CAC1S_CHICK
ID CAC1S_CHICK Reviewed; 281 AA.
AC O42398;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha-1S;
DE AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.1;
DE Flags: Fragment;
GN Name=CACNA1S;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn; TISSUE=Intestinal epithelium;
RA Xu J., Norman A.W., Henry H.L., de Boland A.R., Zanello L.P.;
RT "Molecular characterization of an L-type calcium channel in chick
RT intestinal epithelia cells.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Pore-forming, alpha-1S subunit of the voltage-gated calcium
CC channel that gives rise to L-type calcium currents in skeletal muscle.
CC Calcium channels containing the alpha-1S subunit play an important role
CC in excitation-contraction coupling in skeletal muscle via their
CC interaction with RYR1, which triggers Ca(2+) release from the
CC sarcplasmic reticulum and ultimately results in muscle contraction.
CC Long-lasting (L-type) calcium channels belong to the 'high-voltage
CC activated' (HVA) group. {ECO:0000250|UniProtKB:P07293}.
CC -!- ACTIVITY REGULATION: Channel activity is blocked by dihydropyridines
CC (DHP), phenylalkylamines, and by benzothiazepines.
CC {ECO:0000250|UniProtKB:P07293, ECO:0000305}.
CC -!- SUBUNIT: Component of a calcium channel complex consisting of a pore-
CC forming alpha subunit (CACNA1S) and the ancillary subunits CACNB1 or
CC CACNB2, CACNG1 and CACNA2D1. The channel complex contains alpha, beta,
CC gamma and delta subunits in a 1:1:1:1 ratio, i.e. it contains either
CC CACNB1 or CACNB2 (By similarity). CACNA1S channel activity is modulated
CC by the auxiliary subunits (CACNB1 or CACNB2, CACNG1 and CACNA2D1).
CC Interacts with DYSF and JSRP1 (By similarity). Interacts with RYR1 (By
CC similarity). Interacts with CALM (By similarity).
CC {ECO:0000250|UniProtKB:P07293, ECO:0000250|UniProtKB:Q02789,
CC ECO:0000250|UniProtKB:Q13698}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma, T-tubule
CC {ECO:0000250|UniProtKB:P07293}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P07293}.
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. {ECO:0000250|UniProtKB:P07293}.
CC -!- DOMAIN: The loop between repeats II and III interacts with the
CC ryanodine receptor, and is therefore important for calcium release from
CC the endoplasmic reticulum necessary for muscle contraction.
CC {ECO:0000250|UniProtKB:P07293}.
CC -!- PTM: The alpha-1S subunit is found in two isoforms in the skeletal
CC muscle: a minor form of 212 kDa containing the complete amino acid
CC sequence, and a major form of 190 kDa derived from the full-length form
CC by post-translational proteolysis close to Phe-1690.
CC {ECO:0000250|UniProtKB:P07293}.
CC -!- PTM: Both the minor and major forms are phosphorylated in vitro by PKA.
CC Phosphorylation by PKA activates the calcium channel.
CC {ECO:0000250|UniProtKB:P07293}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. CACNA1S subfamily. {ECO:0000305}.
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DR EMBL; AF007877; AAB63206.1; -; mRNA.
DR AlphaFoldDB; O42398; -.
DR SMR; O42398; -.
DR STRING; 9031.ENSGALP00000001033; -.
DR VEuPathDB; HostDB:geneid_395985; -.
DR eggNOG; KOG2301; Eukaryota.
DR InParanoid; O42398; -.
DR OrthoDB; 172471at2759; -.
DR PhylomeDB; O42398; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:1990454; C:L-type voltage-gated calcium channel complex; ISS:UniProtKB.
DR GO; GO:0030315; C:T-tubule; ISS:UniProtKB.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0008331; F:high voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; ISS:UniProtKB.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0071313; P:cellular response to caffeine; ISS:UniProtKB.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.350; -; 1.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR002077; VDCCAlpha1.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR00167; CACHANNEL.
PE 2: Evidence at transcript level;
KW Calcium; Calcium channel; Calcium transport; Calmodulin-binding;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN <1..>281
FT /note="Voltage-dependent L-type calcium channel subunit
FT alpha-1S"
FT /id="PRO_0000053947"
FT TRANSMEM 59..80
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TRANSMEM 89..110
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TRANSMEM 121..140
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TRANSMEM 153..171
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT TRANSMEM 190..210
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT INTRAMEM 233..251
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT REPEAT <1..8
FT /note="III"
FT REPEAT 45..>281
FT /note="IV"
FT REGION <1..17
FT /note="Dihydropyridine binding"
FT /evidence="ECO:0000250"
FT REGION 258..>281
FT /note="Dihydropyridine binding"
FT /evidence="ECO:0000250"
FT REGION 270..>281
FT /note="Phenylalkylamine binding"
FT /evidence="ECO:0000250"
FT MOTIF 242..245
FT /note="Selectivity filter of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 259..273
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT NON_TER 1
FT NON_TER 281
SQ SEQUENCE 281 AA; 32729 MW; 46BE70FA44D9166B CRC64;
VGFVIVTFQE QGESEYKNCE LDKNQRQCVQ YALKARPLRR YIPKNPYQYQ IWYVVTSSYF
EYLMFFLIML NTICLGMQHY NQSAEMNHVS DILNVAFTVL FTLEMILKLM AFKAKGYFGD
PWNVFDFLIV IGSIIDVILS EIDDPDDNSR VSITFFRLFR VMRLVKLLSR GEGVRTLLWT
FIKSFQALPY VALLIVMLFF IYAVIGMQMF GKIAMVDGTQ INRNNNFQTF PQAVLLLFRC
ATGEAWQEIL LDCSYGKRCD PESDYAEGEE YTCGTGFAYF Y
