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O55017

- CAC1B_MOUSE

UniProt

O55017 - CAC1B_MOUSE

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Protein

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

Gene

Cacna1b

Organism
Mus musculus (Mouse)
Status
Reviewed - 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
Sitei1358 – 13581Calcium ion selectivity and permeabilityBy similarity
Sitei1646 – 16461Calcium ion selectivity and permeabilityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi451 – 4588ATPSequence Analysis
Calcium bindingi1728 – 173912PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calcium ion binding Source: InterPro
  3. high voltage-gated calcium channel activity Source: RefGenome
  4. voltage-gated calcium channel activity Source: MGI

GO - Biological processi

  1. calcium ion import Source: RefGenome
  2. calcium ion transmembrane transport Source: MGI
  3. calcium ion transport Source: MGI
  4. locomotory behavior Source: MGI
  5. membrane depolarization during action potential Source: RefGenome
  6. neurotransmitter secretion Source: MGI
  7. regulation of blood pressure Source: MGI
  8. regulation of calcium ion transport Source: MGI
  9. regulation of heart contraction Source: MGI
  10. 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

ReactomeiREACT_225645. 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
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:88296. Cacna1b.

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 – 13319ExtracellularSequence AnalysisAdd
BLAST
Transmembranei134 – 15118Helical; Name=S2 of repeat ISequence AnalysisAdd
BLAST
Topological domaini152 – 16413CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei165 – 17915Helical; Name=S3 of repeat ISequence AnalysisAdd
BLAST
Topological domaini180 – 1867ExtracellularSequence Analysis
Transmembranei187 – 20519Helical; Name=S4 of repeat ISequence AnalysisAdd
BLAST
Topological domaini206 – 22520CytoplasmicSequence 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 – 482126CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei483 – 50220Helical; Name=S1 of repeat IISequence AnalysisAdd
BLAST
Topological domaini503 – 51614ExtracellularSequence AnalysisAdd
BLAST
Transmembranei517 – 53620Helical; Name=S2 of repeat IISequence AnalysisAdd
BLAST
Topological domaini537 – 5448CytoplasmicSequence Analysis
Transmembranei545 – 56319Helical; Name=S3 of repeat IISequence AnalysisAdd
BLAST
Topological domaini564 – 57411ExtracellularSequence AnalysisAdd
BLAST
Transmembranei575 – 59218Helical; Name=S4 of repeat IISequence AnalysisAdd
BLAST
Topological domaini593 – 61119CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei612 – 63120Helical; Name=S5 of repeat IISequence AnalysisAdd
BLAST
Topological domaini632 – 68453ExtracellularSequence AnalysisAdd
BLAST
Transmembranei685 – 70925Helical; Name=S6 of repeat IISequence AnalysisAdd
BLAST
Topological domaini710 – 1134425CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1135 – 115824Helical; Name=S1 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini1159 – 117517ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1176 – 119520Helical; Name=S2 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini1196 – 12038CytoplasmicSequence Analysis
Transmembranei1204 – 122623Helical; Name=S3 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini1227 – 124115ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1242 – 125615Helical; Name=S4 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini1257 – 127721CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1278 – 129720Helical; Name=S5 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini1298 – 138386ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1384 – 140825Helical; Name=S6 of repeat IIISequence AnalysisAdd
BLAST
Topological domaini1409 – 146557CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1466 – 148419Helical; Name=S1 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1485 – 149814ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1499 – 151820Helical; Name=S2 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1519 – 15279CytoplasmicSequence Analysis
Transmembranei1528 – 154619Helical; Name=S3 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1547 – 15548ExtracellularSequence Analysis
Transmembranei1555 – 157319Helical; Name=S4 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1574 – 159219CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1593 – 161220Helical; Name=S5 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1613 – 167462ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1675 – 169420Helical; Name=S6 of repeat IVSequence AnalysisAdd
BLAST
Topological domaini1695 – 2327633CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. dendrite Source: MGI
  2. membrane Source: MGI
  3. neuronal cell body Source: MGI
  4. voltage-gated calcium channel complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 23272327Voltage-dependent N-type calcium channel subunit alpha-1BPRO_0000053922Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi256 – 2561N-linked (GlcNAc...)Sequence Analysis
Modified residuei783 – 7831Phosphoserine1 Publication
Glycosylationi1554 – 15541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1666 – 16661N-linked (GlcNAc...)Sequence Analysis
Modified residuei1710 – 17101Phosphoserine; by PKASequence Analysis

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiO55017.
PaxDbiO55017.
PRIDEiO55017.

PTM databases

PhosphoSiteiO55017.

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

BgeeiO55017.
ExpressionAtlasiO55017. baseline and differential.
GenevestigatoriO55017.

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 and RIMBP2 (By similarity).By similarity

Protein-protein interaction databases

BioGridi198431. 6 interactions.
IntActiO55017. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliO55017.
SMRiO55017. Positions 97-407, 475-710, 1135-1410, 1466-1700.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati82 – 359278IAdd
BLAST
Repeati468 – 712245IIAdd
BLAST
Repeati1126 – 1412287IIIAdd
BLAST
Repeati1449 – 1702254IVAdd
BLAST
Domaini1715 – 175036EF-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 biasi2040 – 20445Poly-His
Compositional biasi2106 – 21105Poly-Ser

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

eggNOGiCOG1226.
GeneTreeiENSGT00760000118827.
HOGENOMiHOG000231530.
HOVERGENiHBG050763.
InParanoidiO55017.
KOiK04849.
TreeFamiTF312805.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR027359. Channel_four-helix_dom.
IPR002048. EF_hand_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005447. VDCC_N_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PfamiPF08763. Ca_chan_IQ. 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. Align

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 AAB60437.1 differs from that shown. Reason: Frameshift at positions 1924, 1934, 2121 and 2127. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti238 – 2381A → G in AAB60437. (PubMed:8307146)Curated
Sequence conflicti645 – 6451N → I in AAB60437. (PubMed:8307146)Curated
Sequence conflicti757 – 7593RQQ → QE in AAB60437. (PubMed:8307146)Curated
Sequence conflicti880 – 8801A → P in AAB60437. (PubMed:8307146)Curated
Sequence conflicti1128 – 11281L → F in AAB60437. (PubMed:8307146)Curated
Sequence conflicti1173 – 11731K → E in AAB60437. (PubMed:8307146)Curated
Sequence conflicti1185 – 11851F → C in AAB60437. (PubMed:8307146)Curated
Sequence conflicti1227 – 12304Missing in AAB60437. (PubMed:8307146)Curated
Sequence conflicti1388 – 13881F → L in AAB60437. (PubMed:8307146)Curated
Sequence conflicti1549 – 15491A → AET in AAB60437. (PubMed:8307146)Curated
Sequence conflicti1615 – 16151I → S in AAB60437. (PubMed:8307146)Curated
Sequence conflicti1636 – 16361L → I in AAB60437. (PubMed:8307146)Curated
Sequence conflicti1657 – 16571G → D in AAB60437. (PubMed:8307146)Curated
Sequence conflicti1802 – 183736Missing in AAB60437. (PubMed:8307146)CuratedAdd
BLAST
Sequence conflicti1942 – 19421A → G in AAB60437. (PubMed:8307146)Curated
Sequence conflicti1949 – 19491G → D in AAB60437. (PubMed:8307146)Curated
Sequence conflicti1963 – 19631A → L in AAB60437. (PubMed:8307146)Curated
Sequence conflicti1979 – 19791E → D in AAB60437. (PubMed:8307146)Curated
Sequence conflicti1994 – 19941P → L in AAB60437. (PubMed:8307146)Curated
Sequence conflicti2021 – 20211H → D in AAB60437. (PubMed:8307146)Curated
Sequence conflicti2075 – 20751A → AA in AAB60437. (PubMed:8307146)Curated
Sequence conflicti2141 – 21411T → A in AAB60437. (PubMed:8307146)Curated
Sequence conflicti2168 – 21681S → I in AAB60437. (PubMed:8307146)Curated
Sequence conflicti2309 – 23091S → N in AAB60437. (PubMed:8307146)Curated
Sequence conflicti2313 – 23131R → G in AAB60437. (PubMed:8307146)Curated
Sequence conflicti2316 – 23161H → A in AAB60437. (PubMed:8307146)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti414 – 4141D → DA.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei756 – 7561A → AFVKQTRGTVSRSSSVSSVN SP in isoform NB2. 1 PublicationVSP_000883

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.1. 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.
CCDSi CCDS38065.1. [O55017-1 ]
PIRi S41080.
RefSeqi NP_001035993.1. NM_001042528.2. [O55017-1 ]
UniGenei Mm.4424.

3D structure databases

ProteinModelPortali O55017.
SMRi O55017. Positions 97-407, 475-710, 1135-1410, 1466-1700.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198431. 6 interactions.
IntActi O55017. 1 interaction.

Protein family/group databases

TCDBi 1.A.1.11.9. the voltage-gated ion channel (vic) superfamily.

PTM databases

PhosphoSitei O55017.

Proteomic databases

MaxQBi O55017.
PaxDbi O55017.
PRIDEi O55017.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000041342 ; ENSMUSP00000037416 ; ENSMUSG00000004113 . [O55017-1 ]
GeneIDi 12287.
KEGGi mmu:12287.
UCSCi uc008ipe.1. mouse. [O55017-1 ]

Organism-specific databases

CTDi 774.
MGIi MGI:88296. Cacna1b.

Phylogenomic databases

eggNOGi COG1226.
GeneTreei ENSGT00760000118827.
HOGENOMi HOG000231530.
HOVERGENi HBG050763.
InParanoidi O55017.
KOi K04849.
TreeFami TF312805.

Enzyme and pathway databases

Reactomei REACT_225645. Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels.

Miscellaneous databases

NextBioi 280760.
PROi O55017.
SOURCEi Search...

Gene expression databases

Bgeei O55017.
ExpressionAtlasi O55017. baseline and differential.
Genevestigatori O55017.

Family and domain databases

Gene3Di 1.20.120.350. 4 hits.
InterProi IPR027359. Channel_four-helix_dom.
IPR002048. EF_hand_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005447. VDCC_N_a1su.
IPR002077. VDCCAlpha1.
[Graphical view ]
Pfami PF08763. Ca_chan_IQ. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view ]
PRINTSi PR00167. CACHANNEL.
PR01631. NVDCCALPHA1.
SMARTi SM01062. Ca_chan_IQ. 1 hit.
[Graphical view ]
PROSITEi PS50222. EF_HAND_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence polymorphism of mouse alpha1 B."
    Hong T., Birnbaumer L.
    Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
    Tissue: Brain.
  2. "Molecular cloning of a murine N-type calcium channel alpha 1 subunit. Evidence for isoforms, brain distribution, and chromosomal localization."
    Coppola T., Waldmann R., Borsotto M., Heurteaux C., Romey G., Mattei M.-G., Lazdunski M.
    FEBS Lett. 338:1-5(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS NB1 AND NB2).
    Tissue: Neuroblastoma.
  3. "Direct interaction of the Rab3 effector RIM with Ca2+ channels, SNAP-25, and synaptotagmin."
    Coppola T., Magnin-Luethi S., Perret-Menoud V., Gattesco S., Schiavo G., Regazzi R.
    J. Biol. Chem. 276:32756-32762(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RIMS1.
    Tissue: Brain.
  4. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  5. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.

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 26, 2014
This is version 146 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

External Data

Dasty 3