FTId=PRO_0000053923.
TOPO_DOM 1 95 Cytoplasmic. {ECO:0000255}.
TRANSMEM 96 114 Helical; Name=S1 of repeat I.
{ECO:0000255}.
TOPO_DOM 115 132 Extracellular. {ECO:0000255}.
TRANSMEM 133 152 Helical; Name=S2 of repeat I.
{ECO:0000255}.
TOPO_DOM 153 163 Cytoplasmic. {ECO:0000255}.
TRANSMEM 164 183 Helical; Name=S3 of repeat I.
{ECO:0000255}.
TOPO_DOM 184 187 Extracellular. {ECO:0000255}.
TRANSMEM 188 206 Helical; Name=S4 of repeat I.
{ECO:0000255}.
TOPO_DOM 207 225 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 484 502 Helical; Name=S1 of repeat II.
{ECO:0000255}.
TOPO_DOM 503 517 Extracellular. {ECO:0000255}.
TRANSMEM 518 537 Helical; Name=S2 of repeat II.
{ECO:0000255}.
TOPO_DOM 538 545 Cytoplasmic. {ECO:0000255}.
TRANSMEM 546 563 Helical; Name=S3 of repeat II.
{ECO:0000255}.
TOPO_DOM 564 574 Extracellular. {ECO:0000255}.
TRANSMEM 575 593 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 1156 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1157 1174 Helical; Name=S1 of repeat III.
{ECO:0000255}.
TOPO_DOM 1175 1190 Extracellular. {ECO:0000255}.
TRANSMEM 1191 1210 Helical; Name=S2 of repeat III.
{ECO:0000255}.
TOPO_DOM 1211 1222 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1223 1241 Helical; Name=S3 of repeat III.
{ECO:0000255}.
TOPO_DOM 1242 1251 Extracellular. {ECO:0000255}.
TRANSMEM 1252 1270 Helical; Name=S4 of repeat III.
{ECO:0000255}.
TOPO_DOM 1271 1289 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1290 1309 Helical; Name=S5 of repeat III.
{ECO:0000255}.
TOPO_DOM 1310 1396 Extracellular. {ECO:0000255}.
TRANSMEM 1397 1421 Helical; Name=S6 of repeat III.
{ECO:0000255}.
TOPO_DOM 1422 1476 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1477 1495 Helical; Name=S1 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1496 1510 Extracellular. {ECO:0000255}.
TRANSMEM 1511 1530 Helical; Name=S2 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1531 1538 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1539 1557 Helical; Name=S3 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1558 1566 Extracellular. {ECO:0000255}.
TRANSMEM 1567 1585 Helical; Name=S4 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1586 1604 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1605 1624 Helical; Name=S5 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1625 1686 Extracellular. {ECO:0000255}.
TRANSMEM 1687 1711 Helical; Name=S6 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1712 2339 Cytoplasmic. {ECO:0000255}.
REPEAT 82 359 I.
REPEAT 469 713 II.
REPEAT 1142 1424 III.
REPEAT 1461 1714 IV.
DOMAIN 1727 1762 EF-hand. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
NP_BIND 452 459 ATP. {ECO:0000255}.
CA_BIND 1740 1751 {ECO:0000255|PROSITE-ProRule:PRU00448}.
REGION 379 396 Binding to the beta subunit.
{ECO:0000250}.
COMPBIAS 2051 2055 Poly-His.
COMPBIAS 2119 2123 Poly-Ser.
COMPBIAS 2319 2324 Poly-Gly.
SITE 314 314 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 663 663 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1370 1370 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1658 1658 Calcium ion selectivity and permeability.
{ECO:0000250}.
MOD_RES 22 22 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:O55017}.
MOD_RES 411 411 Phosphoserine.
{ECO:0000250|UniProtKB:O55017}.
MOD_RES 746 746 Phosphoserine.
{ECO:0000250|UniProtKB:O55017}.
MOD_RES 749 749 Phosphoserine.
{ECO:0000250|UniProtKB:O55017}.
MOD_RES 784 784 Phosphoserine.
{ECO:0000250|UniProtKB:O55017}.
MOD_RES 1074 1074 Phosphoserine.
{ECO:0000250|UniProtKB:O55017}.
MOD_RES 1722 1722 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 2067 2067 Phosphoserine.
{ECO:0000250|UniProtKB:O55017}.
MOD_RES 2224 2224 Phosphoserine.
{ECO:0000250|UniProtKB:O55017}.
MOD_RES 2233 2233 Phosphoserine.
{ECO:0000250|UniProtKB:O55017}.
MOD_RES 2256 2256 Phosphoserine.
{ECO:0000250|UniProtKB:O55017}.
CARBOHYD 256 256 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1566 1566 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1678 1678 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
HELIX 1855 1869 {ECO:0000244|PDB:3DVE}.
SEQUENCE 2339 AA; 261181 MW; 0413DA93794C8B34 CRC64;
MVRFGDELGG RYGGAGGAER ARGGGAGGAG GPGPGGLPPG QRVLYKQSIA QRARTMALYN
PIPVKQNCFT VNRSLFVFSE DNVVRKYAKR ITEWPPFEYM ILATIIANCI VLALEQHLPD
GDKTPMSERL DDTEPYFIGI FCFEAGIKIL ALGFVLHKGS YLRNGWNVMD FVVVLTGILA
TAGTDFDLRT LRAVRVLRPL KLVSGIPSLQ VVLKSIMKAM VPLLQIGLLL FFAILMFAII
GLEFYMGKFH KACFPNSTDP DPVGDFPCGK EAPARLCEGD TECREYWAGP NFGITNFDNI
LFAILTVFQC ITMEGWTDIL YNTNDAAGNT WNWLYFIPLI IIGSFFMLNL VLGVLSGEFA
KERERVENRR AFLKLRRQQQ IERELNGYLE WIFKAEEVML AEEDRNAEEK SPLDAVLKRA
AAKKSRSDLI QAEEGEGRLT GLCAPGSPFA RASLKSGKTE SSSYFRRKEK MFRFFIRRMV
KAQSFYWTVL CVVALNTLCV AMVHYNQPQR LTTALYFAEF VFLGLFLTEM SLKMYGLGPR
SYFRSSFNCF DFGVIVGSIF EVVWAAVKPG TSFGISVLRA LRLLRIFKVT KYWNSLRNLV
VSLLNSMKSI ISLLFLLFLF IVVFALLGMQ LFGGQFNFKD ETPTTNFDTF PAAILTVFQI
LTGEDWNAVM YHGIESQGGV SRGMFSSFYF IVLTLFGNYT LLNVFLAIAV DNLANAQELT
KDEEEMEEAA NQKLALQKAK EVAEVSPMSA ANISIAARQQ NSAKARSVWE QRASQLRLQN
LRASCEALYS EMDPEERLRY ATARHLRPDV KTHLDRPLVV EPGRDAPRGP PGGKSRPDGS
EAPEGADPPR RHHRHRDKDK APATVPSAGE QDRAEALRAE GGELGPREER GRPRRSRSKE
APGAPEVRSD RGRGPCPEGG RRHHRRGSPE EAAEREPRRH RAHRHGPDPG KEGPASGTRG
ERRARHRTGP RACPREAESS EEPARRHRAR HKAPPTQETA EKDKEAAEKG GEATEAEKDK
EARNHQPKEL PCDLEAIGML GVGAVHTLPS TCLQKVEEQP EDADNQRNVT RMGSQPPDTS
TTVHIPVTLT GPPGETTVVP SGNVDLESQA EGKKEVETSD VMRSGPRPIV PYSSMFCLSP
TNLLRRCCHY IVTMRYFEMV ILVVIALSSI ALAAEDPVRT DSPRNNALKY MDYIFTGVFT
FEMVIKMIDL GLLLHPGAYF RDLWNILDFI VVSGALVAFA FSGSKGKDIS TIKSLRVLRV
LRPLKTIKRL PKLKAVFDCV VNSLKNVLNI LIVYMLFMFI FAVIAVQLFK GKFFYCTDES
KELERDCRGQ YLDYEKEEVE AQPRQWKKYD FHYDNVLWAL LTLFTVSTGE GWPMVLKHSV
DATYEEQGPS PGYRMELSIF YVVYFVVFPF FFVNIFVALI IITFQEQGDK VMSECSLEKN
ERACIDFAIS ARPLTRYMPQ NKQSFQYKTW TFVVSPPFEY FIMAMIALNT VVLMMKFYDA
PYEYELMLKC LNIVFTSMFS MECVLKIIAF GVLNYFRDAW NVFDFVTVLG SITDILVTEI
ANNFINLSFL RLFRAARLIK LLRQGYTIRI LLWTFVQSFK ALPYVCLLIA MLFFIYAIIG
MQVFGNIALD DDTSINRHNN FRTFLQALML LFRSATGEAW HEIMLSCLSS RACDEHSNAS
ECGSDFAYFY FVSFIFLCSF LMLNLFVAVI MDNFEYLTRD SSILGPHHLD EFIRVWAEYD
PAACGRISYS DMFEMLKHMS PPLGLGKKCP ARVAYKRLVR MNMPISSEDM TVHFTSTLMA
LIRTALDIKL APAGTKQHQC DAELRKEISC VWANLPQKTL DLLVPPHKPD EMTVGKVYAA
LMIFDFYKQN KTSRDQTQQA PGGLSQLGPV SLFHPLKATL EQTQPALRGA RAFLRQKSSA
SLSNGGAVQT QESGIKESVS WGTQRTQDVL CEARAPLERG HSAEIPVGQP GTLAVDVQMQ
NMTLSGPDAE PQPGLESQGR AASMPRLAAE TQPAPDASPM KRSISTLAPR PHTARLGSTA
LDRPAPSQAP HHHHHRCHRR RDRKQRSLEK GPSLSADTDG APDSTVGPGL PTGEGPPGCR
RERERRQERG RSQERRQPSS SSSEKHRFYS CDRFGGREPP QPKPSLSSHP TSPTAGQEPG
PHPQGSGSVH GSPLLSTSGA STPGRGRRQL PQTPLTPRPS VTYKTANSSP VHFAGAPSGL
PAFSPGRLSR GLSEHNALLQ RDPLSRPLAP GSRIGSDPYL GQRLDSEAPA RALPEDAPAF
EETAASNSGR SSRTSYVSSL TSQPPPLRRV PNGYHCTLGL GGGGRARRGC HHPDRDRRC


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