Primary Information | |
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BoMiProt ID | Bomi10501 |
Protein Name | Voltage-dependent L-type calcium channel subunit beta-1/CAB1/Calcium channel voltage-dependent subunit beta 1 |
Organism | Bos taurus |
Uniprot ID | Q9MZL7 |
Milk Fraction | Whey |
Aminoacid Length | 562 |
Molecular Weight | 61087 |
FASTA Sequence | Download |
Gene Name | CACNB1 |
Gene ID | 327703 |
Protein Existence Status | reviewed |
Secondary Information | |
Protein Function | Regulatory subunit of L type calcium channels.The β subunit contributes to voltage gated calcium channel function by increasing peak Ca2+ current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling α1 subunit membrane targeting |
PTMs | Phosphorylation on Ser and Thr |
Additional Comments | expressed at high levels in brain and skeletal muscle, and at much lower levels in spleen and heart.Absence of the β1 subunit results in failure of transport and insertion of the α1 subunit into the plasmalemmal membrane.Absence of the β1 subunit modifies the Ca2+ current, and eliminates excitation-contraction coupling in skeletal muscle. |
Linking IDs | Bomi10501 |
Bibliography | 1.Hogan K, Greg RG, Powers PA. Structure and alternative splicing of the gene encoding the human beta1 subunit of voltage dependent calcium channels. Neurosci Lett. 1999 Dec 24;277(2):111-4. doi: 10.1016/s0304-3940(99)00851-4. PMID: 10624822. 2.Freise, D., Held, B., Wissenbach, U., Pfeifer, A., Trost, C., Himmerkus, N., ... & Flockerzi, V. (2000). Absence of the γ subunit of the skeletal muscle dihydropyridine receptor increases L-type Ca2+ currents and alters channel inactivation properties. Journal of Biological Chemistry, 275(19), 14476-14481. |
Protein Function | Regulatory subunit of L type calcium channels.The β subunit contributes to voltage gated calcium channel function by increasing peak Ca2+ current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling α1 subunit membrane targeting |
PTMs | Phosphorylation on Ser and Thr |
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | >sp|Q9MZL7|CACB1_BOVIN Voltage-dependent L-type calcium channel subunit beta-1 OS=Bos taurus OX=9913 GN=CACNB1 PE=1 SV=1 MVQKTSMSRGPYPSSQEIPMEVFDPSPQGKYSKRKGRFKRSDGS*44TSS*47DTTSNSFVRQGSA ESYTSRPSDSDVS*73LEEDREALRKEAERQALAQLEKAKTKPVAFAVRTNVGYNPSPGDEVP VQGVAITFEPKDFLHIKEKYNNDWWIGRLVKEGCEVGFIPSPVKLDSLRLLQEQKLRQNR LSSSKS*186GDNSSSS*193LGDVVTGTRRPTPPASAKQKQKSTEHVPPYDVVPSMRPIILVGPSLK GYEVTDMMQKALFDFLKHRFDGRISITRVTADISLAKRSVLNNPSKHIIIERSNTRSSLA EVQSEIERIFELARTLQLVALDADTINHPAQLSKTSLAPIIVYIKITSPKVLQRLIKSRG KSQSKHLNVQIAASEKLAQCPPEMFDIILDENQLEDACEHLAEYLEAYWKATHPPSSTPP NPLLNRTMATAALAASPAPVSNLQGPYLASGDQSLERATGEHASVHEYPGELGQPPGLYP SSHPPGRAGTLRALSRQDT*493FDADTPGNRNSAYTELGDSCVDMETDPSEGPGLGDPAGGST PPARQGS*547WEDEEEDYEEELTDNRNRGRNKARYCAEGGGPVLGRNKNELEGWGRGVYIR |
Predicted Disorder Regions | 30-78, 95-98, 183-214, 359-367, 431-458, 511-514, 531-563 |
DisProt Annotation | |
TM Helix Prediction | No TM helices |
Additional Comments | expressed at high levels in brain and skeletal muscle, and at much lower levels in spleen and heart.Absence of the β1 subunit results in failure of transport and insertion of the α1 subunit into the plasmalemmal membrane.Absence of the β1 subunit modifies the Ca2+ current, and eliminates excitation-contraction coupling in skeletal muscle. |
Linking IDs | |
Bibliography | 1.Hogan K, Greg RG, Powers PA. Structure and alternative splicing of the gene encoding the human beta1 subunit of voltage dependent calcium channels. Neurosci Lett. 1999 Dec 24;277(2):111-4. doi: 10.1016/s0304-3940(99)00851-4. PMID: 10624822. 2.Freise, D., Held, B., Wissenbach, U., Pfeifer, A., Trost, C., Himmerkus, N., ... & Flockerzi, V. (2000). Absence of the γ subunit of the skeletal muscle dihydropyridine receptor increases L-type Ca2+ currents and alters channel inactivation properties. Journal of Biological Chemistry, 275(19), 14476-14481. |