CAC1S_LITCT
ID CAC1S_LITCT Reviewed; 1688 AA.
AC O57483;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha-1S;
DE AltName: Full=FGalpha1S;
DE AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.1;
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=9738021; DOI=10.1074/jbc.273.39.25503;
RA Zhou J., Cribbs L., Yi J., Shirokov R., Perez-Reyes E., Rios E.;
RT "Molecular cloning and functional expression of a skeletal muscle
RT dihydropyridine receptor from Rana catesbeiana.";
RL J. Biol. Chem. 273:25503-25509(1998).
CC -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry
CC of calcium ions into excitable cells and are also involved in a variety
CC of calcium-dependent processes, including muscle contraction, gene
CC expression, cell motility, cell division and cell death. The isoform
CC alpha-1S gives rise to L-type calcium currents. Long-lasting (L-type)
CC calcium channels belong to the 'high-voltage activated' (HVA) group.
CC They are blocked by dihydropyridines (DHP), phenylalkylamines, and by
CC benzothiazepines. Calcium channels containing the alpha-1S subunit play
CC an important role in excitation-contraction coupling in skeletal muscle
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Multisubunit complex consisting of alpha-1, alpha-2, beta and
CC delta subunits in a 1:1:1:1 ratio. The channel activity is directed by
CC the pore-forming and voltage-sensitive alpha-1 subunit. In many cases,
CC this subunit is sufficient to generate voltage-sensitive calcium
CC channel activity. The auxiliary subunits beta and alpha-2/delta linked
CC by a disulfide bridge regulate the channel activity. An additional
CC gamma subunit is present only in skeletal muscle L-type channel (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Skeletal muscle specific.
CC -!- DOMAIN: Each of the four internal repeats contains five hydrophobic
CC transmembrane segments (S1, S2, S3, S5, S6) and one positively charged
CC transmembrane segment (S4). S4 segments probably represent the voltage-
CC sensor and are characterized by a series of positively charged amino
CC acids at every third position.
CC -!- PTM: Phosphorylation by PKA stimulates the calcium channel function.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. {ECO:0000305}.
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DR EMBL; AF037625; AAC36126.1; -; mRNA.
DR AlphaFoldDB; O57483; -.
DR SMR; O57483; -.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR031649; GPHH_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR014873; VDCC_a1su_IQ.
DR InterPro; IPR005450; VDCC_L_a1ssu.
DR InterPro; IPR005446; VDCC_L_a1su.
DR InterPro; IPR002077; VDCCAlpha1.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR Pfam; PF08763; Ca_chan_IQ; 1.
DR Pfam; PF16905; GPHH; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00167; CACHANNEL.
DR PRINTS; PR01630; LVDCCALPHA1.
DR PRINTS; PR01634; LVDCCALPHA1S.
DR SMART; SM01062; Ca_chan_IQ; 1.
PE 2: Evidence at transcript level;
KW Calcium; Calcium channel; Calcium transport; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Metal-binding; Phosphoprotein;
KW Repeat; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..1688
FT /note="Voltage-dependent L-type calcium channel subunit
FT alpha-1S"
FT /id="PRO_0000053949"
FT TOPO_DOM 1..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..70
FT /note="Helical; Name=S1 of repeat I"
FT TOPO_DOM 71..88
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..108
FT /note="Helical; Name=S2 of repeat I"
FT TOPO_DOM 109..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..139
FT /note="Helical; Name=S3 of repeat I"
FT TOPO_DOM 140..158
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..177
FT /note="Helical; Name=S4 of repeat I"
FT TOPO_DOM 178..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..216
FT /note="Helical; Name=S5 of repeat I"
FT TOPO_DOM 217..307
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..332
FT /note="Helical; Name=S6 of repeat I"
FT TOPO_DOM 333..431
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..450
FT /note="Helical; Name=S1 of repeat II"
FT TOPO_DOM 451..465
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..485
FT /note="Helical; Name=S2 of repeat II"
FT TOPO_DOM 486..493
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..512
FT /note="Helical; Name=S3 of repeat II"
FT TOPO_DOM 513..522
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 523..541
FT /note="Helical; Name=S4 of repeat II"
FT TOPO_DOM 542..560
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 561..580
FT /note="Helical; Name=S5 of repeat II"
FT TOPO_DOM 581..635
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 636..660
FT /note="Helical; Name=S6 of repeat II"
FT TOPO_DOM 661..797
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 798..816
FT /note="Helical; Name=S1 of repeat III"
FT TOPO_DOM 817..832
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 833..852
FT /note="Helical; Name=S2 of repeat III"
FT TOPO_DOM 853..864
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 865..883
FT /note="Helical; Name=S3 of repeat III"
FT TOPO_DOM 884..890
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 891..909
FT /note="Helical; Name=S4 of repeat III"
FT TOPO_DOM 910..928
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 929..948
FT /note="Helical; Name=S5 of repeat III"
FT TOPO_DOM 949..1038
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1039..1063
FT /note="Helical; Name=S6 of repeat III"
FT TOPO_DOM 1064..1116
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1117..1135
FT /note="Helical; Name=S1 of repeat IV"
FT TOPO_DOM 1136..1150
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1151..1170
FT /note="Helical; Name=S2 of repeat IV"
FT TOPO_DOM 1171..1178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1179..1197
FT /note="Helical; Name=S3 of repeat IV"
FT TOPO_DOM 1198..1218
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1219..1237
FT /note="Helical; Name=S4 of repeat IV"
FT TOPO_DOM 1238..1256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1257..1276
FT /note="Helical; Name=S5 of repeat IV"
FT TOPO_DOM 1277..1343
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1344..1368
FT /note="Helical; Name=S6 of repeat IV"
FT TOPO_DOM 1369..1688
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 38..335
FT /note="I"
FT REPEAT 417..663
FT /note="II"
FT REPEAT 784..1066
FT /note="III"
FT REPEAT 1103..1371
FT /note="IV"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..372
FT /note="Binding to the beta subunit"
FT /evidence="ECO:0000250"
FT REGION 672..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1075
FT /note="Dihydropyridine binding"
FT /evidence="ECO:0000250"
FT REGION 1324..1390
FT /note="Dihydropyridine binding"
FT /evidence="ECO:0000250"
FT REGION 1336..1379
FT /note="Phenylalkylamine binding"
FT /evidence="ECO:0000250"
FT REGION 1635..1664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1669..1688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1644..1664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 290
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT BINDING 613
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT BINDING 1012
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1688 AA; 192423 MW; 5BEA06B38823017A CRC64;
MDAMGSAAEE GTQKKKRRPL VPPPPRPPRA LFCLGLQNPF RKFCINIVEW KPFEMIILLT
IFANCVALAI FLPMPEDDTN STNSVLEKVE YIFLFIFTIE SFLKIVAYGF ILHTDAYLRN
GWNILDFTIV SVGVFSVLLE QISKLQGLPA PGKSSGFNVK ALRAFRVLRP LRLVSGVPSL
QVVLNSIIKA MIPLLHIALL VLFMIIIYAI VGLELFSGKM HKTCYFKDTD ITATVDNEKP
APCSSTGQGR QCSINGSECR GWWPGPNNGI THFDNFGFAM LTVYQCITME GWTEVLYWVN
DAIGNEWPWI YFVSLILLGS FFVLNLVLGV LSGEFTKERE KAKSRGAFQM LREQQAMDED
LRGYLDWITH AEVMDPDMEP RDGFSQLEEG GSETDSLYEI EGINKFIAFF RQWRLWHRLL
RRKSRDLVKS RFFYWLVIII ILLNTVIIAT EHHHQPDSLT KAQDIANEVL LALFTMEMIV
KIYALGFQSY FMSLFNRFDS FVVCTGLLEV MLVASDIMSP LGISVLRCIR LLRIFKITRY
WTSLNNLVAS LLNSVRSIAS LLLLLFLFMI IFALLGMQMF GGKFDFEDLE VRRSTFDTFP
QALITVFQIL TGEDWTAVMY NGIMAYGGPT YSGMSVCIYF IILFVCGNYI LLNVFLAIAV
DNLAEAENLT SAQKAKAEER KRKKLARANP DKTEEEKLLL AKKEQKAKGE GIPTTARLKI
DEFESNVNEI KDPYPSADFP GDDEEEEPEI PISPRPRPLA ELQLKEKAVP MPEASSFFIF
SPTNKIRVLC HRIINATTFT NFILLFILLS SISLAAEDPI QPESFRNKVL SKLDIVFTVI
FTTEIVLKMT AYGAFLHKGS FCRNSFNILD LSVVGVSLIS MGIESSAISV VKILRVLRVL
RPLRAINRAK GLKHVVQCLF VAIKTIGNIV LVTTLLQFMF SCIGVQLFKG KFYSCTDTTK
ITADECRGYF FVAKDGNPAH MEAVPRVWSH SDFHFDNVLS GMMSLFTIST FEGWPQLLYR
AIDSHAEDMG PIYNYRIEIA VFFIVYIILI AFFMMNIFVG FVIVTFQEQG EQEYKDCELD
KNQRQCVQYA LKARPLRRYI PKNPHQYKIW YVVTSSYFEY LMFFLITLNT ISLGMQHYGQ
TAEFSYMSDI LNVAFTGIFT VEMFLKLAAF KAKGYFGDPW NVFDFLIVIG SVIDVILSEI
DTPGIPATPG AEESSRISIT FFRLFRVLRL VKLLSRGEGV RTLLWTFIKS FQALPYVALL
IVMLFFIYAV IGMQVFGKIA LVDGTHINRN SNFQTFPQAV LLLFRCATGE AWQEILLACS
YGKLCDPMSD FQPGEEYTCG TSFAYFYFIS FYMLCAFLII NLFVAVIMDN FDYLTRDWSI
LGPHHLDEFK RIWAEYDPEA KGRIKHLDVV TLLRRIQPPL GFGKFCPHRV ACKRLVSMNM
PLNSDGTVTF NATLFSLVRT ALKIKTEGNF EQSNEELRMI IKKIWKRTSM KLLDQVIPPI
GDDEVTVGKF YAIFLIQEHF RKFKKRQEEY YGYRPKKNAN NVEIQAGLRT IEEEEGEGEL
QRAISGDLTP EEELERAMVE AAIEEGIYRR TGGLFGQEDS FHTGPVSPLH TITSQRPLRF
SEAGSEDLDS PVFLPEPVFF PPPRRNRNTN NSTISRGLDQ RLTTPDFERV QQSEEQWDTN
SSISQATN
