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Voltage-dependent L-type calcium channel subunit alpha-1C (Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle) (Rat brain class C) (RBC) (Voltage-gated calcium channel subunit alpha Cav1.2)

 CAC1C_RAT               Reviewed;        2169 AA.
P22002; P27733; P27734; Q62816; Q63271; Q64178;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-AUG-1991, sequence version 1.
25-OCT-2017, entry version 163.
RecName: Full=Voltage-dependent L-type calcium channel subunit alpha-1C;
AltName: Full=Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle;
AltName: Full=Rat brain class C;
Short=RBC;
AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.2;
Name=Cacna1c; Synonyms=Cach2, Cacn2, Cacnl1a1, Cchl1a1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Aorta;
PubMed=2170396;
Koch W.J., Ellinor P.T., Schwartz A.;
"cDNA cloning of a dihydropyridine-sensitive calcium channel from rat
aorta. Evidence for the existence of alternatively spliced forms.";
J. Biol. Chem. 265:17786-17791(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5).
TISSUE=Brain;
PubMed=1648941; DOI=10.1016/0896-6273(91)90073-9;
Snutch T.P., Tomlinson W.J., Leonard J.P., Gilbert M.M.;
"Distinct calcium channels are generated by alternative splicing and
are differentially expressed in the mammalian CNS.";
Neuron 7:45-57(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1168-1413 (ISOFORM 1).
PubMed=1692134; DOI=10.1073/pnas.87.9.3391;
Snutch T.P., Leonard J.P., Gilbert M.M., Lester H.A., Davidson N.;
"Rat brain expresses a heterogeneous family of calcium channels.";
Proc. Natl. Acad. Sci. U.S.A. 87:3391-3395(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1269-1415 (ISOFORMS 1; 2 AND 3).
PubMed=1311102; DOI=10.1073/pnas.89.4.1497;
Diebold R.J., Koch W.J., Ellinor P.T., Wang J.-J., Muthuchamy M.,
Wieczorek D.F., Schwartz A.;
"Mutually exclusive exon splicing of the cardiac calcium channel a1
subunit generates developmentally regulated isoforms in the rat
heart.";
Proc. Natl. Acad. Sci. U.S.A. 89:1497-1501(1992).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1269-1387.
TISSUE=Myometrium;
PubMed=7485440;
Tezuka N., Ali M., Chwalisz K., Garfield R.E.;
"Changes in transcripts encoding calcium channel subunits of rat
myometrium during pregnancy.";
Am. J. Physiol. 269:C1008-C1017(1995).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1202-1495 (ISOFORM 3).
TISSUE=Osteosarcoma;
PubMed=7479909; DOI=10.1073/pnas.92.24.10914;
Barry E.L.R., Gesek F.A., Froehner S.C., Friedman P.A.;
"Multiple calcium channel transcripts in rat osteosarcoma cells:
selective activation of alpha 1D isoform by parathyroid hormone.";
Proc. Natl. Acad. Sci. U.S.A. 92:10914-10918(1995).
[7]
PHOSPHORYLATION.
PubMed=8396138;
Hell J.W., Yokoyama C.T., Wong S.T., Warner C., Snutch T.P.,
Catterall W.A.;
"Differential phosphorylation of two size forms of the neuronal class
C L-type calcium channel alpha 1 subunit.";
J. Biol. Chem. 268:19451-19457(1993).
[8]
INTERACTION WITH CABP1.
PubMed=15140941; DOI=10.1523/JNEUROSCI.5523-03.2004;
Zhou H., Kim S.-A., Kirk E.A., Tippens A.L., Sun H., Haeseleer F.,
Lee A.;
"Ca2+-binding protein-1 facilitates and forms a postsynaptic complex
with Cav1.2 (L-type) Ca2+ channels.";
J. Neurosci. 24:4698-4708(2004).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-845; SER-1699 AND
SER-1720, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[10]
INTERACTION WITH CACNB3.
PubMed=24751537; DOI=10.1083/jcb.201304101;
Beguin P., Nagashima K., Mahalakshmi R.N., Vigot R., Matsunaga A.,
Miki T., Ng M.Y., Ng Y.J., Lim C.H., Tay H.S., Hwang L.A., Firsov D.,
Tang B.L., Inagaki N., Mori Y., Seino S., Launey T., Hunziker W.;
"BARP suppresses voltage-gated calcium channel activity and Ca2+-
evoked exocytosis.";
J. Cell Biol. 205:233-249(2014).
[11]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 452-476 IN COMPLEX WITH
CACNB3, FUNCTION, AND REGION.
PubMed=15170217; DOI=10.1038/nature02641;
Chen Y.H., Li M.H., Zhang Y., He L.L., Yamada Y., Fitzmaurice A.,
Shen Y., Zhang H., Tong L., Yang J.;
"Structural basis of the alpha1-beta subunit interaction of voltage-
gated Ca2+ channels.";
Nature 429:675-680(2004).
-!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the
entry of calcium ions into excitable cells and are also involved
in a variety of calcium-dependent processes, including muscle
contraction, hormone or neurotransmitter release, gene expression,
cell motility, cell division and cell death. The isoform alpha-1C
gives rise to L-type calcium currents. Long-lasting (L-type)
calcium channels belong to the 'high-voltage activated' (HVA)
group. They are blocked by dihydropyridines (DHP),
phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA
(omega-Aga-IIIA). They are however insensitive to omega-conotoxin-
GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA).
Calcium channels containing the alpha-1C subunit play an important
role in excitation-contraction coupling in the heart. Binding of
calmodulin or CABP1 at the same regulatory sites results in an
opposit effects on the channel function.
{ECO:0000269|PubMed:15170217}.
-!- SUBUNIT: Voltage-dependent calcium channels are multisubunit
complexes, consisting of alpha-1, alpha-2, beta and delta subunits
in a 1:1:1:1 ratio. The channel activity is directed by the pore-
forming and voltage-sensitive alpha-1 subunit. In many cases, this
subunit is sufficient to generate voltage-sensitive calcium
channel activity. The auxiliary subunits beta and alpha-2/delta
linked by a disulfide bridge regulate the channel activity.
Interacts (via C-terminal C and IQ motifs) with CABP1. The binding
via the C motif is calcium independent whereas the binding via IQ
requires the presence of calcium and is mutually exclusive with
calmodulin binding. Interacts with CACNA2D4 (By similarity).
Interacts (via C-terminal CDB motif) with CABP5; in a calcium-
dependent manner. Interacts with CIB1; the interaction increases
upon cardiomyocytes hypertrophy (By similarity). {ECO:0000250,
ECO:0000269|PubMed:15140941, ECO:0000269|PubMed:15170217,
ECO:0000269|PubMed:24751537}.
-!- INTERACTION:
P63329:Ppp3ca; NbExp=5; IntAct=EBI-1185084, EBI-7022944;
Q9WUD9:Src; NbExp=4; IntAct=EBI-1185084, EBI-7784541;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P15381};
Multi-pass membrane protein {ECO:0000250|UniProtKB:P15381}. Cell
membrane {ECO:0000250|UniProtKB:P15381}. Note=The interaction
between RRAD and CACNB2 regulates its trafficking to the cell
membrane. {ECO:0000250|UniProtKB:P15381}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Additional isoforms seem to exist.;
Name=2; Synonyms=S3B;
IsoId=P22002-1; Sequence=Displayed;
Name=1; Synonyms=S3A;
IsoId=P22002-2; Sequence=VSP_000911;
Name=3; Synonyms=D1, ROB2;
IsoId=P22002-3; Sequence=VSP_000912;
Name=4; Synonyms=rbC-I;
IsoId=P22002-4; Sequence=VSP_000908, VSP_000910, VSP_000911;
Name=5; Synonyms=rbC-II;
IsoId=P22002-5; Sequence=VSP_000908, VSP_000909, VSP_000910;
-!- TISSUE SPECIFICITY: Isoforms 4 and 5 are expressed throughout the
central nervous system, with highest levels in the olfactory bulb
and cerebellum. Also expressed in heart, pituitary, adrenal gland,
liver, kidney, and in a much lesser extent in testes and spleen.
-!- DEVELOPMENTAL STAGE: Expressed from embryonic day 16 until the
adult stage.
-!- DOMAIN: Each of the four internal repeats contains five
hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one
positively charged transmembrane segment (S4). S4 segments
probably represent the voltage-sensor and are characterized by a
series of positively charged amino acids at every third position.
-!- DOMAIN: Binding of intracellular calcium through the EF-hand motif
inhibits the opening of the channel.
{ECO:0000250|UniProtKB:P15381}.
-!- PTM: Phosphorylation by PKA activates the channel (By similarity).
Is also phosphorylated in vitro by CaM-kinase II, PKC and CGPK
(PubMed:8396138). {ECO:0000250|UniProtKB:P15381,
ECO:0000269|PubMed:8396138}.
-!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
1.A.1.11) family. CACNA1C subfamily. {ECO:0000305}.
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EMBL; M59786; AAA85463.1; -; mRNA.
EMBL; M67515; AAA18905.1; -; mRNA.
EMBL; M67516; AAA42016.1; -; mRNA.
EMBL; M91242; AAA41460.1; -; Genomic_DNA.
EMBL; M91240; AAA41460.1; JOINED; Genomic_DNA.
EMBL; M89924; AAA41460.1; JOINED; Genomic_DNA.
EMBL; M91241; AAA41460.1; JOINED; Genomic_DNA.
EMBL; S80558; AAB35528.1; -; mRNA.
EMBL; U31815; AAA89157.1; -; mRNA.
RefSeq; NP_036649.2; NM_012517.2.
UniGene; Rn.9827; -.
PDB; 1VYT; X-ray; 2.60 A; E/F=452-476.
PDBsum; 1VYT; -.
ProteinModelPortal; P22002; -.
SMR; P22002; -.
BioGrid; 246425; 4.
CORUM; P22002; -.
IntAct; P22002; 4.
MINT; MINT-5026000; -.
STRING; 10116.ENSRNOP00000048790; -.
BindingDB; P22002; -.
ChEMBL; CHEMBL3762; -.
GuidetoPHARMACOLOGY; 529; -.
iPTMnet; P22002; -.
PhosphoSitePlus; P22002; -.
PaxDb; P22002; -.
PRIDE; P22002; -.
GeneID; 24239; -.
KEGG; rno:24239; -.
UCSC; RGD:2245; rat. [P22002-1]
CTD; 775; -.
RGD; 2245; Cacna1c.
eggNOG; KOG2301; Eukaryota.
eggNOG; ENOG410XNP6; LUCA.
HOVERGEN; HBG050763; -.
InParanoid; P22002; -.
KO; K04850; -.
PhylomeDB; P22002; -.
Reactome; R-RNO-400042; Adrenaline,noradrenaline inhibits insulin secretion.
EvolutionaryTrace; P22002; -.
PRO; PR:P22002; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:1990454; C:L-type voltage-gated calcium channel complex; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO.
GO; GO:0042734; C:presynaptic membrane; IDA:SynGO.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0042383; C:sarcolemma; IDA:RGD.
GO; GO:0030315; C:T-tubule; IDA:RGD.
GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:RGD.
GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
GO; GO:0051393; F:alpha-actinin binding; ISS:BHF-UCL.
GO; GO:0008331; F:high voltage-gated calcium channel activity; IDA:RGD.
GO; GO:0044325; F:ion channel binding; IPI:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
GO; GO:0051721; F:protein phosphatase 2A binding; IPI:RGD.
GO; GO:0031369; F:translation initiation factor binding; IPI:RGD.
GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:RGD.
GO; GO:0086056; F:voltage-gated calcium channel activity involved in AV node cell action potential; ISS:BHF-UCL.
GO; GO:0086007; F:voltage-gated calcium channel activity involved in cardiac muscle cell action potential; ISS:BHF-UCL.
GO; GO:0070509; P:calcium ion import; IMP:RGD.
GO; GO:0061577; P:calcium ion transmembrane transport via high voltage-gated calcium channel; IDA:UniProtKB.
GO; GO:0006816; P:calcium ion transport; IMP:RGD.
GO; GO:0061337; P:cardiac conduction; ISS:UniProtKB.
GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; ISS:BHF-UCL.
GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
GO; GO:0098912; P:membrane depolarization during atrial cardiac muscle cell action potential; ISS:BHF-UCL.
GO; GO:0086045; P:membrane depolarization during AV node cell action potential; ISS:BHF-UCL.
GO; GO:0086012; P:membrane depolarization during cardiac muscle cell action potential; ISS:BHF-UCL.
GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISS:BHF-UCL.
GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; ISS:BHF-UCL.
InterPro; IPR031688; CAC1F_C.
InterPro; IPR031649; GPHH_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR014873; VDCC_a1su_IQ.
InterPro; IPR005451; VDCC_L_a1csu.
InterPro; IPR005446; VDCC_L_a1su.
InterPro; IPR002077; VDCCAlpha1.
Pfam; PF08763; Ca_chan_IQ; 1.
Pfam; PF16885; CAC1F_C; 1.
Pfam; PF16905; GPHH; 1.
Pfam; PF00520; Ion_trans; 4.
PRINTS; PR00167; CACHANNEL.
PRINTS; PR01630; LVDCCALPHA1.
PRINTS; PR01635; LVDCCALPHA1C.
SMART; SM01062; Ca_chan_IQ; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Calcium channel;
Calcium transport; Cell membrane; Complete proteome; Disulfide bond;
Glycoprotein; Ion channel; Ion transport; Membrane; Metal-binding;
Phosphoprotein; Reference proteome; Repeat; Transmembrane;
Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 2169 Voltage-dependent L-type calcium channel
subunit alpha-1C.
/FTId=PRO_0000053931.
TOPO_DOM 1 154 Cytoplasmic. {ECO:0000255}.
TRANSMEM 155 173 Helical; Name=S1 of repeat I.
{ECO:0000255}.
TOPO_DOM 174 190 Extracellular. {ECO:0000255}.
TRANSMEM 191 211 Helical; Name=S2 of repeat I.
{ECO:0000255}.
TOPO_DOM 212 223 Cytoplasmic. {ECO:0000255}.
TRANSMEM 224 242 Helical; Name=S3 of repeat I.
{ECO:0000255}.
TOPO_DOM 243 262 Extracellular. {ECO:0000255}.
TRANSMEM 263 281 Helical; Name=S4 of repeat I.
{ECO:0000255}.
TOPO_DOM 282 300 Cytoplasmic. {ECO:0000255}.
TRANSMEM 301 320 Helical; Name=S5 of repeat I.
{ECO:0000255}.
TOPO_DOM 321 410 Extracellular. {ECO:0000255}.
TRANSMEM 411 435 Helical; Name=S6 of repeat I.
{ECO:0000255}.
TOPO_DOM 436 554 Cytoplasmic. {ECO:0000255}.
TRANSMEM 555 573 Helical; Name=S1 of repeat II.
{ECO:0000255}.
TOPO_DOM 574 588 Extracellular. {ECO:0000255}.
TRANSMEM 589 608 Helical; Name=S2 of repeat II.
{ECO:0000255}.
TOPO_DOM 609 616 Cytoplasmic. {ECO:0000255}.
TRANSMEM 617 635 Helical; Name=S3 of repeat II.
{ECO:0000255}.
TOPO_DOM 636 645 Extracellular. {ECO:0000255}.
TRANSMEM 646 664 Helical; Name=S4 of repeat II.
{ECO:0000255}.
TOPO_DOM 665 683 Cytoplasmic. {ECO:0000255}.
TRANSMEM 684 703 Helical; Name=S5 of repeat II.
{ECO:0000255}.
TOPO_DOM 704 758 Extracellular. {ECO:0000255}.
TRANSMEM 759 783 Helical; Name=S6 of repeat II.
{ECO:0000255}.
TOPO_DOM 784 930 Cytoplasmic. {ECO:0000255}.
TRANSMEM 931 949 Helical; Name=S1 of repeat III.
{ECO:0000255}.
TOPO_DOM 950 965 Extracellular. {ECO:0000255}.
TRANSMEM 966 985 Helical; Name=S2 of repeat III.
{ECO:0000255}.
TOPO_DOM 986 997 Cytoplasmic. {ECO:0000255}.
TRANSMEM 998 1016 Helical; Name=S3 of repeat III.
{ECO:0000255}.
TOPO_DOM 1017 1023 Extracellular. {ECO:0000255}.
TRANSMEM 1024 1041 Helical; Name=S4 of repeat III.
{ECO:0000255}.
TOPO_DOM 1042 1060 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1061 1080 Helical; Name=S5 of repeat III.
{ECO:0000255}.
TOPO_DOM 1081 1170 Extracellular. {ECO:0000255}.
TRANSMEM 1171 1195 Helical; Name=S6 of repeat III.
{ECO:0000255}.
TOPO_DOM 1196 1248 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1249 1267 Helical; Name=S1 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1268 1282 Extracellular. {ECO:0000255}.
TRANSMEM 1283 1302 Helical; Name=S2 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1303 1310 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1311 1329 Helical; Name=S3 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1330 1353 Extracellular. {ECO:0000255}.
TRANSMEM 1354 1372 Helical; Name=S4 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1373 1391 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1392 1411 Helical; Name=S5 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1412 1480 Extracellular. {ECO:0000255}.
TRANSMEM 1481 1505 Helical; Name=S6 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1506 2169 Cytoplasmic. {ECO:0000255}.
REPEAT 141 438 I.
REPEAT 540 786 II.
REPEAT 917 1198 III.
REPEAT 1235 1508 IV.
CA_BIND 1534 1545 {ECO:0000250}.
REGION 458 475 AID/alpha-interaction domain; mediates
interaction with the beta subunit.
{ECO:0000269|PubMed:15170217}.
REGION 1118 1208 Dihydropyridine binding. {ECO:0000250}.
REGION 1459 1527 Dihydropyridine binding. {ECO:0000250}.
REGION 1473 1516 Phenylalkylamine binding. {ECO:0000250}.
COMPBIAS 684 690 Poly-Leu.
COMPBIAS 798 804 Poly-Glu.
COMPBIAS 1176 1182 Poly-Ile.
SITE 393 393 Calcium ion selectivity and permeability.
{ECO:0000250|UniProtKB:P15381}.
SITE 736 736 Calcium ion selectivity and permeability.
{ECO:0000250|UniProtKB:P15381}.
SITE 1144 1144 Calcium ion selectivity and permeability.
{ECO:0000250|UniProtKB:P15381}.
SITE 1445 1445 Calcium ion selectivity and permeability.
{ECO:0000250|UniProtKB:P15381}.
MOD_RES 499 499 Phosphoserine.
{ECO:0000250|UniProtKB:Q01815}.
MOD_RES 506 506 Phosphothreonine.
{ECO:0000250|UniProtKB:Q01815}.
MOD_RES 838 838 Phosphoserine.
{ECO:0000250|UniProtKB:Q01815}.
MOD_RES 845 845 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1516 1516 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 1699 1699 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1720 1720 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1919 1919 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 1927 1927 Phosphoserine; by PKA. {ECO:0000255}.
CARBOHYD 183 183 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 358 358 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1417 1417 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1468 1468 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 46 MIRAFAQPSTPPYQPLSSCLSEDTERKFKGKVVHEAQLNCF
YISPG -> MVNENTRMYVPEENHQ (in isoform 4
and isoform 5).
{ECO:0000303|PubMed:1648941}.
/FTId=VSP_000908.
VAR_SEQ 810 810 R -> RPAR (in isoform 5).
{ECO:0000303|PubMed:1648941}.
/FTId=VSP_000909.
VAR_SEQ 964 979 FYFDIVFTTIFTIEIA -> GNADYVFTSIFTLEII (in
isoform 4 and isoform 5).
{ECO:0000303|PubMed:1648941}.
/FTId=VSP_000910.
VAR_SEQ 1306 1333 HYFCDAWNTFDALIVVGSIVDIAITEVH -> GYFSDPSNV
FDFLIVIGSIIAVILSETN (in isoform 1 and
isoform 4). {ECO:0000303|PubMed:1648941,
ECO:0000303|PubMed:1692134}.
/FTId=VSP_000911.
VAR_SEQ 1334 1344 Missing (in isoform 3).
{ECO:0000303|PubMed:7479909}.
/FTId=VSP_000912.
CONFLICT 83 83 L -> Q (in Ref. 2; AAA18905/AAA42016).
{ECO:0000305}.
CONFLICT 87 87 D -> G (in Ref. 2; AAA18905).
{ECO:0000305}.
CONFLICT 520 520 G -> R (in Ref. 2; AAA18905).
{ECO:0000305}.
CONFLICT 648 649 CW -> VL (in Ref. 2; AAA18905/AAA42016).
{ECO:0000305}.
CONFLICT 678 678 L -> V (in Ref. 2; AAA18905/AAA42016).
{ECO:0000305}.
CONFLICT 769 770 SP -> CG (in Ref. 2; AAA18905/AAA42016).
{ECO:0000305}.
CONFLICT 777 777 L -> V (in Ref. 2; AAA18905/AAA42016).
{ECO:0000305}.
CONFLICT 871 871 D -> N (in Ref. 2; AAA18905).
{ECO:0000305}.
CONFLICT 1037 1037 R -> RA (in Ref. 2; AAA18905/AAA42016).
{ECO:0000305}.
CONFLICT 1098 1098 S -> C (in Ref. 2; AAA18905/AAA42016).
{ECO:0000305}.
CONFLICT 1107 1107 T -> D (in Ref. 2; AAA18905/AAA42016).
{ECO:0000305}.
CONFLICT 1229 1229 P -> R (in Ref. 2; AAA18905/AAA42016, 3;
no nucleotide entry and 6; AAA89157).
{ECO:0000305}.
CONFLICT 1306 1306 H -> D (in Ref. 5; AAB35528).
{ECO:0000305}.
CONFLICT 1306 1306 H -> G (in Ref. 2; AAA42016 and 6;
AAA89157). {ECO:0000305}.
CONFLICT 1329 1329 I -> L (in Ref. 5; AAB35528).
{ECO:0000305}.
CONFLICT 1471 1471 E -> K (in Ref. 2; AAA18905).
{ECO:0000305}.
CONFLICT 1911 1911 C -> S (in Ref. 2; AAA18905/AAA42016).
{ECO:0000305}.
CONFLICT 2084 2084 K -> N (in Ref. 2; AAA18905).
{ECO:0000305}.
CONFLICT 2154 2154 R -> Q (in Ref. 2; AAA42016).
{ECO:0000305}.
HELIX 454 474 {ECO:0000244|PDB:1VYT}.
SEQUENCE 2169 AA; 243482 MW; D3ADBD20E4763B69 CRC64;
MIRAFAQPST PPYQPLSSCL SEDTERKFKG KVVHEAQLNC FYISPGGSNY GSPRPAHANM
NANAAAGLAP EHIPTPGAAL SWLAAIDAAR QAKLMGSAGN ATISTVSSTQ RKRQQYGKPK
KQGGTTATRP PRALLCLTLK NPIRRACISI VEWKPFEIII LLTIFANCVA LAIYIPFPED
DSNATNSNLE RVEYLFLIIF TVEAFLKVIA YGLLFHPNAY LRNGWNLLDF IIVVVGLFSA
ILEQATKADG ANALGGKGAG FDVKALRAFR VLRPLRLVSG VPSLQVVLNS IIKAMVPLLH
IALLVLFVII IYAIIGLELF MGKMHKTCYN QEGIIDVPAE EDPSPCALET GHGRQCQNGT
VCKPGWDGPK HGITNFDNFA FAMLTVFQCI TMEGWTDVLY WMQDAMGYEL PWVYFVSLVI
FGSFFVLNLV LGVLSGEFSK EREKAKARGD FQKLREKQQL EEDLKGYLDW ITQAEDIDPE
NEDEGMDEDK PRNMSMPTSE TESVNTENVA GGDIEGENCG ARLAHRISKS KFSRYWRRWN
RFCRRKCRAA VKSNVFYWLV IFLVFLNTLT IASEHYNQPH WLTEVQDTAN KALLALFTAE
MLLKMYSLGL QAYFVSLFNR FDCFIVCGGI LETILVETKI MSPLGISCWR CVRLLRIFKI
TRYWNSLSNL VASLLNSLRS IASLLLLLFL FIIIFSLLGM QLFGGKFNFD EMQTRRSTFD
NFPQSLLTVF QILTGEDWNS VMYDGIMAYG GPSFPGMLVC IYFIILFISP NYILLNLFLA
IAVDNLADAE SLTSAQKEEE EEKERKKLAR TASPEKKQEV MEKPAVEESK EEKIELKSIT
ADGESPPTTK INMDDLQPSE NEDKSPHSNP DTAGEEDEEE PEMPVGPRPR PLSELHLKEK
AVPMPEASAF FIFSPNNRFR LQCHRIVNDT IFTNLILFFI LLSSISLAAE DPVQHTSFRN
HILFYFDIVF TTIFTIEIAL KMTAYGAFLH KGSFCRNYFN ILDLLVVSVS LISFGIQSSA
INVVKILRVL RVLRPLRINR AKGLKHVVQC VFVAIRTIGN IVIVTTLLQF MFACIGVQLF
KGKLYTCSDS SKQTEAESKG NYITYKTGEV DHPIIQPRSW ENSKFDFDNV LAAMMALFTV
STFEGWPELL YRSIDSHTED KGPIYNYRVE ISIFFIIYII IIAFFMMNIF VGFVIVTFQE
QGEQEYKNCE LDKNQRQCVE YALKARPLPR YIPKNQHQYK VWYVVNSTYF EYLMFVLILL
NTICLAMQHY GQSCLFKIAM NILNMLFTGL FTVEMILKLI AFKPKHYFCD AWNTFDALIV
VGSIVDIAIT EVHPAEHTQC SPSMSAEENS RISITFFRLF RVMRLVKLLS RGEGIRTLLW
TFIKSFQALP YVALLIVMLF FIYAVIGMQV FGKIALNDTT EINRNNNFQT FPQAVLLLFR
CATGEAWQDI MLACMPGKKC APESEPSNST EGETPCGSSF AVFYFISFYM LCAFLIINLF
VAVIMDNFDY LTRDWSILGP HHLDEFKRIW AEYDPEAKGR IKHLDVVTLL RRIQPPLGFG
KLCPHRVACK RLVSMNMPLN SDGTVMFNAT LFALVRTALR IKTEGNLEQA NEELRAIIKK
IWKRTSMKLL DQVVPPAGDD EVTVGKFYAT FLIQEYFRKF KKRKEQGLVG KPSQRNALSL
QAGLRTLHDI GPEIRRAISG DLTAEEELDK AMKEAVSAAS EDDIFRRAGG LFGNHVSYYQ
SDSRSNFPQT FATQRPLHIN KTGNNQADTE SPSHEKLVDS TFTPSSYSST GSNANINNAN
NTALGRFPHP AGYSSTVSTV EGHGPPLSPA VRVQEAAWKL SSKRCHSRES QGATVSQDMF
PDETRSSVRL SEEVEYCSEP SLLSTDILSY QDDENRQLTC LEEDKREIQP CPKRSFLRSA
SLGRRASFHL ECLKRQKDQG GDISQKTALP LHLVHHQALA VAGLSPLLQR SHSPSTFPRP
RPTPPVTPGS RGRPLQPIPT LRLEGAESSE KLNSSFPSIH CSSWSEETTA CSGGSSMARR
ARPVSLTVPS QAGAPGRQFH GSASSLVEAV LISEGLGQFA QDPKFIEVTT QELADACDMT
IEEMENAADN ILSGGAQQSP NGTLLPFVNC RDPGQDRAVV PEDESCVYAL GRGRSEEALP
DSRSYVSNL


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