CAC1S_RABIT
ID CAC1S_RABIT Reviewed; 1873 AA.
AC P07293;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha-1S;
DE AltName: Full=Calcium channel, L type, alpha-1 polypeptide, isoform 3, skeletal muscle;
DE AltName: Full=Dihydropyridine receptor alpha-1S subunit {ECO:0000303|PubMed:15201141, ECO:0000303|PubMed:1660150, ECO:0000303|PubMed:25667046};
DE Short=DHPR {ECO:0000303|PubMed:10388749, ECO:0000303|PubMed:25667046};
DE AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.1;
GN Name=CACNA1S; Synonyms=CACH1, CACNL1A3;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY,
RP DIHYDROPYRIDINE BINDING, SUBUNIT, AND SUBCELLULAR LOCATION.
RC TISSUE=Skeletal muscle;
RX PubMed=3037387; DOI=10.1038/328313a0;
RA Tanabe T., Takeshima H., Mikami A., Flockerzi V., Takahashi H., Kangawa K.,
RA Kojima M., Matsuo H., Hirose T., Numa S.;
RT "Primary structure of the receptor for calcium channel blockers from
RT skeletal muscle.";
RL Nature 328:313-318(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=2458626; DOI=10.1126/science.2458626;
RA Ellis S.B., Williams M.E., Ways N.R., Brenner R., Sharp A.H., Leung A.T.,
RA Campbell K.P., McKenna E., Koch W.J., Hui A., Schwartz A., Harpold M.M.;
RT "Sequence and expression of mRNAs encoding the alpha 1 and alpha 2 subunits
RT of a DHP-sensitive calcium channel.";
RL Science 241:1661-1664(1988).
RN [3]
RP BETA-SUBUNIT BINDING DOMAIN, AND INTERACTION WITH CACNB1.
RX PubMed=7509046; DOI=10.1038/368067a0;
RA Pragnell M., de Waard M., Mori Y., Tanabe T., Snutch T.P., Campbell K.P.;
RT "Calcium channel beta-subunit binds to a conserved motif in the I-II
RT cytoplasmic linker of the alpha 1-subunit.";
RL Nature 368:67-70(1994).
RN [4]
RP PHENYLALKYLAMINE-BINDING REGION.
RX PubMed=2174553; DOI=10.1073/pnas.87.23.9108;
RA Striessnig J., Glossmann H., Catterall W.A.;
RT "Identification of a phenylalkylamine binding region within the alpha 1
RT subunit of skeletal muscle Ca2+ channels.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:9108-9112(1990).
RN [5]
RP DIHYDROPYRIDINE-BINDING REGION.
RX PubMed=1656465; DOI=10.1073/pnas.88.20.9203;
RA Nakayama H., Taki M., Striessnig J., Glossmann H., Catterall W.A.,
RA Kanaoka Y.;
RT "Identification of 1,4-dihydropyridine binding regions within the alpha 1
RT subunit of skeletal muscle Ca2+ channels by photoaffinity labeling with
RT diazipine.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:9203-9207(1991).
RN [6]
RP DIHYDROPYRIDINE-BINDING REGION.
RX PubMed=1660150; DOI=10.1073/pnas.88.23.10769;
RA Striessnig J., Murphy B.J., Catterall W.A.;
RT "Dihydropyridine receptor of L-type Ca2+ channels: identification of
RT binding domains for [3H](+)-PN200-110 and [3H]azidopine within the alpha 1
RT subunit.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:10769-10773(1991).
RN [7]
RP PHOSPHORYLATION AT SER-687 AND SER-1617.
RX PubMed=2844809; DOI=10.1016/s0021-9258(19)37591-x;
RA Roehrkasten A., Meyer H.E., Nastainczyk W., Sieber M., Hofmann F.;
RT "CAMP-dependent protein kinase rapidly phosphorylates serine-687 of the
RT skeletal muscle receptor for calcium channel blockers.";
RL J. Biol. Chem. 263:15325-15329(1988).
RN [8]
RP PHOSPHORYLATION BY PKA.
RX PubMed=2549550; DOI=10.1073/pnas.86.17.6816;
RA Nunoki K., Florio V., Catterall W.A.;
RT "Activation of purified calcium channels by stoichiometric protein
RT phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:6816-6820(1989).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9465115; DOI=10.1073/pnas.95.4.1903;
RA Grabner M., Dirksen R.T., Beam K.G.;
RT "Tagging with green fluorescent protein reveals a distinct subcellular
RT distribution of L-type and non-L-type Ca2+ channels expressed in dysgenic
RT myotubes.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:1903-1908(1998).
RN [10]
RP INTERACTION WITH RYR1, AND DOMAIN.
RX PubMed=10388749; DOI=10.1016/s0006-3495(99)76881-5;
RA Dulhunty A.F., Laver D.R., Gallant E.M., Casarotto M.G., Pace S.M.,
RA Curtis S.;
RT "Activation and inhibition of skeletal RyR channels by a part of the
RT skeletal DHPR II-III loop: effects of DHPR Ser687 and FKBP12.";
RL Biophys. J. 77:189-203(1999).
RN [11]
RP FUNCTION, MUTAGENESIS OF ARG-1086, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=15201141; DOI=10.1152/ajpcell.00173.2004;
RA Weiss R.G., O'Connell K.M., Flucher B.E., Allen P.D., Grabner M.,
RA Dirksen R.T.;
RT "Functional analysis of the R1086H malignant hyperthermia mutation in the
RT DHPR reveals an unexpected influence of the III-IV loop on skeletal muscle
RT EC coupling.";
RL Am. J. Physiol. 287:C1094-C1102(2004).
RN [12]
RP PHOSPHORYLATION AT SER-1575 AND THR-1579.
RX PubMed=20937870; DOI=10.1073/pnas.1012384107;
RA Emrick M.A., Sadilek M., Konoki K., Catterall W.A.;
RT "Beta-adrenergic-regulated phosphorylation of the skeletal muscle Ca(V)1.1
RT channel in the fight-or-flight response.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:18712-18717(2010).
RN [13]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=25548159; DOI=10.1073/pnas.1423113112;
RA Polster A., Perni S., Bichraoui H., Beam K.G.;
RT "Stac adaptor proteins regulate trafficking and function of muscle and
RT neuronal L-type Ca2+ channels.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:602-606(2015).
RN [14]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=27621462; DOI=10.1073/pnas.1612441113;
RA Polster A., Nelson B.R., Olson E.N., Beam K.G.;
RT "Stac3 has a direct role in skeletal muscle-type excitation-contraction
RT coupling that is disrupted by a myopathy-causing mutation.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:10986-10991(2016).
RN [15]
RP FUNCTION, SUBUNIT, INTERACTION WITH STAC; STAC1 AND STAC2, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF 752-ILE-PRO-753; 756-PRO--PRO-758 AND ARG-757.
RX PubMed=29078335; DOI=10.1073/pnas.1708852114;
RA Wong King Yuen S.M., Campiglio M., Tung C.C., Flucher B.E., Van Petegem F.;
RT "Structural insights into binding of STAC proteins to voltage-gated calcium
RT channels.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E9520-E9528(2017).
RN [16]
RP INTERACTION WITH STAC; STAC2 AND STAC3, AND SUBCELLULAR LOCATION.
RX PubMed=28112192; DOI=10.1038/srep41003;
RA Campiglio M., Flucher B.E.;
RT "STAC3 stably interacts through its C1 domain with CaV1.1 in skeletal
RT muscle triads.";
RL Sci. Rep. 7:41003-41003(2017).
RN [17]
RP FUNCTION, INTERACTION WITH STAC; STAC2 AND STAC3, AND SUBCELLULAR LOCATION.
RX PubMed=29467163; DOI=10.1085/jgp.201711917;
RA Polster A., Nelson B.R., Papadopoulos S., Olson E.N., Beam K.G.;
RT "STAC proteins associate with the critical domain for excitation-
RT contraction coupling in the II-III loop of CaV1.1.";
RL J. Gen. Physiol. 150:613-624(2018).
RN [18]
RP STRUCTURE BY NMR OF 671-690, AND DOMAIN.
RX PubMed=10766780; DOI=10.1074/jbc.275.16.11631;
RA Casarotto M.G., Gibson F., Pace S.M., Curtis S.M., Mulcair M.,
RA Dulhunty A.F.;
RT "A structural requirement for activation of skeletal ryanodine receptors by
RT peptides of the dihydropyridine receptor II-III loop.";
RL J. Biol. Chem. 275:11631-11637(2000).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 34-415 IN COMPLEX WITH CACNB2, AND
RP SUBUNIT.
RX PubMed=15134636; DOI=10.1016/s0896-6273(04)00250-8;
RA Opatowsky Y., Chen C.-C., Campbell K.P., Hirsch J.A.;
RT "Structural analysis of the voltage-dependent calcium channel beta subunit
RT functional core and its complex with the alpha1 interaction domain.";
RL Neuron 42:387-399(2004).
RN [20]
RP STRUCTURE BY ELECTRON MICROSCOPY (15 ANGSTROMS), SUBUNIT, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, AND TOPOLOGY.
RC TISSUE=Skeletal muscle {ECO:0000303|PubMed:25667046};
RX PubMed=25667046; DOI=10.1038/srep08370;
RA Hu H., Wang Z., Wei R., Fan G., Wang Q., Zhang K., Yin C.C.;
RT "The molecular architecture of dihydropyrindine receptor/L-type Ca2+
RT channel complex.";
RL Sci. Rep. 5:8370-8370(2015).
RN [21] {ECO:0007744|PDB:3JBR}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS) IN COMPLEX WITH CACNG1;
RP CACNB2 AND CACNA2D1, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE
RP SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, AND DOMAIN.
RC TISSUE=Skeletal muscle {ECO:0000303|PubMed:26680202};
RX PubMed=26680202; DOI=10.1126/science.aad2395;
RA Wu J., Yan Z., Li Z., Yan C., Lu S., Dong M., Yan N.;
RT "Structure of the voltage-gated calcium channel Cav1.1 complex.";
RL Science 350:2395-2395(2015).
RN [22] {ECO:0007744|PDB:5GJV, ECO:0007744|PDB:5GJW}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) IN COMPLEX WITH CALCIUM;
RP CACNB1; CACNG1 AND CACNA2D1, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY,
RP TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, DOMAIN, DISULFIDE
RP BONDS, AND GLYCOSYLATION AT ASN-257.
RC TISSUE=Skeletal muscle {ECO:0000303|PubMed:27580036};
RX PubMed=27580036; DOI=10.1038/nature19321;
RA Wu J., Yan Z., Li Z., Qian X., Lu S., Dong M., Zhou Q., Yan N.;
RT "Structure of the voltage-gated calcium channel Ca(v)1.1 at 3.6A
RT resolution.";
RL Nature 537:191-196(2016).
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 (PubMed:9465115, PubMed:15201141, PubMed:25548159, PubMed:27621462,
CC PubMed:29078335, PubMed:29467163). Calcium channels containing the
CC alpha-1S subunit play an important role in excitation-contraction
CC coupling in skeletal muscle via their interaction with RYR1, which
CC triggers Ca(2+) release from the sarcplasmic reticulum and ultimately
CC results in muscle contraction (PubMed:9465115 PubMed:15201141,
CC PubMed:27621462). Long-lasting (L-type) calcium channels belong to the
CC 'high-voltage activated' (HVA) group. {ECO:0000269|PubMed:15201141,
CC ECO:0000269|PubMed:25548159, ECO:0000269|PubMed:27621462,
CC ECO:0000269|PubMed:29078335, ECO:0000269|PubMed:29467163,
CC ECO:0000269|PubMed:9465115, ECO:0000305}.
CC -!- ACTIVITY REGULATION: Channel activity is blocked by dihydropyridines
CC (DHP), phenylalkylamines, and by benzothiazepines.
CC {ECO:0000305|PubMed:1656465, ECO:0000305|PubMed:1660150,
CC ECO:0000305|PubMed:2174553, ECO:0000305|PubMed:3037387}.
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 (PubMed:3037387, PubMed:27621462,
CC PubMed:15134636, PubMed:25667046, PubMed:26680202, PubMed:27580036).
CC The channel complex contains alpha, beta, gamma and delta subunits in a
CC 1:1:1:1 ratio, i.e. it contains either CACNB1 or CACNB2
CC (PubMed:15134636, PubMed:25667046, PubMed:26680202, PubMed:27580036).
CC CACNA1S channel activity is modulated by the auxiliary subunits (CACNB1
CC or CACNB2, CACNG1 and CACNA2D1). Interacts with DYSF and JSRP1 (By
CC similarity). Interacts with RYR1 (PubMed:10388749). Interacts with
CC STAC, STAC2 and STAC3 (via their SH3 domains) (PubMed:28112192,
CC PubMed:29078335, PubMed:29467163). Interaction with STAC3 promotes
CC expression at the cell membrane (PubMed:25548159, PubMed:29467163).
CC Interaction with STAC2 promotes expression at the cell membrane, but
CC with much lower efficiency than STAC3. Interaction with STAC1 leads to
CC very low levels expression at the cell membrane, much less than the
CC levels observed upon interaction with STAC3 and STAC2
CC (PubMed:29467163). Interacts with CALM (By similarity).
CC {ECO:0000250|UniProtKB:Q02789, ECO:0000250|UniProtKB:Q13698,
CC ECO:0000269|PubMed:10388749, ECO:0000269|PubMed:15134636,
CC ECO:0000269|PubMed:25548159, ECO:0000269|PubMed:25667046,
CC ECO:0000269|PubMed:26680202, ECO:0000269|PubMed:27580036,
CC ECO:0000269|PubMed:27621462, ECO:0000269|PubMed:28112192,
CC ECO:0000269|PubMed:29078335, ECO:0000269|PubMed:29467163,
CC ECO:0000269|PubMed:3037387}.
CC -!- INTERACTION:
CC P07293; P13806: CACNA2D1; NbExp=3; IntAct=EBI-8613624, EBI-9683767;
CC P07293; P19517: CACNB1; NbExp=4; IntAct=EBI-8613624, EBI-978604;
CC P07293; P19518: CACNG1; NbExp=3; IntAct=EBI-8613624, EBI-9683808;
CC P07293; Q96RG2: PASK; Xeno; NbExp=2; IntAct=EBI-8613624, EBI-1042651;
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma, T-tubule
CC {ECO:0000269|PubMed:15201141, ECO:0000269|PubMed:25548159,
CC ECO:0000269|PubMed:25667046, ECO:0000269|PubMed:26680202,
CC ECO:0000269|PubMed:27580036, ECO:0000269|PubMed:27621462,
CC ECO:0000269|PubMed:28112192, ECO:0000269|PubMed:29078335,
CC ECO:0000269|PubMed:29467163, ECO:0000269|PubMed:9465115,
CC ECO:0000305|PubMed:3037387}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:25667046, ECO:0000269|PubMed:26680202,
CC ECO:0000269|PubMed:27580036, ECO:0000305|PubMed:3037387}.
CC -!- TISSUE SPECIFICITY: Detected in skeletal muscle T-tubules (at protein
CC level). {ECO:0000269|PubMed:25667046, ECO:0000269|PubMed:26680202,
CC ECO:0000269|PubMed:27580036, ECO:0000269|PubMed:3037387}.
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:0000269|PubMed:26680202,
CC ECO:0000269|PubMed:27580036}.
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:0000305|PubMed:10388749, ECO:0000305|PubMed:10766780,
CC ECO:0000305|PubMed:15201141}.
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:0000305|PubMed:3037387}.
CC -!- PTM: Phosphorylated. Phosphorylation by PKA activates the calcium
CC channel. Both the minor and major forms are phosphorylated in vitro by
CC PKA (PubMed:2549550, PubMed:2844809). Phosphorylation at Ser-1575 is
CC involved in beta-adrenergic-mediated regulation of the channel
CC (PubMed:20937870). {ECO:0000269|PubMed:20937870,
CC ECO:0000269|PubMed:2549550, ECO:0000269|PubMed:2844809}.
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; X05921; CAA29355.1; -; mRNA.
DR EMBL; M23919; AAA31159.1; -; mRNA.
DR PIR; A30063; A30063.
DR RefSeq; NP_001095190.1; NM_001101720.1.
DR PDB; 1DU1; NMR; -; A=671-690.
DR PDB; 1JZP; NMR; -; A=671-690.
DR PDB; 1T3L; X-ray; 2.20 A; B=357-374.
DR PDB; 3JBR; EM; 4.20 A; A=1-1873.
DR PDB; 5GJV; EM; 3.60 A; A=1-1873.
DR PDB; 5GJW; EM; 3.90 A; A=1-1873.
DR PDB; 6BYO; EM; 3.60 A; A=32-1388.
DR PDB; 6JP5; EM; 2.90 A; A=1-1873.
DR PDB; 6JP8; EM; 2.70 A; A=1-1873.
DR PDB; 6JPA; EM; 2.60 A; A=1-1506.
DR PDB; 6JPB; EM; 2.90 A; A=1-1873.
DR PDB; 7JPK; EM; 3.00 A; A=1-1873.
DR PDB; 7JPL; EM; 3.40 A; A=1-1873.
DR PDB; 7JPV; EM; 3.40 A; A=1-1873.
DR PDB; 7JPW; EM; 3.20 A; A=1-1873.
DR PDB; 7JPX; EM; 2.90 A; A=1-1873.
DR PDB; 7RXQ; X-ray; 2.03 A; B=1594-1609.
DR PDBsum; 1DU1; -.
DR PDBsum; 1JZP; -.
DR PDBsum; 1T3L; -.
DR PDBsum; 3JBR; -.
DR PDBsum; 5GJV; -.
DR PDBsum; 5GJW; -.
DR PDBsum; 6BYO; -.
DR PDBsum; 6JP5; -.
DR PDBsum; 6JP8; -.
DR PDBsum; 6JPA; -.
DR PDBsum; 6JPB; -.
DR PDBsum; 7JPK; -.
DR PDBsum; 7JPL; -.
DR PDBsum; 7JPV; -.
DR PDBsum; 7JPW; -.
DR PDBsum; 7JPX; -.
DR PDBsum; 7RXQ; -.
DR AlphaFoldDB; P07293; -.
DR BMRB; P07293; -.
DR SMR; P07293; -.
DR BioGRID; 1172604; 1.
DR ComplexPortal; CPX-3189; Skeletal muscle VGCC complex.
DR DIP; DIP-61879N; -.
DR IntAct; P07293; 4.
DR MINT; P07293; -.
DR STRING; 9986.ENSOCUP00000003147; -.
DR ChEMBL; CHEMBL4169; -.
DR TCDB; 1.A.1.11.2; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; P07293; -.
DR SwissPalm; P07293; -.
DR PRIDE; P07293; -.
DR GeneID; 100009585; -.
DR KEGG; ocu:100009585; -.
DR CTD; 779; -.
DR eggNOG; KOG2301; Eukaryota.
DR InParanoid; P07293; -.
DR OrthoDB; 172471at2759; -.
DR EvolutionaryTrace; P07293; -.
DR PRO; PR:P07293; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:1990454; C:L-type voltage-gated calcium channel complex; IDA:UniProtKB.
DR GO; GO:0030315; C:T-tubule; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:CAFA.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0071313; P:cellular response to caffeine; IDA:UniProtKB.
DR GO; GO:0045933; P:positive regulation of muscle contraction; IC:ComplexPortal.
DR GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IMP:CAFA.
DR DisProt; DP00228; -.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR031688; CAC1F_C.
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; PF16885; CAC1F_C; 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 1: Evidence at protein level;
KW 3D-structure; Calcium; Calcium channel; Calcium transport;
KW Calmodulin-binding; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..1873
FT /note="Voltage-dependent L-type calcium channel subunit
FT alpha-1S"
FT /id="PRO_0000053945"
FT TOPO_DOM 1..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TRANSMEM 52..70
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TOPO_DOM 71..85
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TRANSMEM 86..106
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TOPO_DOM 107..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TRANSMEM 116..136
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TOPO_DOM 137..160
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TRANSMEM 161..179
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TOPO_DOM 180..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TRANSMEM 197..218
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TOPO_DOM 219..279
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27580036"
FT INTRAMEM 280..301
FT /note="Pore-forming"
FT /evidence="ECO:0000269|PubMed:26680202,
FT ECO:0000269|PubMed:27580036"
FT TOPO_DOM 302..309
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TRANSMEM 310..330
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TOPO_DOM 331..432
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TRANSMEM 433..451
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TOPO_DOM 452..462
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TRANSMEM 463..483
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TOPO_DOM 484..494
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TRANSMEM 495..514
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TOPO_DOM 515..523
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TRANSMEM 524..542
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TOPO_DOM 543..561
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TRANSMEM 562..581
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TOPO_DOM 582..601
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27580036"
FT INTRAMEM 602..623
FT /note="Pore-forming"
FT /evidence="ECO:0000269|PubMed:26680202,
FT ECO:0000269|PubMed:27580036"
FT TOPO_DOM 624..633
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TRANSMEM 634..653
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TOPO_DOM 654..799
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TRANSMEM 800..818
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TOPO_DOM 819..830
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TRANSMEM 831..850
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TOPO_DOM 851..866
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TRANSMEM 867..885
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TOPO_DOM 886..892
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TRANSMEM 893..911
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TOPO_DOM 912..930
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TRANSMEM 931..950
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TOPO_DOM 951..1000
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27580036"
FT INTRAMEM 1001..1021
FT /note="Pore-forming"
FT /evidence="ECO:0000269|PubMed:26680202,
FT ECO:0000269|PubMed:27580036"
FT TOPO_DOM 1022..1038
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TRANSMEM 1039..1060
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TOPO_DOM 1061..1118
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TRANSMEM 1119..1140
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TOPO_DOM 1141..1148
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TRANSMEM 1149..1170
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TOPO_DOM 1171..1180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TRANSMEM 1181..1200
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TOPO_DOM 1201..1231
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TRANSMEM 1232..1250
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TOPO_DOM 1251..1268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TRANSMEM 1269..1289
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TOPO_DOM 1290..1311
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27580036"
FT INTRAMEM 1312..1330
FT /note="Pore-forming"
FT /evidence="ECO:0000269|PubMed:26680202,
FT ECO:0000269|PubMed:27580036"
FT TOPO_DOM 1331..1356
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TRANSMEM 1357..1381
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000269|PubMed:27580036"
FT TOPO_DOM 1382..1873
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27580036"
FT REPEAT 38..337
FT /note="I"
FT /evidence="ECO:0000305"
FT REPEAT 418..664
FT /note="II"
FT /evidence="ECO:0000305"
FT REPEAT 786..1068
FT /note="III"
FT /evidence="ECO:0000305"
FT REPEAT 1105..1384
FT /note="IV"
FT /evidence="ECO:0000305"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..374
FT /note="Binding to the beta subunit"
FT /evidence="ECO:0000269|PubMed:27580036"
FT REGION 673..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..760
FT /note="Interaction with STAC, STAC2 and STAC3 (via SH3
FT domains)"
FT /evidence="ECO:0000269|PubMed:29078335"
FT REGION 988..1077
FT /note="Dihydropyridine binding"
FT /evidence="ECO:0000269|PubMed:1656465,
FT ECO:0000269|PubMed:1660150"
FT REGION 1337..1403
FT /note="Dihydropyridine binding"
FT /evidence="ECO:0000269|PubMed:1656465"
FT REGION 1349..1391
FT /note="Phenylalkylamine binding"
FT /evidence="ECO:0000269|PubMed:2174553"
FT REGION 1522..1542
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000250|UniProtKB:Q13698"
FT REGION 1689..1782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1841..1873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 290..293
FT /note="Selectivity filter of repeat I"
FT /evidence="ECO:0000305|PubMed:26680202,
FT ECO:0000305|PubMed:27580036"
FT MOTIF 612..615
FT /note="Selectivity filter of repeat II"
FT /evidence="ECO:0000305|PubMed:26680202,
FT ECO:0000305|PubMed:27580036"
FT MOTIF 1012..1015
FT /note="Selectivity filter of repeat III"
FT /evidence="ECO:0000305|PubMed:26680202,
FT ECO:0000305|PubMed:27580036"
FT MOTIF 1321..1324
FT /note="Selectivity filter of repeat IV"
FT /evidence="ECO:0000305|PubMed:26680202,
FT ECO:0000305|PubMed:27580036"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1746..1778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1843..1867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:27580036,
FT ECO:0007744|PDB:5GJV"
FT BINDING 614
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:27580036,
FT ECO:0007744|PDB:5GJV"
FT BINDING 1014
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:27580036,
FT ECO:0007744|PDB:5GJV"
FT SITE 1690..1691
FT /note="Cleavage"
FT /evidence="ECO:0000305"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02789"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02789"
FT MOD_RES 687
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000305|PubMed:2844809"
FT MOD_RES 1575
FT /note="Phosphoserine; by PKA and CAMK2"
FT /evidence="ECO:0000305|PubMed:20937870"
FT MOD_RES 1579
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000305|PubMed:20937870"
FT MOD_RES 1617
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000305|PubMed:2844809"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PDB:5GJV"
FT DISULFID 226..254
FT /evidence="ECO:0000269|PubMed:27580036,
FT ECO:0007744|PDB:5GJV, ECO:0007744|PDB:5GJW"
FT DISULFID 245..261
FT /evidence="ECO:0000269|PubMed:27580036,
FT ECO:0007744|PDB:5GJV, ECO:0007744|PDB:5GJW"
FT DISULFID 957..968
FT /evidence="ECO:0000269|PubMed:27580036,
FT ECO:0007744|PDB:5GJV, ECO:0007744|PDB:5GJW"
FT DISULFID 1338..1352
FT /evidence="ECO:0000269|PubMed:27580036,
FT ECO:0007744|PDB:5GJV, ECO:0007744|PDB:5GJW"
FT VARIANT 165
FT /note="R -> K"
FT VARIANT 258
FT /note="G -> D"
FT VARIANT 1870
FT /note="P -> L"
FT MUTAGEN 752..753
FT /note="IP->AA: Loss of interaction with STAC2 and STAC3 and
FT strongly decreased channel activity; when associated with
FT A-757."
FT /evidence="ECO:0000269|PubMed:29078335"
FT MUTAGEN 756..758
FT /note="PRP->ARA: Loss of interaction with STAC3."
FT /evidence="ECO:0000269|PubMed:29078335"
FT MUTAGEN 757
FT /note="R->A: Loss of interaction with STAC2 and STAC3 and
FT strongly decreased channel activity; when associated with
FT 752-AA-753."
FT /evidence="ECO:0000269|PubMed:29078335"
FT MUTAGEN 1086
FT /note="R->H: Shifts the threshold potential to more
FT negative values and lowers the concentration threshold for
FT channel activation by caffeine."
FT /evidence="ECO:0000269|PubMed:15201141"
FT CONFLICT 694
FT /note="T -> R (in Ref. 2; AAA31159)"
FT /evidence="ECO:0000305"
FT CONFLICT 1808
FT /note="T -> M (in Ref. 2; AAA31159)"
FT /evidence="ECO:0000305"
FT CONFLICT 1815
FT /note="A -> V (in Ref. 2; AAA31159)"
FT /evidence="ECO:0000305"
FT CONFLICT 1835
FT /note="A -> E (in Ref. 2; AAA31159)"
FT /evidence="ECO:0000305"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:6JP8"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 53..68
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 81..100
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 111..119
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 121..143
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 174..178
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 180..192
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 197..218
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:6JPA"
FT TURN 268..271
FT /evidence="ECO:0007829|PDB:6JP8"
FT HELIX 278..289
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 294..305
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:6JP8"
FT HELIX 310..319
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 321..345
FT /evidence="ECO:0007829|PDB:6JPA"
FT TURN 346..349
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 359..372
FT /evidence="ECO:0007829|PDB:1T3L"
FT HELIX 421..429
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:6JP8"
FT HELIX 434..437
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 439..451
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 458..485
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 488..493
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 495..516
FT /evidence="ECO:0007829|PDB:6JPA"
FT TURN 520..522
FT /evidence="ECO:0007829|PDB:7JPX"
FT HELIX 523..529
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 530..541
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 543..558
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 560..581
FT /evidence="ECO:0007829|PDB:6JPA"
FT TURN 582..584
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 588..590
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 597..599
FT /evidence="ECO:0007829|PDB:6JP8"
FT HELIX 600..612
FT /evidence="ECO:0007829|PDB:6JPA"
FT TURN 613..615
FT /evidence="ECO:0007829|PDB:6JP8"
FT HELIX 616..625
FT /evidence="ECO:0007829|PDB:6JPA"
FT TURN 626..628
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 629..631
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 632..636
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 638..676
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 679..686
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 791..797
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 799..805
FT /evidence="ECO:0007829|PDB:6JPA"
FT TURN 806..808
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 809..815
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 816..818
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 821..823
FT /evidence="ECO:0007829|PDB:7JPK"
FT HELIX 827..831
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 833..853
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 870..882
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 893..898
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 899..902
FT /evidence="ECO:0007829|PDB:6JPB"
FT HELIX 903..905
FT /evidence="ECO:0007829|PDB:6JPA"
FT TURN 906..910
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 912..923
FT /evidence="ECO:0007829|PDB:6JPA"
FT TURN 926..929
FT /evidence="ECO:0007829|PDB:7JPK"
FT HELIX 930..950
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 955..959
FT /evidence="ECO:0007829|PDB:6JPA"
FT TURN 965..967
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 970..975
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 976..978
FT /evidence="ECO:0007829|PDB:6JP8"
FT STRAND 983..987
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 990..992
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 1000..1011
FT /evidence="ECO:0007829|PDB:6JPA"
FT TURN 1012..1015
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 1016..1025
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 1028..1030
FT /evidence="ECO:0007829|PDB:7JPK"
FT HELIX 1041..1070
FT /evidence="ECO:0007829|PDB:6JPA"
FT TURN 1071..1074
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 1079..1081
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 1083..1094
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 1106..1116
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 1118..1135
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 1144..1170
FT /evidence="ECO:0007829|PDB:6JPA"
FT TURN 1171..1179
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 1181..1205
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 1235..1237
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 1240..1248
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 1251..1261
FT /evidence="ECO:0007829|PDB:6JPA"
FT TURN 1262..1266
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 1268..1289
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 1290..1292
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 1298..1304
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 1306..1308
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 1309..1320
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 1325..1331
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 1333..1336
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 1349..1351
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 1357..1381
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 1384..1387
FT /evidence="ECO:0007829|PDB:6JPA"
FT TURN 1391..1393
FT /evidence="ECO:0007829|PDB:6JP8"
FT HELIX 1396..1406
FT /evidence="ECO:0007829|PDB:6JPA"
FT TURN 1407..1409
FT /evidence="ECO:0007829|PDB:6JPA"
FT STRAND 1415..1417
FT /evidence="ECO:0007829|PDB:6JPA"
FT TURN 1420..1422
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 1423..1426
FT /evidence="ECO:0007829|PDB:6JPA"
FT TURN 1431..1433
FT /evidence="ECO:0007829|PDB:6JPA"
FT TURN 1440..1442
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 1443..1450
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 1463..1474
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 1483..1492
FT /evidence="ECO:0007829|PDB:6JPA"
FT TURN 1498..1500
FT /evidence="ECO:0007829|PDB:6JPA"
FT HELIX 1501..1505
FT /evidence="ECO:0007829|PDB:6JPA"
SQ SEQUENCE 1873 AA; 212029 MW; 047B10D1946B0796 CRC64;
MEPSSPQDEG LRKKQPKKPL PEVLPRPPRA LFCLTLQNPL RKACISIVEW KPFETIILLT
IFANCVALAV YLPMPEDDNN SLNLGLEKLE YFFLTVFSIE AAMKIIAYGF LFHQDAYLRS
GWNVLDFIIV FLGVFTAILE QVNVIQSNTA PMSSKGAGLD VKALRAFRVL RPLRLVSGVP
SLQVVLNSIF KAMLPLFHIA LLVLFMVIIY AIIGLELFKG KMHKTCYYIG TDIVATVENE
KPSPCARTGS GRPCTINGSE CRGGWPGPNH GITHFDNFGF SMLTVYQCIT MEGWTDVLYW
VNDAIGNEWP WIYFVTLILL GSFFILNLVL GVLSGEFTKE REKAKSRGTF QKLREKQQLE
EDLRGYMSWI TQGEVMDVED LREGKLSLEE GGSDTESLYE IEGLNKIIQF IRHWRQWNRV
FRWKCHDLVK SRVFYWLVIL IVALNTLSIA SEHHNQPLWL THLQDIANRV LLSLFTIEML
LKMYGLGLRQ YFMSIFNRFD CFVVCSGILE LLLVESGAMT PLGISVLRCI RLLRLFKITK
YWTSLSNLVA SLLNSIRSIA SLLLLLFLFI IIFALLGMQL FGGRYDFEDT EVRRSNFDNF
PQALISVFQV LTGEDWNSVM YNGIMAYGGP SYPGVLVCIY FIILFVCGNY ILLNVFLAIA
VDNLAEAESL TSAQKAKAEE RKRRKMSRGL PDKTEEEKSV MAKKLEQKPK GEGIPTTAKL
KVDEFESNVN EVKDPYPSAD FPGDDEEDEP EIPVSPRPRP LAELQLKEKA VPIPEASSFF
IFSPTNKVRV LCHRIVNATW FTNFILLFIL LSSAALAAED PIRAESVRNQ ILGYFDIAFT
SVFTVEIVLK MTTYGAFLHK GSFCRNYFNI LDLLVVAVSL ISMGLESSTI SVVKILRVLR
VLRPLRAINR AKGLKHVVQC VFVAIRTIGN IVLVTTLLQF MFACIGVQLF KGKFFSCNDL
SKMTEEECRG YYYVYKDGDP TQMELRPRQW IHNDFHFDNV LSAMMSLFTV STFEGWPQLL
YRAIDSNEED MGPVYNNRVE MAIFFIIYII LIAFFMMNIF VGFVIVTFQE QGETEYKNCE
LDKNQRQCVQ YALKARPLRC YIPKNPYQYQ VWYVVTSSYF EYLMFALIML NTICLGMQHY
HQSEEMNHIS DILNVAFTII FTLEMILKLL AFKARGYFGD PWNVFDFLIV IGSIIDVILS
EIDTFLASSG GLYCLGGGCG NVDPDESARI SSAFFRLFRV MRLIKLLSRA EGVRTLLWTF
IKSFQALPYV ALLIVMLFFI YAVIGMQMFG KIALVDGTQI NRNNNFQTFP QAVLLLFRCA
TGEAWQEILL ACSYGKLCDP ESDYAPGEEY TCGTNFAYYY FISFYMLCAF LIINLFVAVI
MDNFDYLTRD WSILGPHHLD EFKAIWAEYD PEAKGRIKHL DVVTLLRRIQ PPLGFGKFCP
HRVACKRLVG MNMPLNSDGT VTFNATLFAL VRTALKIKTE GNFEQANEEL RAIIKKIWKR
TSMKLLDQVI PPIGDDEVTV GKFYATFLIQ EHFRKFMKRQ EEYYGYRPKK DTVQIQAGLR
TIEEEAAPEI RRTISGDLTA EEELERAMVE AAMEERIFRR TGGLFGQVDT FLERTNSLPP
VMANQRPLQF AEIEMEELES PVFLEDFPQD ARTNPLARAN TNNANANVAY GNSNHSNNQM
FSSVHCEREF PGEAETPAAG RGALSHSHRA LGPHSKPCAG KLNGQLVQPG MPINQAPPAP
CQQPSTDPPE RGQRRTSLTG SLQDEAPQRR SSEGSTPRRP APATALLIQE ALVRGGLDTL
AADAGFVTAT SQALADACQM EPEEVEVAAT ELLKARESVQ GMASVPGSLS RRSSLGSLDQ
VQGSQETLIP PRP
