GenomeNet

Database: UniProt
Entry: CAC1D_RAT
LinkDB: CAC1D_RAT
Original site: CAC1D_RAT 
ID   CAC1D_RAT               Reviewed;        2203 AA.
AC   P27732; O09022; O09023; O09024; Q01542; Q62691; Q62815; Q63491;
AC   Q63492;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   27-SEP-2017, entry version 146.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha-1D;
DE   AltName: Full=Calcium channel, L type, alpha-1 polypeptide, isoform 2;
DE   AltName: Full=Rat brain class D;
DE            Short=RBD;
DE   AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.3;
GN   Name=Cacna1d; Synonyms=Cach3, Cacn4, Cacnl1a2, Cchl1a2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Insulinoma;
RX   PubMed=7760845; DOI=10.1210/mend.9.1.7760845;
RA   Ihara Y., Yamada Y., Fujii Y., Gonoi T., Yano H., Yasuda K.,
RA   Inagaki N., Seino Y., Seino S.;
RT   "Molecular diversity and functional characterization of voltage-
RT   dependent calcium channels (CACN4) expressed in pancreatic beta-
RT   cells.";
RL   Mol. Endocrinol. 9:121-130(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 6; 7; 8 AND 13).
RC   TISSUE=Brain;
RX   PubMed=1648940; DOI=10.1016/0896-6273(91)90072-8;
RA   Hui A., Ellinor P.T., Krizanova O., Wang J.-J., Diebold R.J.,
RA   Schwartz A.;
RT   "Molecular cloning of multiple subtypes of a novel rat brain isoform
RT   of the alpha-1 subunit of the voltage-dependent calcium channel.";
RL   Neuron 7:35-44(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125.
RX   PubMed=7553731; DOI=10.1007/BF02089942;
RA   Kamp T.J., Mitas M., Fields K.L., Asoh S., Chin H., Marban E.,
RA   Nirenberg M.;
RT   "Transcriptional regulation of the neuronal L-type calcium channel
RT   alpha 1D subunit gene.";
RL   Cell. Mol. Neurobiol. 15:307-326(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1100-1410 (ISOFORMS 4 AND 11).
RC   TISSUE=Kidney;
RX   PubMed=1279681; DOI=10.1073/pnas.89.21.10494;
RA   Yu A.S.L., Hebert S.C., Brenner B.M., Lytton J.;
RT   "Molecular characterization and nephron distribution of a family of
RT   transcripts encoding the pore-forming subunit of Ca2+ channels in the
RT   kidney.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:10494-10498(1992).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1218-1498 (ISOFORM 12).
RC   TISSUE=Osteosarcoma;
RX   PubMed=7479909; DOI=10.1073/pnas.92.24.10914;
RA   Barry E.L.R., Gesek F.A., Froehner S.C., Friedman P.A.;
RT   "Multiple calcium channel transcripts in rat osteosarcoma cells:
RT   selective activation of alpha 1D isoform by parathyroid hormone.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:10914-10918(1995).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1200-1493 (ISOFORMS 3; 4; 5; 9 AND 10).
RC   TISSUE=Hepatoma;
RX   PubMed=9232351; DOI=10.1016/S0143-4160(97)90088-9;
RA   Brereton H.M., Harland M.L., Froscio M., Petronijevic T.,
RA   Barritt G.J.;
RT   "Novel variants of voltage-operated calcium channel alpha-1 subunit
RT   transcripts in a rat liver-derived cell line: deletion in the IVS4
RT   voltage sensing region.";
RL   Cell Calcium 22:39-52(1997).
RN   [7]
RP   NUCLEOTIDE SEQUENCE OF 1307-1479 (ISOFORM 3).
RX   PubMed=1692134; DOI=10.1073/pnas.87.9.3391;
RA   Snutch T.P., Leonard J.P., Gilbert M.M., Lester H.A., Davidson N.;
RT   "Rat brain expresses a heterogeneous family of calcium channels.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:3391-3395(1990).
RN   [8]
RP   FUNCTION, MUTAGENESIS OF 1656-ILE-GLN-1657, INTERACTION WITH CABP1 AND
RP   CABP4, AND TISSUE SPECIFICITY.
RX   PubMed=17050707; DOI=10.1523/JNEUROSCI.3236-06.2006;
RA   Yang P.S., Alseikhan B.A., Hiel H., Grant L., Mori M.X., Yang W.,
RA   Fuchs P.A., Yue D.T.;
RT   "Switching of Ca2+-dependent inactivation of Ca(v)1.3 channels by
RT   calcium binding proteins of auditory hair cells.";
RL   J. Neurosci. 26:10677-10689(2006).
CC   -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the
CC       entry of calcium ions into excitable cells and are also involved
CC       in a variety of calcium-dependent processes, including muscle
CC       contraction, hormone or neurotransmitter release, gene expression,
CC       cell motility, cell division and cell death. The isoform alpha-1D
CC       gives rise to L-type calcium currents. Long-lasting (L-type)
CC       calcium channels belong to the 'high-voltage activated' (HVA)
CC       group. They are blocked by dihydropyridines (DHP),
CC       phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA
CC       (omega-Aga-IIIA). They are however insensitive to omega-conotoxin-
CC       GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA).
CC       {ECO:0000269|PubMed:17050707}.
CC   -!- SUBUNIT: Voltage-dependent calcium channels are multisubunit
CC       complexes, consisting of alpha-1, alpha-2, beta and delta subunits
CC       in a 1:1:1:1 ratio. The channel activity is directed by the pore-
CC       forming and voltage-sensitive alpha-1 subunit. In many cases, this
CC       subunit is sufficient to generate voltage-sensitive calcium
CC       channel activity. The auxiliary subunits beta and alpha-2/delta
CC       linked by a disulfide bridge regulate the channel activity.
CC       Interacts with CABP1 and CABP4, resulting in a near elimination of
CC       calcium-dependent inactivation of the channel. Interacts with
CC       RIMBP2 (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       O88871:Gabbr2; NbExp=6; IntAct=EBI-8072674, EBI-7090239;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=13;
CC         Comment=The region sequenced in isoforms ROB3 and RKC5 is
CC         identical to CACN4.;
CC       Name=1; Synonyms=CACN4A;
CC         IsoId=P27732-1; Sequence=Displayed;
CC       Name=2; Synonyms=CACN4B;
CC         IsoId=P27732-2; Sequence=VSP_000923, VSP_000924;
CC       Name=3; Synonyms=CACH3A, RB48, RBD-55;
CC         IsoId=P27732-3; Sequence=VSP_000921;
CC       Name=4; Synonyms=Delta-IV-S3, RKC6;
CC         IsoId=P27732-4; Sequence=VSP_000919;
CC       Name=5; Synonyms=Delta-IV-S4;
CC         IsoId=P27732-5; Sequence=VSP_000922;
CC       Name=6; Synonyms=RB9;
CC         IsoId=P27732-6; Sequence=VSP_000920, VSP_000921;
CC       Name=7; Synonyms=RB11;
CC         IsoId=P27732-7; Sequence=VSP_000917;
CC       Name=8; Synonyms=RB34;
CC         IsoId=P27732-8; Sequence=VSP_000916;
CC       Name=9; Synonyms=RH1;
CC         IsoId=P27732-9; Sequence=VSP_000918;
CC       Name=10; Synonyms=RH2;
CC         IsoId=P27732-10; Sequence=VSP_000919, VSP_000922;
CC       Name=11; Synonyms=RKC5;
CC         IsoId=P27732-13; Sequence=Not described;
CC       Name=12; Synonyms=ROB3;
CC         IsoId=P27732-14; Sequence=Not described;
CC       Name=13; Synonyms=Truncated;
CC         IsoId=P27732-12; Sequence=VSP_000925, VSP_000926;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, pancreatic islets and B-
CC       lymphocytes. {ECO:0000269|PubMed:17050707}.
CC   -!- DOMAIN: Each of the four internal repeats contains five
CC       hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one
CC       positively charged transmembrane segment (S4). S4 segments
CC       probably represent the voltage-sensor and are characterized by a
CC       series of positively charged amino acids at every third position.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC       1.A.1.11) family. CACNA1D subfamily. {ECO:0000305}.
DR   EMBL; D38101; BAA07282.1; -; mRNA.
DR   EMBL; D38102; BAA07283.1; -; mRNA.
DR   EMBL; M57682; AAA42015.1; -; mRNA.
DR   EMBL; U14005; AAB60515.1; -; Genomic_DNA.
DR   EMBL; M99221; AAA40895.1; -; mRNA.
DR   EMBL; U31772; AAA89156.1; -; mRNA.
DR   EMBL; U49126; AAB61634.1; -; mRNA.
DR   EMBL; U49127; AAB61635.1; -; mRNA.
DR   EMBL; U49128; AAB61636.1; -; mRNA.
DR   PIR; JH0422; JH0422.
DR   PIR; T42742; T42742.
DR   RefSeq; NP_058994.1; NM_017298.1. [P27732-1]
DR   UniGene; Rn.89671; -.
DR   ProteinModelPortal; P27732; -.
DR   SMR; P27732; -.
DR   DIP; DIP-60740N; -.
DR   IntAct; P27732; 2.
DR   MINT; MINT-7965882; -.
DR   STRING; 10116.ENSRNOP00000051407; -.
DR   BindingDB; P27732; -.
DR   ChEMBL; CHEMBL4132; -.
DR   GuidetoPHARMACOLOGY; 530; -.
DR   TCDB; 1.A.1.11.1; the voltage-gated ion channel (vic) superfamily.
DR   iPTMnet; P27732; -.
DR   PhosphoSitePlus; P27732; -.
DR   PaxDb; P27732; -.
DR   PRIDE; P27732; -.
DR   GeneID; 29716; -.
DR   KEGG; rno:29716; -.
DR   CTD; 776; -.
DR   RGD; 70973; Cacna1d.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   HOVERGEN; HBG050763; -.
DR   InParanoid; P27732; -.
DR   KO; K04851; -.
DR   PhylomeDB; P27732; -.
DR   Reactome; R-RNO-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR   PRO; PR:P27732; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0032590; C:dendrite membrane; IDA:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR   GO; GO:0042383; C:sarcolemma; IDA:RGD.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IC:RGD.
DR   GO; GO:0030506; F:ankyrin binding; IPI:BHF-UCL.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IDA:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030165; F:PDZ domain binding; IDA:RGD.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:BHF-UCL.
DR   GO; GO:0086007; F:voltage-gated calcium channel activity involved in cardiac muscle cell action potential; IC:BHF-UCL.
DR   GO; GO:0007568; P:aging; IEP:RGD.
DR   GO; GO:0070509; P:calcium ion import; IMP:RGD.
DR   GO; GO:0006816; P:calcium ion transport; IDA:BHF-UCL.
DR   GO; GO:0019722; P:calcium-mediated signaling; IDA:RGD.
DR   GO; GO:0070838; P:divalent metal ion transport; IMP:RGD.
DR   GO; GO:0007507; P:heart development; IEP:RGD.
DR   GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR   GO; GO:0086012; P:membrane depolarization during cardiac muscle cell action potential; IC:BHF-UCL.
DR   GO; GO:0007613; P:memory; IEP:RGD.
DR   GO; GO:0032793; P:positive regulation of CREB transcription factor activity; IMP:RGD.
DR   GO; GO:0051924; P:regulation of calcium ion transport; IDA:BHF-UCL.
DR   InterPro; IPR031688; CAC1F_C.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR005452; LVDCC_a1dsu.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF239; PTHR10037:SF239; 1.
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; PR01636; LVDCCALPHA1D.
DR   SMART; SM01062; Ca_chan_IQ; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW   Complete proteome; Disulfide bond; Glycoprotein; Ion channel;
KW   Ion transport; Membrane; Metal-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix;
KW   Transport; Voltage-gated channel.
FT   CHAIN         1   2203       Voltage-dependent L-type calcium channel
FT                                subunit alpha-1D.
FT                                /FTId=PRO_0000053936.
FT   TOPO_DOM      1    126       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    127    145       Helical; Name=S1 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    146    163       Extracellular. {ECO:0000255}.
FT   TRANSMEM    164    183       Helical; Name=S2 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    184    195       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    196    214       Helical; Name=S3 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    215    235       Extracellular. {ECO:0000255}.
FT   TRANSMEM    236    254       Helical; Name=S4 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    255    273       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    274    293       Helical; Name=S5 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    294    381       Extracellular. {ECO:0000255}.
FT   TRANSMEM    382    406       Helical; Name=S6 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    407    582       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    583    602       Helical; Name=S1 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    603    617       Extracellular. {ECO:0000255}.
FT   TRANSMEM    618    636       Helical; Name=S2 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    637    644       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    645    663       Helical; Name=S3 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    664    673       Extracellular. {ECO:0000255}.
FT   TRANSMEM    674    692       Helical; Name=S4 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    693    711       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    712    732       Helical; Name=S5 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    733    786       Extracellular. {ECO:0000255}.
FT   TRANSMEM    787    811       Helical; Name=S6 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    812    945       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    946    964       Helical; Name=S1 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM    965    980       Extracellular. {ECO:0000255}.
FT   TRANSMEM    981   1000       Helical; Name=S2 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1001   1012       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1013   1031       Helical; Name=S3 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1032   1037       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1038   1057       Helical; Name=S4 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1058   1076       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1077   1096       Helical; Name=S5 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1097   1186       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1187   1207       Helical; Name=S6 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1208   1264       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1265   1283       Helical; Name=S1 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1284   1298       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1299   1318       Helical; Name=S2 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1319   1325       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1326   1347       Helical; Name=S3 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1348   1357       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1358   1377       Helical; Name=S4 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1378   1396       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1397   1416       Helical; Name=S5 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1417   1483       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1484   1508       Helical; Name=S6 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1509   2203       Cytoplasmic. {ECO:0000255}.
FT   REPEAT      112    408       I.
FT   REPEAT      528    774       II.
FT   REPEAT      892   1174       III.
FT   REPEAT     1211   1486       IV.
FT   CA_BIND    1537   1548       {ECO:0000255}.
FT   REGION      429    446       Binding to the beta subunit.
FT                                {ECO:0000250}.
FT   REGION     1134   1224       Dihydropyridine binding. {ECO:0000250}.
FT   REGION     1464   1530       Dihydropyridine binding. {ECO:0000250}.
FT   REGION     1476   1519       Phenylalkylamine binding. {ECO:0000250}.
FT   COMPBIAS      1      7       Poly-Met.
FT   COMPBIAS    712    718       Poly-Leu.
FT   COMPBIAS    886    897       Poly-Glu.
FT   SITE        364    364       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   SITE        763    763       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   SITE       1160   1160       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   SITE       1450   1450       Calcium ion selectivity and permeability.
FT                                {ECO:0000250}.
FT   MOD_RES    1519   1519       Phosphoserine; by PKA. {ECO:0000255}.
FT   CARBOHYD    155    155       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    225    225       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    329    329       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   VAR_SEQ     481    492       Missing (in isoform 8).
FT                                {ECO:0000303|PubMed:1648940}.
FT                                /FTId=VSP_000916.
FT   VAR_SEQ     493    512       Missing (in isoform 7).
FT                                {ECO:0000303|PubMed:1648940}.
FT                                /FTId=VSP_000917.
FT   VAR_SEQ    1322   1392       Missing (in isoform 9).
FT                                {ECO:0000303|PubMed:9232351}.
FT                                /FTId=VSP_000918.
FT   VAR_SEQ    1322   1349       Missing (in isoform 4 and isoform 10).
FT                                {ECO:0000303|PubMed:1279681,
FT                                ECO:0000303|PubMed:9232351}.
FT                                /FTId=VSP_000919.
FT   VAR_SEQ    1322   1348       GYFSDAWNTFDSLIVIGSIIDVALSEA -> HYFTDAWNTF
FT                                DALIVVGSVVDIAITEVN (in isoform 6).
FT                                {ECO:0000303|PubMed:1648940}.
FT                                /FTId=VSP_000920.
FT   VAR_SEQ    1349   1349       D -> DPSDSENIPLPTATPG (in isoform 6 and
FT                                isoform 3). {ECO:0000303|PubMed:1648940,
FT                                ECO:0000303|PubMed:9232351}.
FT                                /FTId=VSP_000921.
FT   VAR_SEQ    1354   1368       Missing (in isoform 10 and isoform 5).
FT                                {ECO:0000303|PubMed:9232351}.
FT                                /FTId=VSP_000922.
FT   VAR_SEQ    1642   1668       DDEVTVGKFYATFLIQDYFRKFKKRKE -> GNSRSGKSKA
FT                                WWGNTLRRTPRSPYRRD (in isoform 2).
FT                                {ECO:0000303|PubMed:7760845}.
FT                                /FTId=VSP_000923.
FT   VAR_SEQ    1669   2203       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:7760845}.
FT                                /FTId=VSP_000924.
FT   VAR_SEQ    1686   1691       AGLRTL -> MLERML (in isoform 13).
FT                                {ECO:0000303|PubMed:1648940}.
FT                                /FTId=VSP_000925.
FT   VAR_SEQ    1692   2203       Missing (in isoform 13).
FT                                {ECO:0000303|PubMed:1648940}.
FT                                /FTId=VSP_000926.
FT   MUTAGEN    1656   1657       IQ->AA: Loss of calcium-dependent
FT                                inactivation related to the C-terminal
FT                                lobe of calmodulin.
FT                                {ECO:0000269|PubMed:17050707}.
FT   CONFLICT    124    124       D -> N (in Ref. 2; AAA42015).
FT                                {ECO:0000305}.
FT   CONFLICT    183    183       S -> Y (in Ref. 2; AAA42015).
FT                                {ECO:0000305}.
FT   CONFLICT    192    192       S -> Y (in Ref. 2; AAA42015).
FT                                {ECO:0000305}.
FT   CONFLICT    513    513       G -> C (in Ref. 2). {ECO:0000305}.
FT   CONFLICT    522    560       Missing (in Ref. 2). {ECO:0000305}.
FT   CONFLICT   1452   1452       W -> R (in Ref. 5; AAA89156).
FT                                {ECO:0000305}.
SQ   SEQUENCE   2203 AA;  250136 MW;  8E746A8D988050C6 CRC64;
     MMMMMMMKKM QHQRQQQEDH ANEANYARGT RLPISGEGPT SQPNSSKQTV LSWQAAIDAA
     RQAKAAQTMS TSAPPPVGSL SQRKRQQYAK SKKQGNSSNS RPARALFCLS LNNPIRRACI
     SIVDWKPFDI FILLAIFANC VALAIYIPFP EDDSNSTNHN LEKVEYAFLI IFTVETFLKI
     IASGLLLHPN ASVRNGWNLL DFVIVIVGLF SVILEQLTKE TEGGNHSSGK SGGFDVKALR
     AFRVLRPLRL VSGVPSLQVV LNSIIKAMVP LLHIALLVLF VIIIYAIIGL ELFIGKMHKT
     CFFADSDIVA EEDPAPCAFS GNGRQCAANG TECRSGWVGP NGGITNFDNF AFAMLTVFQC
     ITMEGWTDVL YWVNDAIGWE WPWVYFVSLI ILGSFFVLNL VLGVLSGEFS KEREKAKARG
     DFQKLREKQQ LEEDLKGYLD WITQAEDIDP ENEEEGGEEG KRNTSMPTSE TESVNTENVS
     GEGETQGCCG SLWCWWKRRG AAKTGPSGCR RWGQAISKSK LRSHGAREAL CVCRCSLESL
     VKLWTSRFSA HLQAAYVRPY SRRWRRWNRF NRRRCRAAVK SVTFYWLVIV LVFLNTLTIS
     SEHYNQPDWL TQIQDIANKV LLALFTCEML VKMYSLGLQA YFVSLFNRFD CFVVCGGITE
     TILVELELMS PLGVSVFRCV RLLRIFKVTR HWTSLSNLVA SLLNSMKSIA SLLLLLFLFI
     IIFSLLGMQL FGGKFNFDET QTKRSTFDNF PQALLTVFQI LTGEDWNAVM YDGIMAYGGP
     SSSGMIVCIY FIILFICGNY ILLKLFLAIA VDNLADAESL NTAQKEEAEE KERKKIARKE
     SLENKKNNKP EVNQIANSDN KVTIDDYQEE AEDKDPYPPC DVPVGEEEEE EEEDEPEVPA
     GPRPRRISEL NMKEKIAPIP EGSAFFILSK TNPIRVGCHK LINHHIFTNL ILVFIMLSSA
     ALAAEDPIRS HSFRNTILGY FDYAFTAIFT VEILLKMTTF GAFLHKGAFC RNYFNLLDML
     VVGVSLVSFG IQSSAISVVK ILRVLRVLRP LRAINRAKGL KHVVQCVFVA IRTIGNIMIV
     TTLLQFMFAC IGVQLFKGKF YRCTDEAKSN PEECRGLFIL YKDGDVDSPV VRERIWQNSD
     FNFDNVLSAM MALFTVSTFE GWPALLYKAI DSNGENVGPV YNYRVEISIF FIIYIIIVAF
     FMMNIFVGFV IVTFQEQGEK EYKNCELDKN QRQCVEYALK ARPLRRYIPK NPYQYKFWYV
     VNSSPFEYMM FVLIMLNTLC LAMQHYEQSK MFNDAMDILN MVFTGVFTVE MVLKVIAFKP
     KGYFSDAWNT FDSLIVIGSI IDVALSEADN SEESNRISIT FFRLFRVMRL VKLLSRGEGI
     RTLLWTFIKS FQALPYVALL IAMLFFIYAV IGMQMFGKVA MRDNNQINRN NNFQTFPQAV
     LLLFRCATGE AWQEIMLACL PGKLCDPDSD YNPGEEYTCG SNFAIVYFIS FYMLCAFLII
     NLFVAVIMDN FDYLTRDWSI LGPHHLDEFK RIWSEYDPEA KGRIKHLDVV TLLRRIQPPL
     GFGKLCPHRV ACKRLVAMNM PLNSDGTVMF NATLFALVRT ALKIKTEGNL EQANEELRAV
     IKKIWKKTSM KLLDQVVPPA GDDEVTVGKF YATFLIQDYF RKFKKRKEQG LVGKYPAKNT
     TIALQAGLRT LHDIGPEIRR AISCDLQDDE PEDSKPEEED VFKRNGALLG NYVNHVNSDR
     RESLQQTNTT HRPLHVQRPS IPPASDTEKP LFPPAGNSVC HNHHNHNSIG KQVPTSTNAN
     LNNANMSKAA HGKRPSIGDL EHVSENGHYS YKHDRELQRR SSIKRTRYYE TYIRSESGDE
     QLPTIFREDP EIHGYFRDPR CFGEQEYFSS EECCEDDSSP TWSRQNYSYY NRYPGSSMDF
     ERPRGYHHPQ GFLEDDDSPI GYDSRRSPRR RLLPPTPPSH RRSSFNFECL RRQNSQDDVL
     PSPALPHRAA LPLHLMQQQI MAVAGLDSSK AQKYSPSHST RSWATPPATP PYRDWTPCYT
     PLIQVDRSES MDQVNGSLPS LHRSSWYTDE PDISYRTFTP ASLTVPSSFR NKNSDKQRSA
     DSLVEAVLIS EGLGRYARDP KFVSATKHEI ADACDLTIDE MESAASTLLN GSVCPRANGD
     MGPISHRQDY ELQDFGPGYS DEEPDPGREE EDLADEMICI TTL
//
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