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Protein

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

Gene

Cacna1b

Organism
Mus musculus (Mouse)
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)DescriptionActionsGraphical viewLength
Sitei314Calcium ion selectivity and permeabilityBy similarity1
Sitei663Calcium ion selectivity and permeabilityBy similarity1
Sitei1358Calcium ion selectivity and permeabilityBy similarity1
Sitei1646Calcium ion selectivity and permeabilityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi451 – 458ATPSequence analysis8
Calcium bindingi1728 – 1739PROSITE-ProRule annotationAdd BLAST12

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calcium ion binding Source: InterPro
  • high voltage-gated calcium channel activity Source: MGI
  • protein C-terminus binding Source: MGI
  • voltage-gated calcium channel activity Source: MGI

GO - Biological processi

  • calcium ion transmembrane transport Source: MGI
  • calcium ion transport Source: MGI
  • locomotory behavior Source: MGI
  • membrane depolarization during action potential Source: GO_Central
  • neurotransmitter secretion Source: MGI
  • regulation of blood pressure Source: MGI
  • regulation of calcium ion transport Source: MGI
  • regulation of heart contraction Source: MGI
  • response to pain Source: MGI
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

Enzyme and pathway databases

ReactomeiR-MMU-112308. Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels.

Protein family/group databases

TCDBi1.A.1.11.9. the voltage-gated ion channel (vic) superfamily.

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, Cchn1a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:88296. Cacna1b.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 95CytoplasmicSequence analysisAdd BLAST95
Transmembranei96 – 114Helical; Name=S1 of repeat ISequence analysisAdd BLAST19
Topological domaini115 – 133ExtracellularSequence analysisAdd BLAST19
Transmembranei134 – 151Helical; Name=S2 of repeat ISequence analysisAdd BLAST18
Topological domaini152 – 164CytoplasmicSequence analysisAdd BLAST13
Transmembranei165 – 179Helical; Name=S3 of repeat ISequence analysisAdd BLAST15
Topological domaini180 – 186ExtracellularSequence analysis7
Transmembranei187 – 205Helical; Name=S4 of repeat ISequence analysisAdd BLAST19
Topological domaini206 – 225CytoplasmicSequence analysisAdd BLAST20
Transmembranei226 – 245Helical; Name=S5 of repeat ISequence analysisAdd BLAST20
Topological domaini246 – 331ExtracellularSequence analysisAdd BLAST86
Transmembranei332 – 356Helical; Name=S6 of repeat ISequence analysisAdd BLAST25
Topological domaini357 – 482CytoplasmicSequence analysisAdd BLAST126
Transmembranei483 – 502Helical; Name=S1 of repeat IISequence analysisAdd BLAST20
Topological domaini503 – 516ExtracellularSequence analysisAdd BLAST14
Transmembranei517 – 536Helical; Name=S2 of repeat IISequence analysisAdd BLAST20
Topological domaini537 – 544CytoplasmicSequence analysis8
Transmembranei545 – 563Helical; Name=S3 of repeat IISequence analysisAdd BLAST19
Topological domaini564 – 574ExtracellularSequence analysisAdd BLAST11
Transmembranei575 – 592Helical; Name=S4 of repeat IISequence analysisAdd BLAST18
Topological domaini593 – 611CytoplasmicSequence analysisAdd BLAST19
Transmembranei612 – 631Helical; Name=S5 of repeat IISequence analysisAdd BLAST20
Topological domaini632 – 684ExtracellularSequence analysisAdd BLAST53
Transmembranei685 – 709Helical; Name=S6 of repeat IISequence analysisAdd BLAST25
Topological domaini710 – 1134CytoplasmicSequence analysisAdd BLAST425
Transmembranei1135 – 1158Helical; Name=S1 of repeat IIISequence analysisAdd BLAST24
Topological domaini1159 – 1175ExtracellularSequence analysisAdd BLAST17
Transmembranei1176 – 1195Helical; Name=S2 of repeat IIISequence analysisAdd BLAST20
Topological domaini1196 – 1203CytoplasmicSequence analysis8
Transmembranei1204 – 1226Helical; Name=S3 of repeat IIISequence analysisAdd BLAST23
Topological domaini1227 – 1241ExtracellularSequence analysisAdd BLAST15
Transmembranei1242 – 1256Helical; Name=S4 of repeat IIISequence analysisAdd BLAST15
Topological domaini1257 – 1277CytoplasmicSequence analysisAdd BLAST21
Transmembranei1278 – 1297Helical; Name=S5 of repeat IIISequence analysisAdd BLAST20
Topological domaini1298 – 1383ExtracellularSequence analysisAdd BLAST86
Transmembranei1384 – 1408Helical; Name=S6 of repeat IIISequence analysisAdd BLAST25
Topological domaini1409 – 1465CytoplasmicSequence analysisAdd BLAST57
Transmembranei1466 – 1484Helical; Name=S1 of repeat IVSequence analysisAdd BLAST19
Topological domaini1485 – 1498ExtracellularSequence analysisAdd BLAST14
Transmembranei1499 – 1518Helical; Name=S2 of repeat IVSequence analysisAdd BLAST20
Topological domaini1519 – 1527CytoplasmicSequence analysis9
Transmembranei1528 – 1546Helical; Name=S3 of repeat IVSequence analysisAdd BLAST19
Topological domaini1547 – 1554ExtracellularSequence analysis8
Transmembranei1555 – 1573Helical; Name=S4 of repeat IVSequence analysisAdd BLAST19
Topological domaini1574 – 1592CytoplasmicSequence analysisAdd BLAST19
Transmembranei1593 – 1612Helical; Name=S5 of repeat IVSequence analysisAdd BLAST20
Topological domaini1613 – 1674ExtracellularSequence analysisAdd BLAST62
Transmembranei1675 – 1694Helical; Name=S6 of repeat IVSequence analysisAdd BLAST20
Topological domaini1695 – 2327CytoplasmicSequence analysisAdd BLAST633

GO - Cellular componenti

  • dendrite Source: MGI
  • membrane Source: MGI
  • neuronal cell body Source: MGI
  • presynapse Source: GOC
  • voltage-gated calcium channel complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3637936.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000539221 – 2327Voltage-dependent N-type calcium channel subunit alpha-1BAdd BLAST2327

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei22Omega-N-methylarginineCombined sources1
Glycosylationi256N-linked (GlcNAc...)Sequence analysis1
Modified residuei411PhosphoserineCombined sources1
Modified residuei745PhosphoserineCombined sources1
Modified residuei748PhosphoserineCombined sources1
Modified residuei783PhosphoserineCombined sources1
Modified residuei1058PhosphoserineCombined sources1
Glycosylationi1554N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1666N-linked (GlcNAc...)Sequence analysis1
Modified residuei1710Phosphoserine; by PKASequence analysis1
Modified residuei2056PhosphoserineCombined sources1
Modified residuei2212PhosphoserineCombined sources1
Modified residuei2221PhosphoserineCombined sources1
Modified residuei2244PhosphoserineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

MaxQBiO55017.
PaxDbiO55017.
PRIDEiO55017.

PTM databases

iPTMnetiO55017.
PhosphoSitePlusiO55017.

Expressioni

Tissue specificityi

Widespread expression throughout the brain. Highest levels in pyramidal cell layers C1, C2 and C3 of the hippocampus, in the dentate gyrus, in the cortex layers 2 et 4, in the subiculum and the habenula.

Gene expression databases

BgeeiENSMUSG00000004113.
ExpressionAtlasiO55017. baseline and differential.
GenevisibleiO55017. MM.

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 (PubMed:11438518). Interacts with FMR1 (via C-terminus); this interaction induces a deacrease in the number of presynaptic functional CACNA1B channels at the cell surface (PubMed:24709664).2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198431. 5 interactors.
IntActiO55017. 2 interactors.
STRINGi10090.ENSMUSP00000037416.

Structurei

3D structure databases

ProteinModelPortaliO55017.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati82 – 359IAdd BLAST278
Repeati468 – 712IIAdd BLAST245
Repeati1126 – 1412IIIAdd BLAST287
Repeati1449 – 1702IVAdd BLAST254
Domaini1715 – 1750EF-handPROSITE-ProRule annotationAdd BLAST36

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni379 – 396Binding to the beta subunitBy similarityAdd BLAST18

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2040 – 2044Poly-His5
Compositional biasi2106 – 2110Poly-Ser5

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.
GeneTreeiENSGT00830000128247.
HOGENOMiHOG000231530.
HOVERGENiHBG050763.
InParanoidiO55017.
KOiK04849.
TreeFamiTF312805.

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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform NB1 (identifier: O55017-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MVRFGDELGG RYGGTGGGER ARGGGAGGAG GPGQGGLPPG QRVLYKQSIA
60 70 80 90 100
QRARTMALYN PIPVKQNCFT VNRSLFVFSE DNVVRKYAKR ITEWPPFEYM
110 120 130 140 150
ILATIIANCI VLALEQHLPD GDKTPMSERL DDTEPYFIGI FCFEAGIKII
160 170 180 190 200
ALGFVFHKGS YLRNGWNVMD FVVVLTGILA TAGTDFDLRT LRAVRVLRPL
210 220 230 240 250
KLVSGIPSLQ VVLKSIMKAM VPLLQIGLLL FFAILMFAII GLEFYMGKFH
260 270 280 290 300
KACFPNSTDT EPVGDFPCGK DPPARQCDGD TECREYWPGP 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
AEEDKNAEEK SPLDVLKRAA TKKSRNDLIH AEEGEDRFVD LCAVGSPFAR
460 470 480 490 500
ASLKSGKTES SSYFRRKEKM FRFFIRRMVK AQSFYWVVLC VVALNTLCVA
510 520 530 540 550
MVHYNQPQRL TTALYFAEFV FLGLFLTEMS LKMYGLGPRS YFRSSFNCFD
560 570 580 590 600
FGVIVGSIFE VVWAAIKPGT SFGISVLRAL RLLRIFKVTK YWNSLRNLVV
610 620 630 640 650
SLLNSMKSII SLLFLLFLFI VVFALLGMQL FGGQFNFQDE TPTTNFDTFP
660 670 680 690 700
AAILTVFQIL TGEDWNAVMY HGIESQGGVS KGMFSSFYFI VLTLFGNYTL
710 720 730 740 750
LNVFLAIAVD NLANAQELTK DEEEMEEAAN QKLALQKAKE VAEVSPMSAA
760 770 780 790 800
NISIAARQQN SAKARSVWEQ RASQLRLQNL RASCEALYSE MDPEERLRYA
810 820 830 840 850
STRHVRPDMK THMDRPLVVE PGRDGLRGPV GSKSKPEGTE ATESADLPRR
860 870 880 890 900
HHRHRDRDKT SATAPAGGEQ DRTESTETGA REERARPRRS HSKETPGADT
910 920 930 940 950
QVRCERSRRH HRRGSPEEAT EREPRRHRAH RHAQDSSKEG TAPVLVPKGE
960 970 980 990 1000
RRARHRGPRT GPREAENNEE PTRRHRARHK VPPTLQPPER EAAEKESNAV
1010 1020 1030 1040 1050
EGDKETRNHQ PKEPHCDLEA IAVTGVGPLH MLPSTCLQKV DEQPEDADNQ
1060 1070 1080 1090 1100
RNVTRMGSQP SDPSTTVHVP VTLTGPPGET PVVPSGNMNL EGQAEGKKEA
1110 1120 1130 1140 1150
EADDVLRRGP RPIVPYSSMF CLSPTNLLRR FCHYIVTMRY FEMVILVVIA
1160 1170 1180 1190 1200
LSSIALAAED PVRTDSFRNN ALKYMDYIFT GVFTFEMVIK MIDLGLLLHP
1210 1220 1230 1240 1250
GAYFRDLWNI LDFIVVSGAL VAFAFSSFMG GSKGKDINTI KSLRVLRVLR
1260 1270 1280 1290 1300
PLKTIKRLPK LKAVFDCVVN SLKNVLNILI VYMLFMFIFA VIAVQLFKGK
1310 1320 1330 1340 1350
FFYCTDESKE LERDCRGQYL DYEKEEVEAQ PRQWKKYDFH YDNVLWALLT
1360 1370 1380 1390 1400
LFTVSTGEGW PMVLKHSVDA TYEEQGPSPG FRMELSIFYV VYFVVFPFFF
1410 1420 1430 1440 1450
VNIFVALIII TFQEQGDKVM SECSLEKNER ACIDFAISAK PLTRYMPQNK
1460 1470 1480 1490 1500
QSFQYKTWTF VVSPPFEYFI MAMIALNTVV LMMKFYDAPY EYELMLKCLN
1510 1520 1530 1540 1550
IVFTSMFSME CILKIIAFGV LNYFRDAWNV FDFVTVLGSI TDILVTEIAN
1560 1570 1580 1590 1600
NFINLSFLRL FRAARLIKLL RQGYTIRILL WTFVQSFKAL PYVCLLIAML
1610 1620 1630 1640 1650
FFIYAIIGMQ VFGNIALDDD TSINRHNNFR TFLQALMLLF RSATGEAWHE
1660 1670 1680 1690 1700
IMLSCLGNRA CDPHANASEC GSDFAYFYFV SFIFLCSFLM LNLFVAVIMD
1710 1720 1730 1740 1750
NFEYLTRDSS ILGPHHLDEF IRVWAEYDPA ACGRISYNDM FEMLKHMSPP
1760 1770 1780 1790 1800
LGLGKKCPAR VAYKRLVRMN MPISNEDMTV HFTSTLMALI RTALEIKLAP
1810 1820 1830 1840 1850
AGTKQHQCDA ELRKEISSVW ANLPQKTLDL LVPPHKPDEM TVGKVYAALM
1860 1870 1880 1890 1900
IFDFYKQNKT TRDQTHQAPG GLSQMGPVSL FHPLKATLEQ TQPAVLRGAR
1910 1920 1930 1940 1950
VFLRQKSATS LSNGGAIQTQ ESGIKESLSW GTQRTQDALY EARAPLERGH
1960 1970 1980 1990 2000
SAEIPVGQSG TLAVDVQMQN MTLRGPDGEP QPGLESQGRA ASMPRLAAET
2010 2020 2030 2040 2050
QPAPNASPMK RSISTLAPRP HGTQLCSTVL DRPPPSQASH HHHHRCHRRR
2060 2070 2080 2090 2100
DKKQRSLEKG PSLSVDPEGA PSTAAGPGLP HGEGSTACRR DRKQERGRSQ
2110 2120 2130 2140 2150
ERRQPSSSSS EKQRFYSCDR FGSREPPQLM PSLSSHPTSP TAALEPAPHP
2160 2170 2180 2190 2200
QGSGSVNGSP LMSTSGASTP GRGGRRQLPQ TPLTPRPSIT YKTANSSPVH
2210 2220 2230 2240 2250
FAEGQSGLPA FSPGRLSRGL SEHNALLQKE PLSQPLAPGS RIGSDPYLGQ
2260 2270 2280 2290 2300
RLDSEASAHT LPEDTLTFEE AVATNSGRSS RTSYVSSLTS QSHPLRRVPN
2310 2320
GYHCTLGLST GVRARHSYHH PDQDHWC
Length:2,327
Mass (Da):261,481
Last modified:June 1, 1998 - v1
Checksum:iAD42CDD38482895A
GO
Isoform NB2 (identifier: O55017-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     756-756: A → AFVKQTRGTVSRSSSVSSVNSP

Show »
Length:2,348
Mass (Da):263,674
Checksum:i16B0576EA8DCACC6
GO

Sequence cautioni

The sequence AAB60437 differs from that shown. Reason: Frameshift at positions 1924, 1934, 2121 and 2127.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti238A → G in AAB60437 (PubMed:8307146).Curated1
Sequence conflicti645N → I in AAB60437 (PubMed:8307146).Curated1
Sequence conflicti757 – 759RQQ → QE in AAB60437 (PubMed:8307146).Curated3
Sequence conflicti880A → P in AAB60437 (PubMed:8307146).Curated1
Sequence conflicti1128L → F in AAB60437 (PubMed:8307146).Curated1
Sequence conflicti1173K → E in AAB60437 (PubMed:8307146).Curated1
Sequence conflicti1185F → C in AAB60437 (PubMed:8307146).Curated1
Sequence conflicti1227 – 1230Missing in AAB60437 (PubMed:8307146).Curated4
Sequence conflicti1388F → L in AAB60437 (PubMed:8307146).Curated1
Sequence conflicti1549A → AET in AAB60437 (PubMed:8307146).Curated1
Sequence conflicti1615I → S in AAB60437 (PubMed:8307146).Curated1
Sequence conflicti1636L → I in AAB60437 (PubMed:8307146).Curated1
Sequence conflicti1657G → D in AAB60437 (PubMed:8307146).Curated1
Sequence conflicti1802 – 1837Missing in AAB60437 (PubMed:8307146).CuratedAdd BLAST36
Sequence conflicti1942A → G in AAB60437 (PubMed:8307146).Curated1
Sequence conflicti1949G → D in AAB60437 (PubMed:8307146).Curated1
Sequence conflicti1963A → L in AAB60437 (PubMed:8307146).Curated1
Sequence conflicti1979E → D in AAB60437 (PubMed:8307146).Curated1
Sequence conflicti1994P → L in AAB60437 (PubMed:8307146).Curated1
Sequence conflicti2021H → D in AAB60437 (PubMed:8307146).Curated1
Sequence conflicti2075A → AA in AAB60437 (PubMed:8307146).Curated1
Sequence conflicti2141T → A in AAB60437 (PubMed:8307146).Curated1
Sequence conflicti2168S → I in AAB60437 (PubMed:8307146).Curated1
Sequence conflicti2309S → N in AAB60437 (PubMed:8307146).Curated1
Sequence conflicti2313R → G in AAB60437 (PubMed:8307146).Curated1
Sequence conflicti2316H → A in AAB60437 (PubMed:8307146).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti414D → DA.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000883756A → AFVKQTRGTVSRSSSVSSVN SP in isoform NB2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF042317 mRNA. Translation: AAB97840.1.
U04999 mRNA. Translation: AAB60437.1. Frameshift.
CCDSiCCDS38065.1. [O55017-1]
PIRiS41080.
RefSeqiNP_001035993.1. NM_001042528.2. [O55017-1]
UniGeneiMm.4424.

Genome annotation databases

EnsembliENSMUST00000041342; ENSMUSP00000037416; ENSMUSG00000004113. [O55017-1]
GeneIDi12287.
KEGGimmu:12287.
UCSCiuc008ipe.2. mouse. [O55017-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF042317 mRNA. Translation: AAB97840.1.
U04999 mRNA. Translation: AAB60437.1. Frameshift.
CCDSiCCDS38065.1. [O55017-1]
PIRiS41080.
RefSeqiNP_001035993.1. NM_001042528.2. [O55017-1]
UniGeneiMm.4424.

3D structure databases

ProteinModelPortaliO55017.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198431. 5 interactors.
IntActiO55017. 2 interactors.
STRINGi10090.ENSMUSP00000037416.

Chemistry databases

ChEMBLiCHEMBL3637936.

Protein family/group databases

TCDBi1.A.1.11.9. the voltage-gated ion channel (vic) superfamily.

PTM databases

iPTMnetiO55017.
PhosphoSitePlusiO55017.

Proteomic databases

MaxQBiO55017.
PaxDbiO55017.
PRIDEiO55017.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000041342; ENSMUSP00000037416; ENSMUSG00000004113. [O55017-1]
GeneIDi12287.
KEGGimmu:12287.
UCSCiuc008ipe.2. mouse. [O55017-1]

Organism-specific databases

CTDi774.
MGIiMGI:88296. Cacna1b.

Phylogenomic databases

eggNOGiKOG2301. Eukaryota.
ENOG410XNP6. LUCA.
GeneTreeiENSGT00830000128247.
HOGENOMiHOG000231530.
HOVERGENiHBG050763.
InParanoidiO55017.
KOiK04849.
TreeFamiTF312805.

Enzyme and pathway databases

ReactomeiR-MMU-112308. Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels.

Miscellaneous databases

PROiO55017.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000004113.
ExpressionAtlasiO55017. baseline and differential.
GenevisibleiO55017. MM.

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_MOUSE
AccessioniPrimary (citable) accession number: O55017
Secondary accession number(s): Q60609
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: November 30, 2016
This is version 164 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.