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Q02294 (CAC1B_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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 names
Name:Cacna1b
Synonyms:Cach5, Cacnl1a5
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length2336 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-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 structure

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 and RIMBP2 By similarity. Ref.4

Subcellular location

Membrane; Multi-pass membrane protein.

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. Ref.4

Post-translational modification

Phosphorylated in vitro by CaM-kinase II, PKA, PKC and CGPK. Ref.3

Sequence similarities

Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family. CACNA1B subfamily. [View classification]

Contains 1 EF-hand domain.

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandATP-binding
Calcium
Metal-binding
Nucleotide-binding
   Molecular functionCalcium channel
Ion channel
Voltage-gated channel
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion import

Inferred from mutant phenotype PubMed 15548655. Source: RGD

positive regulation of neurotransmitter secretion

Inferred from mutant phenotype PubMed 15987667. Source: RGD

response to ethanol

Inferred from expression pattern PubMed 16860782. Source: RGD

response to testosterone stimulus

Inferred from mutant phenotype PubMed 15987667. Source: RGD

sensory perception of pain

Inferred from mutant phenotype PubMed 18433788. Source: RGD

   Cellular_componentaxon terminus

Inferred from direct assay PubMed 16736476. Source: RGD

dendritic shaft

Inferred from direct assay PubMed 11353727. Source: RGD

neuronal cell body

Inferred from direct assay PubMed 11353727. Source: RGD

plasma membrane

Inferred from direct assay PubMed 10864934PubMed 17068255. Source: RGD

protein complex

Inferred from direct assay PubMed 17068255. Source: RGD

voltage-gated calcium channel complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium ion binding

Inferred from electronic annotation. Source: InterPro

high voltage-gated calcium channel activity

Inferred from direct assay PubMed 18701069. Source: RGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Syt1P217072EBI-540038,EBI-458098

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: 2 isoforms may be produced.
Isoform 1 (identifier: Q02294-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 23362336Voltage-dependent N-type calcium channel subunit alpha-1B
PRO_0000053924

Regions

Topological domain1 – 9595Cytoplasmic Potential
Transmembrane96 – 11419Helical; Name=S1 of repeat I; Potential
Topological domain115 – 13319Extracellular Potential
Transmembrane134 – 15118Helical; Name=S2 of repeat I; Potential
Topological domain152 – 16413Cytoplasmic Potential
Transmembrane165 – 17915Helical; Name=S3 of repeat I; Potential
Topological domain180 – 1867Extracellular Potential
Transmembrane187 – 20519Helical; Name=S4 of repeat I; Potential
Topological domain206 – 22520Cytoplasmic Potential
Transmembrane226 – 24520Helical; Name=S5 of repeat I; Potential
Topological domain246 – 33186Extracellular Potential
Transmembrane332 – 35625Helical; Name=S6 of repeat I; Potential
Topological domain357 – 483127Cytoplasmic Potential
Transmembrane484 – 50320Helical; Name=S1 of repeat II; Potential
Topological domain504 – 51714Extracellular Potential
Transmembrane518 – 53720Helical; Name=S2 of repeat II; Potential
Topological domain538 – 5458Cytoplasmic Potential
Transmembrane546 – 56419Helical; Name=S3 of repeat II; Potential
Topological domain565 – 57511Extracellular Potential
Transmembrane576 – 59318Helical; Name=S4 of repeat II; Potential
Topological domain594 – 61219Cytoplasmic Potential
Transmembrane613 – 63220Helical; Name=S5 of repeat II; Potential
Topological domain633 – 68553Extracellular Potential
Transmembrane686 – 71025Helical; Name=S6 of repeat II; Potential
Topological domain711 – 1143433Cytoplasmic Potential
Transmembrane1144 – 116724Helical; Name=S1 of repeat III; Potential
Topological domain1168 – 118417Extracellular Potential
Transmembrane1185 – 120420Helical; Name=S2 of repeat III; Potential
Topological domain1205 – 12128Cytoplasmic Potential
Transmembrane1213 – 123523Helical; Name=S3 of repeat III; Potential
Topological domain1236 – 125015Extracellular Potential
Transmembrane1251 – 126515Helical; Name=S4 of repeat III; Potential
Topological domain1266 – 128621Cytoplasmic Potential
Transmembrane1287 – 130620Helical; Name=S5 of repeat III; Potential
Topological domain1307 – 139286Extracellular Potential
Transmembrane1393 – 141725Helical; Name=S6 of repeat III; Potential
Topological domain1418 – 147457Cytoplasmic Potential
Transmembrane1475 – 149319Helical; Name=S1 of repeat IV; Potential
Topological domain1494 – 150714Extracellular Potential
Transmembrane1508 – 152720Helical; Name=S2 of repeat IV; Potential
Topological domain1528 – 15369Cytoplasmic Potential
Transmembrane1537 – 155519Helical; Name=S3 of repeat IV; Potential
Topological domain1556 – 15638Extracellular Potential
Transmembrane1564 – 158219Helical; Name=S4 of repeat IV; Potential
Topological domain1583 – 160119Cytoplasmic Potential
Transmembrane1602 – 162120Helical; Name=S5 of repeat IV; Potential
Topological domain1622 – 168362Extracellular Potential
Transmembrane1684 – 170320Helical; Name=S6 of repeat IV; Potential
Topological domain1704 – 2336633Cytoplasmic Potential
Repeat82 – 359278I
Repeat469 – 713245II
Repeat1135 – 1421287III
Repeat1458 – 1711254IV
Domain1724 – 175936EF-hand
Nucleotide binding452 – 4598ATP Potential
Calcium binding1737 – 174812 By similarity
Region379 – 39618Binding to the beta subunit
Compositional bias2049 – 20535Poly-His
Compositional bias2115 – 21195Poly-Ser

Sites

Site3141Calcium ion selectivity and permeability By similarity
Site6641Calcium ion selectivity and permeability By similarity
Site13671Calcium ion selectivity and permeability By similarity
Site16551Calcium ion selectivity and permeability By similarity

Amino acid modifications

Modified residue7461Phosphoserine By similarity
Modified residue7841Phosphoserine By similarity
Modified residue17191Phosphoserine; by PKA Potential
Modified residue22531Phosphoserine By similarity
Glycosylation2561N-linked (GlcNAc...) Potential
Glycosylation15631N-linked (GlcNAc...) Potential
Glycosylation16751N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict15381N → D no nucleotide entry Ref.2
Sequence conflict15791C → L no nucleotide entry Ref.2

Secondary structure

1 ... 2336
Helix Strand Turn

Details...

Sequences

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

Last modified October 1, 1996. Version 1.
Checksum: 8D50AF67834FD1BC

FASTA2,336262,256
        10         20         30         40         50         60 
MVRFGDELGG RYGGTGGGER ARGGGAGGAG GPGQGGLPPG QRVLYKQSIA QRARTMALYN 

        70         80         90        100        110        120 
PIPVKQNCFT VNRSLFVFSE DNVVRKYAKR ITEWPPFEYM ILATIIANCI VLALEQHLPD 

       130        140        150        160        170        180 
GDKTPMSERL DDTEPYFIGI FCFEAGIKII ALGFVFHKGS YLRNGWNVMD FVVVLTEILA 

       190        200        210        220        230        240 
TAGTDFDLRT LRAVRVLRPL KLVSGIPSLQ VVLKSIMKAM VPLLQIGLLL FFAILMFAII 

       250        260        270        280        290        300 
GLEFYMGKFH KACFPNSTDA EPVGDFPCGK EAPARLCDSD TECREYWPGP NFGITNFDNI 

       310        320        330        340        350        360 
LFAILTVFQC ITMEGWTDIL YNTNDAAGNT WNWLYFIPLI IIGSFFMLNL VLGVLSGEFA 

       370        380        390        400        410        420 
KERERVENRR AFLKLRRQQQ IERELNGYLE WIFKAEEVML AEEDKNAEEK SPLDAVLKRA 

       430        440        450        460        470        480 
ATKKSRNDLI HAEEGEDRFV DLCAAGSPFA RASLKSGKTE SSSYFRRKEK MFRFLIRRMV 

       490        500        510        520        530        540 
KAQSFYWVVL CVVALNTLCV AMVHYNQPQR LTTALYFAEF VFLGLFLTEM SLKMYGLGPR 

       550        560        570        580        590        600 
SYFRSSFNCF DFGVIVGSIF EVVWAAIKPG TSFGISVLRA LRLLRIFKVT KYWNSLRNLV 

       610        620        630        640        650        660 
VSLLNSMKSI ISLLFLLFLF IVVFALLGMQ LFGGQFNFQD ETPTTNFDTF PAAILTVFQI 

       670        680        690        700        710        720 
LTGEDWNAVM YHGIESQGGV SKGMFSSFYF IVLTLFGNYT LLNVFLAIAV DNLANAQELT 

       730        740        750        760        770        780 
KDEEEMEEAA NQKLALQKAK EVAEVSPMSA ANISIAARQQ NSAKARSVWE QRASQLRLQN 

       790        800        810        820        830        840 
LRASCEALYS EMDPEERLRY ASTRHVRPDM KTHMDRPLVV EPGRDGLRGP AGNKSKPEGT 

       850        860        870        880        890        900 
EATEGADPPR RHHRHRDRDK TSASTPAGGE QDRTDCPKAE STETGAREER ARPRRSHSKE 

       910        920        930        940        950        960 
APGADTQVRC ERSRRHHRRG SPEEATEREP RRHRAHRHAQ DSSKEGKEGT APVLVPKGER 

       970        980        990       1000       1010       1020 
RARHRGPRTG PRETENSEEP TRRHRAKHKV PPTLEPPERE VAEKESNVVE GDKETRNHQP 

      1030       1040       1050       1060       1070       1080 
KEPRCDLEAI AVTGVGSLHM LPSTCLQKVD EQPEDADNQR NVTRMGSQPS DPSTTVHVPV 

      1090       1100       1110       1120       1130       1140 
TLTGPPGEAT VVPSANTDLE GQAEGKKEAE ADDVLRRGPR PIVPYSSMFC LSPTNLLRRF 

      1150       1160       1170       1180       1190       1200 
CHYIVTMRYF EMVILVVIAL SSIALAAEDP VRTDSFRNNA LKYMDYIFTG VFTFEMVIKM 

      1210       1220       1230       1240       1250       1260 
IDLGLLLHPG AYFRDLWNIL DFIVVSGALV AFAFSSFMGG SKGKDINTIK SLRVLRVLRP 

      1270       1280       1290       1300       1310       1320 
LKTIKRLPKL KAVFDCVVNS LKNVLNILIV YMLFMFIFAV IAVQLFKGKF FYCTDESKEL 

      1330       1340       1350       1360       1370       1380 
ERDCRGQYLD YEKEEVEAQP RQWKKYDFHY DNVLWALLTL FTVSTGEGWP MVLKHSVDAT 

      1390       1400       1410       1420       1430       1440 
YEEQGPSPGF RMELSIFYVV YFVVFPFFFV NIFVALIIIT FQEQGDKVMS ECSLEKNERA 

      1450       1460       1470       1480       1490       1500 
CIDFAISAKP LTRYMPQNKQ SFQYKTWTFV VSPPFEYFIM AMIALNTVVL MMKFYDAPYE 

      1510       1520       1530       1540       1550       1560 
YELMLKCLNI VFTSMFSLEC ILKIIAFGVL NYFRDAWNVF DFVTVLGSIT DILVTEIANN 

      1570       1580       1590       1600       1610       1620 
FINLSFLRLF RAARLIKLCR QGYTIRILLW TFVQSFKALP YVCLLIAMLF FIYAIIGMQV 

      1630       1640       1650       1660       1670       1680 
FGNIALDDGT SINRHNNFRT FLQALMLLFR SATGEAWHEI MLSCLGNRAC DPHANASECG 

      1690       1700       1710       1720       1730       1740 
SDFAYFYFVS FIFLCSFLML NLFVAVIMDN FEYLTRDSSI LGPHHLDEFI RVWAEYDPAA 

      1750       1760       1770       1780       1790       1800 
CGRISYNDMF EMLKHMSPPL GLGKKCPARV AYKRLVRMNM PISNEDMTVH FTSTLMALIR 

      1810       1820       1830       1840       1850       1860 
TALEIKLAPA GTKQHQCDAE LRKEISSVWA NLPQKTLDLL VPPHKPDEMT VGKVYAALMI 

      1870       1880       1890       1900       1910       1920 
FDFYKQNKTT RDQTHQAPGG LSQMGPVSLF HPLKATLEQT QPAVLRGARV FLRQKSATSL 

      1930       1940       1950       1960       1970       1980 
SNGGAIQTQE SGIKESLSWG TQRTQDVLYE ARAPLERGHS AEIPVGQPGA LAVDVQMQNM 

      1990       2000       2010       2020       2030       2040 
TLRGPDGEPQ PGLESQGRAA SMPRLAAETQ PAPNASPMKR SISTLAPRPH GTQLCNTVLD 

      2050       2060       2070       2080       2090       2100 
RPPPSQVSHH HHHRCHRRRD KKQRSLEKGP SLSVDTEGAP STAAGSGLPH GEGSTGCRRE 

      2110       2120       2130       2140       2150       2160 
RKQERGRSQE RRQPSSSSSE KQRFYSCDRF GSREPPQPKP SLSSHPISPT AALEPGPHPQ 

      2170       2180       2190       2200       2210       2220 
GSGSVNGSPL MSTSGASTPG RGGRRQLPQT PLTPRPSITY KTANSSPVHF AEGQSGLPAF 

      2230       2240       2250       2260       2270       2280 
SPGRLSRGLS EHNALLQKEP LSQPLASGSR IGSDPYLGQR LDSEASAHNL PEDTLTFEEA 

      2290       2300       2310       2320       2330 
VATNSGRSSR TSYVSSLTSQ SHPLRRVPNG YHCTLGLSTG VRARHSYHHP DQDHWC

« Hide

References

[1]"Molecular cloning of the alpha-1 subunit of an omega-conotoxin-sensitive calcium channel."
Dubel S.J., Starr T.V.B., Hell J.W., Ahlijanian M.K., Enyeart J.J., Catterall W.A., Snutch T.P.
Proc. Natl. Acad. Sci. U.S.A. 89:5058-5062(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Brain.
[2]"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 1516-1679 (CLONE RBB-10).
[3]"Differential phosphorylation of two size forms of the N-type calcium channel alpha 1 subunit which have different COOH termini."
Hell J.W., Appleyard S.M., Yokoyama C.T., Warner C., Catterall W.A.
J. Biol. Chem. 269:7390-7396(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[4]"Calcium channel beta-subunit binds to a conserved motif in the I-II cytoplasmic linker of the alpha 1-subunit."
Pragnell M., de Waard M., Mori Y., Tanabe T., Snutch T.P., Campbell K.P.
Nature 368:67-70(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: BETA-SUBUNIT BINDING DOMAIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M92905 mRNA. Translation: AAA42014.1.
IPIIPI00948114.
PIRB35901.
UniGeneRn.85880.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4DEXX-ray2.00B358-468[»]
ProteinModelPortalQ02294.
ModBaseSearch...

Protein-protein interaction databases

IntActQ02294. 3 interactions.
MINTMINT-102470.

PTM databases

PhosphoSiteQ02294.

Proteomic databases

PaxDbQ02294.
PRIDEQ02294.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:628852. rat.

Organism-specific databases

RGD628852. Cacna1b.

Phylogenomic databases

eggNOGCOG1226.
HOGENOMHOG000231530.
HOVERGENHBG050763.

Gene expression databases

ArrayExpressQ02294.
GenevestigatorQ02294.
GermOnlineENSRNOG00000004560. Rattus norvegicus.

Family and domain databases

InterProIPR002048. EF_hand_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005447. VDCC_N_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PANTHERPTHR10037:SF131. PTHR10037:SF131. 1 hit.
PfamPF08763. Ca_chan_IQ. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSPR00167. CACHANNEL.
PR01631. NVDCCALPHA1.
SMARTSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]
PROSITEPS50222. EF_HAND_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBQ02294.
ChEMBLCHEMBL5107.

Entry information

Entry nameCAC1B_RAT
AccessionPrimary (citable) accession number: Q02294
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 1, 2013
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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