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Voltage-dependent N-type calcium channel subunit alpha-1B (Brain calcium channel III) (BIII) (Calcium channel, L type, alpha-1 polypeptide isoform 5) (Voltage-gated calcium channel subunit alpha Cav2.2)

 CAC1B_HUMAN             Reviewed;        2339 AA.
Q00975; B1AQK5;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
07-JUN-2017, entry version 168.
RecName: Full=Voltage-dependent N-type calcium channel subunit alpha-1B;
AltName: Full=Brain calcium channel III;
Short=BIII;
AltName: Full=Calcium channel, L type, alpha-1 polypeptide isoform 5;
AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.2;
Name=CACNA1B; Synonyms=CACH5, CACNL1A5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-1B-1 AND ALPHA-1B-2).
TISSUE=Brain;
PubMed=1321501; DOI=10.1126/science.1321501;
Williams M.E., Brust P.F., Feldman D.H., Patthi S., Simerson S.,
Maroufi A., McCue A.F., Velicelebi G., Ellis S.B., Harpold M.M.;
"Structure and functional expression of an omega-conotoxin-sensitive
human N-type calcium channel.";
Science 257:389-395(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-94.
TISSUE=Lung fibroblast;
PubMed=9030575; DOI=10.1074/jbc.272.8.5098;
Kim D.S., Jung H.-H., Park S.-H., Chin H.;
"Isolation and characterization of the 5'-upstream region of the human
N-type calcium channel alpha1B subunit gene. Chromosomal localization
and promoter analysis.";
J. Biol. Chem. 272:5098-5104(1997).
[4]
INVOLVEMENT IN DYT23, VARIANT DYT23 HIS-1389, AND CHARACTERIZATION OF
VARIANT DYT23 HIS-1389.
PubMed=25296916; DOI=10.1093/hmg/ddu513;
Groen J.L., Andrade A., Ritz K., Jalalzadeh H., Haagmans M.,
Bradley T.E., Jongejan A., Verbeek D.S., Nuernberg P., Denome S.,
Hennekam R.C., Lipscombe D., Baas F., Tijssen M.A.;
"CACNA1B mutation is linked to unique myoclonus-dystonia syndrome.";
Hum. Mol. Genet. 24:987-993(2015).
-!- 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-1B
gives rise to N-type calcium currents. N-type calcium channels
belong to the 'high-voltage activated' (HVA) group and are blocked
by omega-conotoxin-GVIA (omega-CTx-GVIA) and by omega-agatoxin-
IIIA (omega-Aga-IIIA). They are however insensitive to
dihydropyridines (DHP), and omega-agatoxin-IVA (omega-Aga-IVA).
Calcium channels containing alpha-1B subunit may play a role in
directed migration of immature neurons.
-!- SUBUNIT: Multisubunit complex 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 with RIMS1. Interacts with FMR1 (via
C-terminus); this interaction induces a deacrease in the number of
presynaptic functional CACNA1B channels at the cell surface.
{ECO:0000250|UniProtKB:O55017}.
-!- INTERACTION:
P20650:Ppm1a (xeno); NbExp=3; IntAct=EBI-1055161, EBI-7491743;
P28702:RXRB; NbExp=3; IntAct=EBI-1055161, EBI-748576;
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Alpha-1B-1;
IsoId=Q00975-1; Sequence=Displayed;
Name=Alpha-1B-2;
IsoId=Q00975-2; Sequence=VSP_000882;
Note=Ref.1 (AAA51898) sequence is in conflict in position:
2215:L->R. {ECO:0000305};
-!- TISSUE SPECIFICITY: Isoform Alpha-1b-1 and isoform Alpha-1b-2 are
expressed in the central nervous system, but not in skeletal
muscle or aorta.
-!- 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.
-!- PTM: Phosphorylated in vitro by CaM-kinase II, PKA, PKC and CGPK.
{ECO:0000250}.
-!- DISEASE: Dystonia 23 (DYT23) [MIM:614860]: A form of dystonia, a
disorder defined by the presence of sustained involuntary muscle
contraction, often leading to abnormal postures. DYT23 is an
autosomal dominant dystonia affecting the face, neck, limbs. Some
DYT23 patients manifest generalized myoclonus in addition to
progressive action-induced multifocal dystonia.
{ECO:0000269|PubMed:25296916}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
1.A.1.11) family. CACNA1B subfamily. {ECO:0000305}.
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EMBL; M94172; AAA51897.1; -; mRNA.
EMBL; M94173; AAA51898.1; -; mRNA.
EMBL; AL591424; CAI40687.1; -; Genomic_DNA.
EMBL; AL772363; CAI40687.1; JOINED; Genomic_DNA.
EMBL; AL772363; CAI17144.1; -; Genomic_DNA.
EMBL; AL591424; CAI17144.1; JOINED; Genomic_DNA.
EMBL; U76666; AAC51138.1; -; Genomic_DNA.
CCDS; CCDS59522.1; -. [Q00975-1]
CCDS; CCDS59523.1; -. [Q00975-2]
PIR; A42566; A42566.
PIR; T45115; T45115.
RefSeq; NP_000709.1; NM_000718.3. [Q00975-1]
RefSeq; NP_001230741.1; NM_001243812.1. [Q00975-2]
UniGene; Hs.495522; -.
PDB; 2LCM; NMR; -; A=1242-1269.
PDBsum; 2LCM; -.
ProteinModelPortal; Q00975; -.
SMR; Q00975; -.
BioGrid; 107228; 7.
IntAct; Q00975; 7.
MINT; MINT-102376; -.
STRING; 9606.ENSP00000360406; -.
BindingDB; Q00975; -.
ChEMBL; CHEMBL4478; -.
DrugBank; DB08838; Agmatine.
DrugBank; DB00381; Amlodipine.
DrugBank; DB00996; Gabapentin.
DrugBank; DB01202; Levetiracetam.
DrugBank; DB00421; Spironolactone.
DrugBank; DB00661; Verapamil.
GuidetoPHARMACOLOGY; 533; -.
iPTMnet; Q00975; -.
PhosphoSitePlus; Q00975; -.
BioMuta; CACNA1B; -.
DMDM; 1705854; -.
EPD; Q00975; -.
PaxDb; Q00975; -.
PeptideAtlas; Q00975; -.
PRIDE; Q00975; -.
Ensembl; ENST00000277551; ENSP00000277551; ENSG00000148408. [Q00975-2]
Ensembl; ENST00000371372; ENSP00000360423; ENSG00000148408. [Q00975-1]
GeneID; 774; -.
KEGG; hsa:774; -.
UCSC; uc064xny.1; human. [Q00975-1]
CTD; 774; -.
DisGeNET; 774; -.
GeneCards; CACNA1B; -.
HGNC; HGNC:1389; CACNA1B.
HPA; HPA044347; -.
MalaCards; CACNA1B; -.
MIM; 601012; gene.
MIM; 614860; phenotype.
neXtProt; NX_Q00975; -.
OpenTargets; ENSG00000148408; -.
PharmGKB; PA26008; -.
eggNOG; KOG2301; Eukaryota.
eggNOG; ENOG410XNP6; LUCA.
GeneTree; ENSGT00830000128247; -.
HOGENOM; HOG000231530; -.
HOVERGEN; HBG050763; -.
InParanoid; Q00975; -.
KO; K04849; -.
PhylomeDB; Q00975; -.
Reactome; R-HSA-112308; Presynaptic depolarization and calcium channel opening.
SIGNOR; Q00975; -.
ChiTaRS; CACNA1B; human.
GeneWiki; N-type_calcium_channel; -.
GenomeRNAi; 774; -.
PRO; PR:Q00975; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000148408; -.
CleanEx; HS_CACNA1B; -.
ExpressionAtlas; Q00975; baseline and differential.
Genevisible; Q00975; HS.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0098793; C:presynapse; IEA:GOC.
GO; GO:0005891; C:voltage-gated calcium channel complex; TAS:ProtInc.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005262; F:calcium channel activity; TAS:Reactome.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0008331; F:high voltage-gated calcium channel activity; IBA:GO_Central.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0005245; F:voltage-gated calcium channel activity; TAS:ProtInc.
GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
GO; GO:0051899; P:membrane depolarization; TAS:Reactome.
GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
GO; GO:0007269; P:neurotransmitter secretion; IEA:Ensembl.
GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
GO; GO:0051924; P:regulation of calcium ion transport; IEA:Ensembl.
GO; GO:0008016; P:regulation of heart contraction; IEA:Ensembl.
GO; GO:0048265; P:response to pain; IEA:Ensembl.
GO; GO:0006810; P:transport; TAS:ProtInc.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR031649; GPHH_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR014873; VDCC_a1su_IQ.
InterPro; IPR005447; VDCC_N_a1su.
InterPro; IPR002077; VDCCAlpha1.
PANTHER; PTHR10037:SF246; PTHR10037:SF246; 1.
Pfam; PF08763; Ca_chan_IQ; 1.
Pfam; PF16905; GPHH; 1.
Pfam; PF00520; Ion_trans; 4.
PRINTS; PR00167; CACHANNEL.
PRINTS; PR01631; NVDCCALPHA1.
SMART; SM01062; Ca_chan_IQ; 1.
PROSITE; PS50222; EF_HAND_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Calcium;
Calcium channel; Calcium transport; Complete proteome;
Congenital generalized lipodystrophy; Disease mutation;
Disulfide bond; Dystonia; Glycoprotein; Ion channel; Ion transport;
Membrane; Mental retardation; Metal-binding; Methylation;
Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; Transmembrane; Transmembrane helix; Transport;
Voltage-gated channel.
CHAIN 1 2339 Voltage-dependent N-type calcium channel
subunit alpha-1B.
/FTId=PRO_0000053921.
TOPO_DOM 1 95 Cytoplasmic. {ECO:0000255}.
TRANSMEM 96 114 Helical; Name=S1 of repeat I.
{ECO:0000255}.
TOPO_DOM 115 132 Extracellular. {ECO:0000255}.
TRANSMEM 133 152 Helical; Name=S2 of repeat I.
{ECO:0000255}.
TOPO_DOM 153 163 Cytoplasmic. {ECO:0000255}.
TRANSMEM 164 183 Helical; Name=S3 of repeat I.
{ECO:0000255}.
TOPO_DOM 184 187 Extracellular. {ECO:0000255}.
TRANSMEM 188 206 Helical; Name=S4 of repeat I.
{ECO:0000255}.
TOPO_DOM 207 225 Cytoplasmic. {ECO:0000255}.
TRANSMEM 226 245 Helical; Name=S5 of repeat I.
{ECO:0000255}.
TOPO_DOM 246 331 Extracellular. {ECO:0000255}.
TRANSMEM 332 356 Helical; Name=S6 of repeat I.
{ECO:0000255}.
TOPO_DOM 357 482 Cytoplasmic. {ECO:0000255}.
TRANSMEM 483 501 Helical; Name=S1 of repeat II.
{ECO:0000255}.
TOPO_DOM 502 516 Extracellular. {ECO:0000255}.
TRANSMEM 517 536 Helical; Name=S2 of repeat II.
{ECO:0000255}.
TOPO_DOM 537 544 Cytoplasmic. {ECO:0000255}.
TRANSMEM 545 562 Helical; Name=S3 of repeat II.
{ECO:0000255}.
TOPO_DOM 563 573 Extracellular. {ECO:0000255}.
TRANSMEM 574 592 Helical; Name=S4 of repeat II.
{ECO:0000255}.
TOPO_DOM 593 611 Cytoplasmic. {ECO:0000255}.
TRANSMEM 612 631 Helical; Name=S5 of repeat II.
{ECO:0000255}.
TOPO_DOM 632 684 Extracellular. {ECO:0000255}.
TRANSMEM 685 709 Helical; Name=S6 of repeat II.
{ECO:0000255}.
TOPO_DOM 710 1151 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1152 1169 Helical; Name=S1 of repeat III.
{ECO:0000255}.
TOPO_DOM 1170 1185 Extracellular. {ECO:0000255}.
TRANSMEM 1186 1205 Helical; Name=S2 of repeat III.
{ECO:0000255}.
TOPO_DOM 1206 1217 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1218 1236 Helical; Name=S3 of repeat III.
{ECO:0000255}.
TOPO_DOM 1237 1246 Extracellular. {ECO:0000255}.
TRANSMEM 1247 1265 Helical; Name=S4 of repeat III.
{ECO:0000255}.
TOPO_DOM 1266 1284 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1285 1304 Helical; Name=S5 of repeat III.
{ECO:0000255}.
TOPO_DOM 1305 1391 Extracellular. {ECO:0000255}.
TRANSMEM 1392 1416 Helical; Name=S6 of repeat III.
{ECO:0000255}.
TOPO_DOM 1417 1471 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1472 1490 Helical; Name=S1 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1491 1505 Extracellular. {ECO:0000255}.
TRANSMEM 1506 1525 Helical; Name=S2 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1526 1533 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1534 1552 Helical; Name=S3 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1553 1563 Extracellular. {ECO:0000255}.
TRANSMEM 1564 1582 Helical; Name=S4 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1583 1601 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1602 1621 Helical; Name=S5 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1622 1683 Extracellular. {ECO:0000255}.
TRANSMEM 1684 1708 Helical; Name=S6 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1709 2339 Cytoplasmic. {ECO:0000255}.
REPEAT 82 359 I.
REPEAT 468 712 II.
REPEAT 1137 1419 III.
REPEAT 1456 1711 IV.
DOMAIN 1724 1759 EF-hand. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
NP_BIND 451 458 ATP. {ECO:0000255}.
CA_BIND 1737 1748 {ECO:0000255|PROSITE-ProRule:PRU00448}.
REGION 379 396 Binding to the beta subunit.
{ECO:0000250}.
COMPBIAS 2050 2054 Poly-His.
COMPBIAS 2118 2122 Poly-Ser.
SITE 314 314 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 663 663 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1365 1365 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1655 1655 Calcium ion selectivity and permeability.
{ECO:0000250}.
MOD_RES 22 22 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:O55017}.
MOD_RES 411 411 Phosphoserine.
{ECO:0000250|UniProtKB:O55017}.
MOD_RES 745 745 Phosphoserine.
{ECO:0000250|UniProtKB:O55017}.
MOD_RES 748 748 Phosphoserine.
{ECO:0000250|UniProtKB:O55017}.
MOD_RES 783 783 Phosphoserine.
{ECO:0000250|UniProtKB:O55017}.
MOD_RES 1069 1069 Phosphoserine.
{ECO:0000250|UniProtKB:O55017}.
MOD_RES 1719 1719 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 2066 2066 Phosphoserine.
{ECO:0000250|UniProtKB:O55017}.
MOD_RES 2224 2224 Phosphoserine.
{ECO:0000250|UniProtKB:O55017}.
MOD_RES 2233 2233 Phosphoserine.
{ECO:0000250|UniProtKB:O55017}.
MOD_RES 2256 2256 Phosphoserine.
{ECO:0000250|UniProtKB:O55017}.
CARBOHYD 256 256 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1563 1563 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1675 1675 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 2164 2339 GSGSVNGSPLLSTSGASTPGRGGRRQLPQTPLTPRPSITYK
TANSSPIHFAGAQTSLPAFSPGRLSRGLSEHNALLQRDPLS
QPLAPGSRIGSDPYLGQRLDSEASVHALPEDTLTFEEAVAT
NSGRSSRTSYVSSLTSQSHPLRRVPNGYHCTLGLSSGGRAR
HSYHHPDQDHWC -> AGSAVGFPNTTPCCRETPSASPWPL
ALELALTLTWGSVWTVRPLSTPCLRTLSLSRRLWPPTRAAP
PGLPTCPP (in isoform Alpha-1B-2).
{ECO:0000303|PubMed:1321501}.
/FTId=VSP_000882.
VARIANT 167 167 N -> K (in dbSNP:rs4422842).
/FTId=VAR_048741.
VARIANT 862 862 A -> S (in dbSNP:rs7873074).
/FTId=VAR_061100.
VARIANT 996 996 T -> A (in dbSNP:rs11137342).
/FTId=VAR_061101.
VARIANT 1389 1389 R -> H (in DYT23; gain of function
mutation; dbSNP:rs184841813).
{ECO:0000269|PubMed:25296916}.
/FTId=VAR_073432.
VARIANT 1436 1436 E -> K (in dbSNP:rs12377346).
/FTId=VAR_048742.
VARIANT 1500 1500 E -> K (in dbSNP:rs12377346).
/FTId=VAR_048743.
HELIX 1244 1263 {ECO:0000244|PDB:2LCM}.
TURN 1264 1266 {ECO:0000244|PDB:2LCM}.
SEQUENCE 2339 AA; 262496 MW; 17A45C6D1E76B39D CRC64;
MVRFGDELGG RYGGPGGGER ARGGGAGGAG GPGPGGLQPG QRVLYKQSIA QRARTMALYN
PIPVKQNCFT VNRSLFVFSE DNVVRKYAKR ITEWPPFEYM ILATIIANCI VLALEQHLPD
GDKTPMSERL DDTEPYFIGI FCFEAGIKII ALGFVFHKGS YLRNGWNVMD FVVVLTGILA
TAGTDFDLRT LRAVRVLRPL KLVSGIPSLQ VVLKSIMKAM VPLLQIGLLL FFAILMFAII
GLEFYMGKFH KACFPNSTDA EPVGDFPCGK EAPARLCEGD TECREYWPGP NFGITNFDNI
LFAILTVFQC ITMEGWTDIL YNTNDAAGNT WNWLYFIPLI IIGSFFMLNL VLGVLSGEFA
KERERVENRR AFLKLRRQQQ IERELNGYLE WIFKAEEVML AEEDRNAEEK SPLDVLKRAA
TKKSRNDLIH AEEGEDRFAD LCAVGSPFAR ASLKSGKTES SSYFRRKEKM FRFFIRRMVK
AQSFYWVVLC VVALNTLCVA MVHYNQPRRL TTTLYFAEFV FLGLFLTEMS LKMYGLGPRS
YFRSSFNCFD FGVIVGSVFE VVWAAIKPGS SFGISVLRAL RLLRIFKVTK YWSSLRNLVV
SLLNSMKSII SLLFLLFLFI VVFALLGMQL FGGQFNFQDE TPTTNFDTFP AAILTVFQIL
TGEDWNAVMY HGIESQGGVS KGMFSSFYFI VLTLFGNYTL LNVFLAIAVD NLANAQELTK
DEEEMEEAAN QKLALQKAKE VAEVSPMSAA NISIAARQQN SAKARSVWEQ RASQLRLQNL
RASCEALYSE MDPEERLRFA TTRHLRPDMK THLDRPLVVE LGRDGARGPV GGKARPEAAE
APEGVDPPRR HHRHRDKDKT PAAGDQDRAE APKAESGEPG AREERPRPHR SHSKEAAGPP
EARSERGRGP GPEGGRRHHR RGSPEEAAER EPRRHRAHRH QDPSKECAGA KGERRARHRG
GPRAGPREAE SGEEPARRHR ARHKAQPAHE AVEKETTEKE ATEKEAEIVE ADKEKELRNH
QPREPHCDLE TSGTVTVGPM HTLPSTCLQK VEEQPEDADN QRNVTRMGSQ PPDPNTIVHI
PVMLTGPLGE ATVVPSGNVD LESQAEGKKE VEADDVMRSG PRPIVPYSSM FCLSPTNLLR
RFCHYIVTMR YFEVVILVVI ALSSIALAAE DPVRTDSPRN NALKYLDYIF TGVFTFEMVI
KMIDLGLLLH PGAYFRDLWN ILDFIVVSGA LVAFAFSGSK GKDINTIKSL RVLRVLRPLK
TIKRLPKLKA VFDCVVNSLK NVLNILIVYM LFMFIFAVIA VQLFKGKFFY CTDESKELER
DCRGQYLDYE KEEVEAQPRQ WKKYDFHYDN VLWALLTLFT VSTGEGWPMV LKHSVDATYE
EQGPSPGYRM ELSIFYVVYF VVFPFFFVNI FVALIIITFQ EQGDKVMSEC SLEKNERACI
DFAISAKPLT RYMPQNRQSF QYKTWTFVVS PPFEYFIMAM IALNTVVLMM KFYDAPYEYE
LMLKCLNIVF TSMFSMECVL KIIAFGVLNY FRDAWNVFDF VTVLGSITDI LVTEIAETNN
FINLSFLRLF RAARLIKLLR QGYTIRILLW TFVQSFKALP YVCLLIAMLF FIYAIIGMQV
FGNIALDDDT SINRHNNFRT FLQALMLLFR SATGEAWHEI MLSCLSNQAC DEQANATECG
SDFAYFYFVS FIFLCSFLML NLFVAVIMDN FEYLTRDSSI LGPHHLDEFI RVWAEYDPAA
CGRISYNDMF EMLKHMSPPL GLGKKCPARV AYKRLVRMNM PISNEDMTVH FTSTLMALIR
TALEIKLAPA GTKQHQCDAE LRKEISVVWA NLPQKTLDLL VPPHKPDEMT VGKVYAALMI
FDFYKQNKTT RDQMQQAPGG LSQMGPVSLF HPLKATLEQT QPAVLRGARV FLRQKSSTSL
SNGGAIQNQE SGIKESVSWG TQRTQDAPHE ARPPLERGHS TEIPVGRSGA LAVDVQMQSI
TRRGPDGEPQ PGLESQGRAA SMPRLAAETQ PVTDASPMKR SISTLAQRPR GTHLCSTTPD
RPPPSQASSH HHHHRCHRRR DRKQRSLEKG PSLSADMDGA PSSAVGPGLP PGEGPTGCRR
ERERRQERGR SQERRQPSSS SSEKQRFYSC DRFGGREPPK PKPSLSSHPT SPTAGQEPGP
HPQGSGSVNG SPLLSTSGAS TPGRGGRRQL PQTPLTPRPS ITYKTANSSP IHFAGAQTSL
PAFSPGRLSR GLSEHNALLQ RDPLSQPLAP GSRIGSDPYL GQRLDSEASV HALPEDTLTF
EEAVATNSGR SSRTSYVSSL TSQSHPLRRV PNGYHCTLGL SSGGRARHSY HHPDQDHWC


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