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Protein

Voltage-dependent N-type calcium channel subunit alpha-1B

Gene

CACNA1B

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei314 – 3141Calcium ion selectivity and permeabilityBy similarity
Sitei663 – 6631Calcium ion selectivity and permeabilityBy similarity
Sitei1370 – 13701Calcium ion selectivity and permeabilityBy similarity
Sitei1658 – 16581Calcium ion selectivity and permeabilityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi452 – 4598ATPSequence analysis
Calcium bindingi1740 – 175112PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • calcium ion transport Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel, Voltage-gated channel

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Calcium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-dependent N-type calcium channel subunit alpha-1B
Alternative name(s):
Brain calcium channel III
Short name:
BIII
Calcium channel, L type, alpha-1 polypeptide isoform 5
Voltage-gated calcium channel subunit alpha Cav2.2
Gene namesi
Name:CACNA1B
Synonyms:CACH5, CACNL1A5
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 9595CytoplasmicSequence analysisAdd
BLAST
Transmembranei96 – 11419Helical; Name=S1 of repeat ISequence analysisAdd
BLAST
Topological domaini115 – 13218ExtracellularSequence analysisAdd
BLAST
Transmembranei133 – 15220Helical; Name=S2 of repeat ISequence analysisAdd
BLAST
Topological domaini153 – 16311CytoplasmicSequence analysisAdd
BLAST
Transmembranei164 – 18320Helical; Name=S3 of repeat ISequence analysisAdd
BLAST
Topological domaini184 – 1874ExtracellularSequence analysis
Transmembranei188 – 20619Helical; Name=S4 of repeat ISequence analysisAdd
BLAST
Topological domaini207 – 22519CytoplasmicSequence analysisAdd
BLAST
Transmembranei226 – 24520Helical; Name=S5 of repeat ISequence analysisAdd
BLAST
Topological domaini246 – 33186ExtracellularSequence analysisAdd
BLAST
Transmembranei332 – 35625Helical; Name=S6 of repeat ISequence analysisAdd
BLAST
Topological domaini357 – 483127CytoplasmicSequence analysisAdd
BLAST
Transmembranei484 – 50219Helical; Name=S1 of repeat IISequence analysisAdd
BLAST
Topological domaini503 – 51715ExtracellularSequence analysisAdd
BLAST
Transmembranei518 – 53720Helical; Name=S2 of repeat IISequence analysisAdd
BLAST
Topological domaini538 – 5458CytoplasmicSequence analysis
Transmembranei546 – 56318Helical; Name=S3 of repeat IISequence analysisAdd
BLAST
Topological domaini564 – 57411ExtracellularSequence analysisAdd
BLAST
Transmembranei575 – 59319Helical; Name=S4 of repeat IISequence analysisAdd
BLAST
Topological domaini594 – 61219CytoplasmicSequence analysisAdd
BLAST
Transmembranei613 – 63220Helical; Name=S5 of repeat IISequence analysisAdd
BLAST
Topological domaini633 – 68553ExtracellularSequence analysisAdd
BLAST
Transmembranei686 – 71025Helical; Name=S6 of repeat IISequence analysisAdd
BLAST
Topological domaini711 – 1156446CytoplasmicSequence analysisAdd
BLAST
Transmembranei1157 – 117418Helical; Name=S1 of repeat IIISequence analysisAdd
BLAST
Topological domaini1175 – 119016ExtracellularSequence analysisAdd
BLAST
Transmembranei1191 – 121020Helical; Name=S2 of repeat IIISequence analysisAdd
BLAST
Topological domaini1211 – 122212CytoplasmicSequence analysisAdd
BLAST
Transmembranei1223 – 124119Helical; Name=S3 of repeat IIISequence analysisAdd
BLAST
Topological domaini1242 – 125110ExtracellularSequence analysis
Transmembranei1252 – 127019Helical; Name=S4 of repeat IIISequence analysisAdd
BLAST
Topological domaini1271 – 128919CytoplasmicSequence analysisAdd
BLAST
Transmembranei1290 – 130920Helical; Name=S5 of repeat IIISequence analysisAdd
BLAST
Topological domaini1310 – 139687ExtracellularSequence analysisAdd
BLAST
Transmembranei1397 – 142125Helical; Name=S6 of repeat IIISequence analysisAdd
BLAST
Topological domaini1422 – 147655CytoplasmicSequence analysisAdd
BLAST
Transmembranei1477 – 149519Helical; Name=S1 of repeat IVSequence analysisAdd
BLAST
Topological domaini1496 – 151015ExtracellularSequence analysisAdd
BLAST
Transmembranei1511 – 153020Helical; Name=S2 of repeat IVSequence analysisAdd
BLAST
Topological domaini1531 – 15388CytoplasmicSequence analysis
Transmembranei1539 – 155719Helical; Name=S3 of repeat IVSequence analysisAdd
BLAST
Topological domaini1558 – 15669ExtracellularSequence analysis
Transmembranei1567 – 158519Helical; Name=S4 of repeat IVSequence analysisAdd
BLAST
Topological domaini1586 – 160419CytoplasmicSequence analysisAdd
BLAST
Transmembranei1605 – 162420Helical; Name=S5 of repeat IVSequence analysisAdd
BLAST
Topological domaini1625 – 168662ExtracellularSequence analysisAdd
BLAST
Transmembranei1687 – 171125Helical; Name=S6 of repeat IVSequence analysisAdd
BLAST
Topological domaini1712 – 2339628CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • voltage-gated calcium channel complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 23392339Voltage-dependent N-type calcium channel subunit alpha-1BPRO_0000053923Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi256 – 2561N-linked (GlcNAc...)Sequence analysis
Modified residuei411 – 4111PhosphoserineBy similarity
Modified residuei746 – 7461PhosphoserineBy similarity
Modified residuei749 – 7491PhosphoserineBy similarity
Modified residuei784 – 7841PhosphoserineBy similarity
Modified residuei1074 – 10741PhosphoserineBy similarity
Glycosylationi1566 – 15661N-linked (GlcNAc...)Sequence analysis
Glycosylationi1678 – 16781N-linked (GlcNAc...)Sequence analysis
Modified residuei1722 – 17221Phosphoserine; by PKASequence analysis
Modified residuei2067 – 20671PhosphoserineBy similarity
Modified residuei2224 – 22241PhosphoserineBy similarity
Modified residuei2233 – 22331PhosphoserineBy similarity
Modified residuei2256 – 22561PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated in vitro by CaM-kinase II, PKA, PKC and CGPK.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

PTM databases

iPTMnetiQ05152.

Expressioni

Tissue specificityi

Widespread expression throughout the brain. Highest levels in corpus striatum and midbrain.

Interactioni

Subunit structurei

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.By similarity

Protein-protein interaction databases

DIPiDIP-29592N.
STRINGi9986.ENSOCUP00000010930.

Structurei

Secondary structure

1
2339
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1855 – 186915Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DVEX-ray2.35B1855-1875[»]
3DVJX-ray2.80B1853-1873[»]
ProteinModelPortaliQ05152.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05152.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati82 – 359278IAdd
BLAST
Repeati469 – 713245IIAdd
BLAST
Repeati1142 – 1424283IIIAdd
BLAST
Repeati1461 – 1714254IVAdd
BLAST
Domaini1727 – 176236EF-handPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni379 – 39618Binding to the beta subunitBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2051 – 20555Poly-His
Compositional biasi2119 – 21235Poly-Ser
Compositional biasi2319 – 23246Poly-Gly

Domaini

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 similaritiesi

Contains 1 EF-hand domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2301. Eukaryota.
ENOG410XNP6. LUCA.
HOVERGENiHBG050763.
InParanoidiQ05152.
KOiK04849.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR027359. Channel_four-helix_dom.
IPR002048. EF_hand_dom.
IPR031649. GPHH_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005447. VDCC_N_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PANTHERiPTHR10037:SF161. PTHR10037:SF161. 3 hits.
PfamiPF08763. Ca_chan_IQ. 1 hit.
PF16905. GPHH. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSiPR00167. CACHANNEL.
PR01631. NVDCCALPHA1.
SMARTiSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]
PROSITEiPS50222. EF_HAND_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q05152-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVRFGDELGG RYGGAGGAER ARGGGAGGAG GPGPGGLPPG QRVLYKQSIA
60 70 80 90 100
QRARTMALYN PIPVKQNCFT VNRSLFVFSE DNVVRKYAKR ITEWPPFEYM
110 120 130 140 150
ILATIIANCI VLALEQHLPD GDKTPMSERL DDTEPYFIGI FCFEAGIKIL
160 170 180 190 200
ALGFVLHKGS YLRNGWNVMD FVVVLTGILA TAGTDFDLRT LRAVRVLRPL
210 220 230 240 250
KLVSGIPSLQ VVLKSIMKAM VPLLQIGLLL FFAILMFAII GLEFYMGKFH
260 270 280 290 300
KACFPNSTDP DPVGDFPCGK EAPARLCEGD TECREYWAGP NFGITNFDNI
310 320 330 340 350
LFAILTVFQC ITMEGWTDIL YNTNDAAGNT WNWLYFIPLI IIGSFFMLNL
360 370 380 390 400
VLGVLSGEFA KERERVENRR AFLKLRRQQQ IERELNGYLE WIFKAEEVML
410 420 430 440 450
AEEDRNAEEK SPLDAVLKRA AAKKSRSDLI QAEEGEGRLT GLCAPGSPFA
460 470 480 490 500
RASLKSGKTE SSSYFRRKEK MFRFFIRRMV KAQSFYWTVL CVVALNTLCV
510 520 530 540 550
AMVHYNQPQR LTTALYFAEF VFLGLFLTEM SLKMYGLGPR SYFRSSFNCF
560 570 580 590 600
DFGVIVGSIF EVVWAAVKPG TSFGISVLRA LRLLRIFKVT KYWNSLRNLV
610 620 630 640 650
VSLLNSMKSI ISLLFLLFLF IVVFALLGMQ LFGGQFNFKD ETPTTNFDTF
660 670 680 690 700
PAAILTVFQI LTGEDWNAVM YHGIESQGGV SRGMFSSFYF IVLTLFGNYT
710 720 730 740 750
LLNVFLAIAV DNLANAQELT KDEEEMEEAA NQKLALQKAK EVAEVSPMSA
760 770 780 790 800
ANISIAARQQ NSAKARSVWE QRASQLRLQN LRASCEALYS EMDPEERLRY
810 820 830 840 850
ATARHLRPDV KTHLDRPLVV EPGRDAPRGP PGGKSRPDGS EAPEGADPPR
860 870 880 890 900
RHHRHRDKDK APATVPSAGE QDRAEALRAE GGELGPREER GRPRRSRSKE
910 920 930 940 950
APGAPEVRSD RGRGPCPEGG RRHHRRGSPE EAAEREPRRH RAHRHGPDPG
960 970 980 990 1000
KEGPASGTRG ERRARHRTGP RACPREAESS EEPARRHRAR HKAPPTQETA
1010 1020 1030 1040 1050
EKDKEAAEKG GEATEAEKDK EARNHQPKEL PCDLEAIGML GVGAVHTLPS
1060 1070 1080 1090 1100
TCLQKVEEQP EDADNQRNVT RMGSQPPDTS TTVHIPVTLT GPPGETTVVP
1110 1120 1130 1140 1150
SGNVDLESQA EGKKEVETSD VMRSGPRPIV PYSSMFCLSP TNLLRRCCHY
1160 1170 1180 1190 1200
IVTMRYFEMV ILVVIALSSI ALAAEDPVRT DSPRNNALKY MDYIFTGVFT
1210 1220 1230 1240 1250
FEMVIKMIDL GLLLHPGAYF RDLWNILDFI VVSGALVAFA FSGSKGKDIS
1260 1270 1280 1290 1300
TIKSLRVLRV LRPLKTIKRL PKLKAVFDCV VNSLKNVLNI LIVYMLFMFI
1310 1320 1330 1340 1350
FAVIAVQLFK GKFFYCTDES KELERDCRGQ YLDYEKEEVE AQPRQWKKYD
1360 1370 1380 1390 1400
FHYDNVLWAL LTLFTVSTGE GWPMVLKHSV DATYEEQGPS PGYRMELSIF
1410 1420 1430 1440 1450
YVVYFVVFPF FFVNIFVALI IITFQEQGDK VMSECSLEKN ERACIDFAIS
1460 1470 1480 1490 1500
ARPLTRYMPQ NKQSFQYKTW TFVVSPPFEY FIMAMIALNT VVLMMKFYDA
1510 1520 1530 1540 1550
PYEYELMLKC LNIVFTSMFS MECVLKIIAF GVLNYFRDAW NVFDFVTVLG
1560 1570 1580 1590 1600
SITDILVTEI ANNFINLSFL RLFRAARLIK LLRQGYTIRI LLWTFVQSFK
1610 1620 1630 1640 1650
ALPYVCLLIA MLFFIYAIIG MQVFGNIALD DDTSINRHNN FRTFLQALML
1660 1670 1680 1690 1700
LFRSATGEAW HEIMLSCLSS RACDEHSNAS ECGSDFAYFY FVSFIFLCSF
1710 1720 1730 1740 1750
LMLNLFVAVI MDNFEYLTRD SSILGPHHLD EFIRVWAEYD PAACGRISYS
1760 1770 1780 1790 1800
DMFEMLKHMS PPLGLGKKCP ARVAYKRLVR MNMPISSEDM TVHFTSTLMA
1810 1820 1830 1840 1850
LIRTALDIKL APAGTKQHQC DAELRKEISC VWANLPQKTL DLLVPPHKPD
1860 1870 1880 1890 1900
EMTVGKVYAA LMIFDFYKQN KTSRDQTQQA PGGLSQLGPV SLFHPLKATL
1910 1920 1930 1940 1950
EQTQPALRGA RAFLRQKSSA SLSNGGAVQT QESGIKESVS WGTQRTQDVL
1960 1970 1980 1990 2000
CEARAPLERG HSAEIPVGQP GTLAVDVQMQ NMTLSGPDAE PQPGLESQGR
2010 2020 2030 2040 2050
AASMPRLAAE TQPAPDASPM KRSISTLAPR PHTARLGSTA LDRPAPSQAP
2060 2070 2080 2090 2100
HHHHHRCHRR RDRKQRSLEK GPSLSADTDG APDSTVGPGL PTGEGPPGCR
2110 2120 2130 2140 2150
RERERRQERG RSQERRQPSS SSSEKHRFYS CDRFGGREPP QPKPSLSSHP
2160 2170 2180 2190 2200
TSPTAGQEPG PHPQGSGSVH GSPLLSTSGA STPGRGRRQL PQTPLTPRPS
2210 2220 2230 2240 2250
VTYKTANSSP VHFAGAPSGL PAFSPGRLSR GLSEHNALLQ RDPLSRPLAP
2260 2270 2280 2290 2300
GSRIGSDPYL GQRLDSEAPA RALPEDAPAF EETAASNSGR SSRTSYVSSL
2310 2320 2330
TSQPPPLRRV PNGYHCTLGL GGGGRARRGC HHPDRDRRC
Length:2,339
Mass (Da):261,181
Last modified:November 1, 1996 - v1
Checksum:i0413DA93794C8B34
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14157 mRNA. Translation: BAA03202.1.
RefSeqiNP_001075660.1. NM_001082191.1.
UniGeneiOcu.2138.

Genome annotation databases

GeneIDi100008979.
KEGGiocu:100008979.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14157 mRNA. Translation: BAA03202.1.
RefSeqiNP_001075660.1. NM_001082191.1.
UniGeneiOcu.2138.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DVEX-ray2.35B1855-1875[»]
3DVJX-ray2.80B1853-1873[»]
ProteinModelPortaliQ05152.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29592N.
STRINGi9986.ENSOCUP00000010930.

PTM databases

iPTMnetiQ05152.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100008979.
KEGGiocu:100008979.

Organism-specific databases

CTDi774.

Phylogenomic databases

eggNOGiKOG2301. Eukaryota.
ENOG410XNP6. LUCA.
HOVERGENiHBG050763.
InParanoidiQ05152.
KOiK04849.

Miscellaneous databases

EvolutionaryTraceiQ05152.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR027359. Channel_four-helix_dom.
IPR002048. EF_hand_dom.
IPR031649. GPHH_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005447. VDCC_N_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PANTHERiPTHR10037:SF161. PTHR10037:SF161. 3 hits.
PfamiPF08763. Ca_chan_IQ. 1 hit.
PF16905. GPHH. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSiPR00167. CACHANNEL.
PR01631. NVDCCALPHA1.
SMARTiSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]
PROSITEiPS50222. EF_HAND_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCAC1B_RABIT
AccessioniPrimary (citable) accession number: Q05152
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.