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Voltage-dependent R-type calcium channel subunit alpha-1E (Brain calcium channel II) (BII) (Calcium channel, L type, alpha-1 polypeptide, isoform 6) (Voltage-gated calcium channel subunit alpha Cav2.3)

 CAC1E_HUMAN             Reviewed;        2313 AA.
Q15878; B1AM12; B1AM13; B1AM14; Q14580; Q14581;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
14-OCT-2008, sequence version 3.
18-JUL-2018, entry version 176.
RecName: Full=Voltage-dependent R-type calcium channel subunit alpha-1E;
AltName: Full=Brain calcium channel II;
Short=BII;
AltName: Full=Calcium channel, L type, alpha-1 polypeptide, isoform 6;
AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.3;
Name=CACNA1E; Synonyms=CACH6, CACNL1A6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-1955.
TISSUE=Brain;
PubMed=7536609;
Schneider T., Wei X., Olcese R., Costantin J.L., Neely A., Palade P.,
Perez-Reyes E., Qin N., Zhou J., Crawford G.D., Smith R.G.,
Appel S.H., Stefani E., Birnbaumer M.;
"Molecular analysis and functional expression of the human type E
neuronal Ca2+ channel alpha 1 subunit.";
Recept. Channels 2:255-270(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
TISSUE=Hippocampus;
PubMed=8071363;
Williams M.E., Marubio L.M., Deal C.R., Hans M., Brust P.F.,
Philipson L.H., Miller R.J., Johnson E.C., Harpold M.M., Ellis S.B.;
"Structure and functional characterization of neuronal alpha 1E
calcium channel subtypes.";
J. Biol. Chem. 269:22347-22357(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
INTERACTION WITH CACNA1E.
PubMed=15258581; DOI=10.1038/ng1393;
Suzuki T., Delgado-Escueta A.V., Aguan K., Alonso M.E., Shi J.,
Hara Y., Nishida M., Numata T., Medina M.T., Takeuchi T., Morita R.,
Bai D., Ganesh S., Sugimoto Y., Inazawa J., Bailey J.N., Ochoa A.,
Jara-Prado A., Rasmussen A., Ramos-Peek J., Cordova S.,
Rubio-Donnadieu F., Inoue Y., Osawa M., Kaneko S., Oguni H., Mori Y.,
Yamakawa K.;
"Mutations in EFHC1 cause juvenile myoclonic epilepsy.";
Nat. Genet. 36:842-849(2004).
[5]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1867-1885.
PubMed=18400181; DOI=10.1016/j.str.2008.01.011;
Mori M.X., Vander Kooi C.W., Leahy D.J., Yue D.T.;
"Crystal structure of the CaV2 IQ domain in complex with
Ca2+/calmodulin: high-resolution mechanistic implications for channel
regulation by Ca2+.";
Structure 16:607-620(2008).
-!- 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-1E
gives rise to R-type calcium currents. R-type calcium channels
belong to the 'high-voltage activated' (HVA) group and are blocked
by nickel. They are however insensitive to dihydropyridines (DHP).
Calcium channels containing alpha-1E subunit could be involved in
the modulation of firing patterns of neurons which is important
for information processing.
-!- SUBUNIT: Interacts with EFHC1. 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. {ECO:0000269|PubMed:15258581}.
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Alpha-1E;
IsoId=Q15878-1; Sequence=Displayed;
Name=2; Synonyms=Alpha-1E-1;
IsoId=Q15878-2; Sequence=VSP_000937, VSP_024817;
Name=3; Synonyms=Alpha-1E-3;
IsoId=Q15878-3; Sequence=VSP_024817;
-!- TISSUE SPECIFICITY: Expressed in neuronal tissues and in kidney.
-!- 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.
-!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
1.A.1.11) family. CACNA1E subfamily. {ECO:0000305}.
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EMBL; L27745; AAA72125.1; -; mRNA.
EMBL; L29384; AAA59204.1; -; mRNA.
EMBL; L29385; AAA59205.1; -; mRNA.
EMBL; AL161734; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL359270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL160059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL590998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS53443.1; -. [Q15878-3]
CCDS; CCDS55664.1; -. [Q15878-1]
CCDS; CCDS55665.1; -. [Q15878-2]
PIR; A54972; A54972.
PIR; B54972; B54972.
RefSeq; NP_000712.2; NM_000721.3. [Q15878-3]
RefSeq; NP_001192222.1; NM_001205293.1. [Q15878-1]
RefSeq; NP_001192223.1; NM_001205294.1. [Q15878-2]
UniGene; Hs.437444; -.
UniGene; Hs.611396; -.
PDB; 3BXL; X-ray; 2.30 A; B=1867-1887.
PDBsum; 3BXL; -.
ProteinModelPortal; Q15878; -.
SMR; Q15878; -.
BioGrid; 107231; 2.
STRING; 9606.ENSP00000356545; -.
BindingDB; Q15878; -.
ChEMBL; CHEMBL1687682; -.
GuidetoPHARMACOLOGY; 534; -.
iPTMnet; Q15878; -.
PhosphoSitePlus; Q15878; -.
BioMuta; CACNA1E; -.
DMDM; 209572758; -.
EPD; Q15878; -.
MaxQB; Q15878; -.
PaxDb; Q15878; -.
PeptideAtlas; Q15878; -.
PRIDE; Q15878; -.
ProteomicsDB; 60800; -.
ProteomicsDB; 60801; -. [Q15878-2]
ProteomicsDB; 60802; -. [Q15878-3]
Ensembl; ENST00000358338; ENSP00000351101; ENSG00000198216. [Q15878-2]
Ensembl; ENST00000367567; ENSP00000356539; ENSG00000198216. [Q15878-3]
Ensembl; ENST00000367570; ENSP00000356542; ENSG00000198216. [Q15878-3]
Ensembl; ENST00000367573; ENSP00000356545; ENSG00000198216. [Q15878-1]
Ensembl; ENST00000621551; ENSP00000483914; ENSG00000198216. [Q15878-1]
Ensembl; ENST00000621791; ENSP00000481619; ENSG00000198216. [Q15878-2]
GeneID; 777; -.
KEGG; hsa:777; -.
UCSC; uc001gow.5; human. [Q15878-1]
CTD; 777; -.
DisGeNET; 777; -.
EuPathDB; HostDB:ENSG00000198216.10; -.
GeneCards; CACNA1E; -.
HGNC; HGNC:1392; CACNA1E.
HPA; CAB079032; -.
HPA; HPA042515; -.
MIM; 601013; gene.
neXtProt; NX_Q15878; -.
OpenTargets; ENSG00000198216; -.
PharmGKB; PA26009; -.
eggNOG; ENOG410INF5; Eukaryota.
eggNOG; ENOG410YD06; LUCA.
GeneTree; ENSGT00830000128247; -.
HOGENOM; HOG000231530; -.
HOVERGEN; HBG050763; -.
InParanoid; Q15878; -.
KO; K04852; -.
OMA; RRRHHMS; -.
OrthoDB; EOG091G0TKO; -.
PhylomeDB; Q15878; -.
TreeFam; TF312805; -.
Reactome; R-HSA-112308; Presynaptic depolarization and calcium channel opening.
Reactome; R-HSA-422356; Regulation of insulin secretion.
ChiTaRS; CACNA1E; human.
EvolutionaryTrace; Q15878; -.
GeneWiki; R-type_calcium_channel; -.
GenomeRNAi; 777; -.
PRO; PR:Q15878; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000198216; -.
CleanEx; HS_CACNA1E; -.
ExpressionAtlas; Q15878; baseline and differential.
Genevisible; Q15878; HS.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0005891; C:voltage-gated calcium channel complex; TAS:ProtInc.
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:0005245; F:voltage-gated calcium channel activity; IDA:MGI.
GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
GO; GO:0051899; P:membrane depolarization; TAS:Reactome.
GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
Gene3D; 1.20.120.350; -; 4.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR031649; GPHH_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR014873; VDCC_a1su_IQ.
InterPro; IPR005449; VDCC_R_a1su.
InterPro; IPR002077; VDCCAlpha1.
InterPro; IPR027359; Volt_channel_dom_sf.
PANTHER; PTHR10037:SF57; PTHR10037:SF57; 1.
Pfam; PF08763; Ca_chan_IQ; 1.
Pfam; PF16905; GPHH; 1.
Pfam; PF00520; Ion_trans; 4.
PRINTS; PR00167; CACHANNEL.
PRINTS; PR01633; RVDCCALPHA1.
SMART; SM01062; Ca_chan_IQ; 1.
PROSITE; PS50222; EF_HAND_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Calcium channel;
Calcium transport; Complete proteome; Disulfide bond; Glycoprotein;
Ion channel; Ion transport; Membrane; Metal-binding; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Transmembrane;
Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 2313 Voltage-dependent R-type calcium channel
subunit alpha-1E.
/FTId=PRO_0000053938.
TOPO_DOM 1 89 Cytoplasmic. {ECO:0000255}.
TRANSMEM 90 108 Helical; Name=S1 of repeat I.
TOPO_DOM 109 127 Extracellular. {ECO:0000255}.
TRANSMEM 128 146 Helical; Name=S2 of repeat I.
TOPO_DOM 147 158 Cytoplasmic. {ECO:0000255}.
TRANSMEM 159 173 Helical; Name=S3 of repeat I.
TOPO_DOM 174 185 Extracellular. {ECO:0000255}.
TRANSMEM 186 205 Helical; Name=S4 of repeat I.
TOPO_DOM 206 223 Cytoplasmic. {ECO:0000255}.
TRANSMEM 224 244 Helical; Name=S5 of repeat I.
TOPO_DOM 245 326 Extracellular. {ECO:0000255}.
TRANSMEM 327 350 Helical; Name=S6 of repeat I.
TOPO_DOM 351 476 Cytoplasmic. {ECO:0000255}.
TRANSMEM 477 496 Helical; Name=S1 of repeat II.
TOPO_DOM 497 509 Extracellular. {ECO:0000255}.
TRANSMEM 510 529 Helical; Name=S2 of repeat II.
TOPO_DOM 530 538 Cytoplasmic. {ECO:0000255}.
TRANSMEM 539 557 Helical; Name=S3 of repeat II.
TOPO_DOM 558 567 Extracellular. {ECO:0000255}.
TRANSMEM 568 586 Helical; Name=S4 of repeat II.
TOPO_DOM 587 605 Cytoplasmic. {ECO:0000255}.
TRANSMEM 606 625 Helical; Name=S5 of repeat II.
TOPO_DOM 626 678 Extracellular. {ECO:0000255}.
TRANSMEM 679 703 Helical; Name=S6 of repeat II.
TOPO_DOM 704 1148 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1149 1165 Helical; Name=S1 of repeat III.
TOPO_DOM 1166 1189 Extracellular. {ECO:0000255}.
TRANSMEM 1190 1209 Helical; Name=S2 of repeat III.
TOPO_DOM 1210 1217 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1218 1240 Helical; Name=S3 of repeat III.
TOPO_DOM 1241 1254 Extracellular. {ECO:0000255}.
TRANSMEM 1255 1272 Helical; Name=S4 of repeat III.
TOPO_DOM 1273 1291 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1292 1311 Helical; Name=S5 of repeat III.
TOPO_DOM 1312 1398 Extracellular. {ECO:0000255}.
TRANSMEM 1399 1422 Helical; Name=S6 of repeat III.
TOPO_DOM 1423 1479 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1480 1498 Helical; Name=S1 of repeat IV.
TOPO_DOM 1499 1513 Extracellular. {ECO:0000255}.
TRANSMEM 1514 1533 Helical; Name=S2 of repeat IV.
TOPO_DOM 1534 1541 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1542 1560 Helical; Name=S3 of repeat IV.
TOPO_DOM 1561 1571 Extracellular. {ECO:0000255}.
TRANSMEM 1572 1590 Helical; Name=S4 of repeat IV.
TOPO_DOM 1591 1609 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1610 1629 Helical; Name=S5 of repeat IV.
TOPO_DOM 1630 1698 Extracellular. {ECO:0000255}.
TRANSMEM 1699 1724 Helical; Name=S6 of repeat IV.
TOPO_DOM 1725 2313 Cytoplasmic. {ECO:0000255}.
REPEAT 76 354 I.
REPEAT 462 706 II.
REPEAT 1140 1426 III.
REPEAT 1463 1726 IV.
DOMAIN 1739 1774 EF-hand. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 426 437 {ECO:0000255|PROSITE-ProRule:PRU00448}.
CA_BIND 1752 1763 {ECO:0000255|PROSITE-ProRule:PRU00448}.
REGION 374 391 Binding to the beta subunit.
{ECO:0000250}.
COMPBIAS 716 721 Poly-Glu.
COMPBIAS 748 753 Poly-Arg.
COMPBIAS 767 772 Poly-Arg.
COMPBIAS 1228 1231 Poly-Val.
COMPBIAS 2284 2288 Poly-Arg.
SITE 309 309 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 657 657 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1372 1372 Calcium ion selectivity and permeability.
{ECO:0000250}.
SITE 1663 1663 Calcium ion selectivity and permeability.
{ECO:0000250}.
MOD_RES 14 14 Phosphoserine.
{ECO:0000250|UniProtKB:Q61290}.
MOD_RES 19 19 Phosphoserine.
{ECO:0000250|UniProtKB:Q61290}.
MOD_RES 427 427 Phosphoserine.
{ECO:0000250|UniProtKB:Q61290}.
MOD_RES 440 440 Phosphothreonine.
{ECO:0000250|UniProtKB:Q61290}.
MOD_RES 736 736 Phosphoserine.
{ECO:0000250|UniProtKB:Q07652}.
MOD_RES 745 745 Phosphoserine.
{ECO:0000250|UniProtKB:Q61290}.
MOD_RES 793 793 Phosphoserine.
{ECO:0000250|UniProtKB:Q07652}.
MOD_RES 815 815 Phosphoserine.
{ECO:0000250|UniProtKB:Q61290}.
MOD_RES 855 855 Phosphoserine.
{ECO:0000250|UniProtKB:Q61290}.
MOD_RES 947 947 Phosphoserine.
{ECO:0000250|UniProtKB:Q07652}.
MOD_RES 1097 1097 Phosphoserine.
{ECO:0000250|UniProtKB:Q07652}.
MOD_RES 1734 1734 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 2094 2094 Phosphoserine.
{ECO:0000250|UniProtKB:Q61290}.
MOD_RES 2113 2113 Phosphoserine.
{ECO:0000250|UniProtKB:Q07652}.
CARBOHYD 254 254 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1566 1566 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1571 1571 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 748 766 Missing (in isoform 2).
{ECO:0000303|PubMed:8071363}.
/FTId=VSP_000937.
VAR_SEQ 1967 2009 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:8071363}.
/FTId=VSP_024817.
VARIANT 859 859 D -> E (in dbSNP:rs35737760).
/FTId=VAR_031912.
VARIANT 1955 1955 A -> T (in dbSNP:rs704326).
{ECO:0000269|PubMed:7536609}.
/FTId=VAR_046996.
CONFLICT 648 648 M -> I (in Ref. 1; AAA72125).
{ECO:0000305}.
CONFLICT 836 838 LAL -> WP (in Ref. 1; AAA72125).
{ECO:0000305}.
CONFLICT 2077 2077 R -> P (in Ref. 2; AAA59204/AAA59205).
{ECO:0000305}.
CONFLICT 2084 2084 G -> R (in Ref. 2; AAA59204/AAA59205).
{ECO:0000305}.
CONFLICT 2206 2206 C -> W (in Ref. 2; AAA59204/AAA59205).
{ECO:0000305}.
CONFLICT 2219 2219 S -> R (in Ref. 2; AAA59204/AAA59205).
{ECO:0000305}.
CONFLICT 2245 2245 G -> V (in Ref. 2; AAA59204/AAA59205).
{ECO:0000305}.
HELIX 1868 1882 {ECO:0000244|PDB:3BXL}.
SEQUENCE 2313 AA; 261731 MW; CCC7F309C27C42F1 CRC64;
MARFGEAVVA RPGSGDGDSD QSRNRQGTPV PASGQAAAYK QTKAQRARTM ALYNPIPVRQ
NCFTVNRSLF IFGEDNIVRK YAKKLIDWPP FEYMILATII ANCIVLALEQ HLPEDDKTPM
SRRLEKTEPY FIGIFCFEAG IKIVALGFIF HKGSYLRNGW NVMDFIVVLS GILATAGTHF
NTHVDLRTLR AVRVLRPLKL VSGIPSLQIV LKSIMKAMVP LLQIGLLLFF AILMFAIIGL
EFYSGKLHRA CFMNNSGILE GFDPPHPCGV QGCPAGYECK DWIGPNDGIT QFDNILFAVL
TVFQCITMEG WTTVLYNTND ALGATWNWLY FIPLIIIGSF FVLNLVLGVL SGEFAKERER
VENRRAFMKL RRQQQIEREL NGYRAWIDKA EEVMLAEENK NAGTSALEVL RRATIKRSRT
EAMTRDSSDE HCVDISSVGT PLARASIKSA KVDGVSYFRH KERLLRISIR HMVKSQVFYW
IVLSLVALNT ACVAIVHHNQ PQWLTHLLYY AEFLFLGLFL LEMSLKMYGM GPRLYFHSSF
NCFDFGVTVG SIFEVVWAIF RPGTSFGISV LRALRLLRIF KITKYWASLR NLVVSLMSSM
KSIISLLFLL FLFIVVFALL GMQLFGGRFN FNDGTPSANF DTFPAAIMTV FQILTGEDWN
EVMYNGIRSQ GGVSSGMWSA IYFIVLTLFG NYTLLNVFLA IAVDNLANAQ ELTKDEQEEE
EAFNQKHALQ KAKEVSPMSA PNMPSIERDR RRRHHMSMWE PRSSHLRERR RRHHMSVWEQ
RTSQLRKHMQ MSSQEALNRE EAPTMNPLNP LNPLSSLNPL NAHPSLYRRP RAIEGLALGL
ALEKFEEERI SRGGSLKGDG GDRSSALDNQ RTPLSLGQRE PPWLARPCHG NCDPTQQEAG
GGEAVVTFED RARHRQSQRR SRHRRVRTEG KESSSASRSR SASQERSLDE AMPTEGEKDH
ELRGNHGAKE PTIQEERAQD LRRTNSLMVS RGSGLAGGLD EADTPLVLPH PELEVGKHVV
LTEQEPEGSS EQALLGNVQL DMGRVISQSE PDLSCITANT DKATTESTSV TVAIPDVDPL
VDSTVVHISN KTDGEASPLK EAEIREDEEE VEKKKQKKEK RETGKAMVPH SSMFIFSTTN
PIRRACHYIV NLRYFEMCIL LVIAASSIAL AAEDPVLTNS ERNKVLRYFD YVFTGVFTFE
MVIKMIDQGL ILQDGSYFRD LWNILDFVVV VGALVAFALA NALGTNKGRD IKTIKSLRVL
RVLRPLKTIK RLPKLKAVFD CVVTSLKNVF NILIVYKLFM FIFAVIAVQL FKGKFFYCTD
SSKDTEKECI GNYVDHEKNK MEVKGREWKR HEFHYDNIIW ALLTLFTVST GEGWPQVLQH
SVDVTEEDRG PSRSNRMEMS IFYVVYFVVF PFFFVNIFVA LIIITFQEQG DKMMEECSLE
KNERACIDFA ISAKPLTRYM PQNRHTFQYR VWHFVVSPSF EYTIMAMIAL NTVVLMMKYY
SAPCTYELAL KYLNIAFTMV FSLECVLKVI AFGFLNYFRD TWNIFDFITV IGSITEIILT
DSKLVNTSGF NMSFLKLFRA ARLIKLLRQG YTIRILLWTF VQSFKALPYV CLLIAMLFFI
YAIIGMQVFG NIKLDEESHI NRHNNFRSFF GSLMLLFRSA TGEAWQEIML SCLGEKGCEP
DTTAPSGQNE NERCGTDLAY VYFVSFIFFC SFLMLNLFVA VIMDNFEYLT RDSSILGPHH
LDEFVRVWAE YDRAACGRIH YTEMYEMLTL MSPPLGLGKR CPSKVAYKRL VLMNMPVAED
MTVHFTSTLM ALIRTALDIK IAKGGADRQQ LDSELQKETL AIWPHLSQKM LDLLVPMPKA
SDLTVGKIYA AMMIMDYYKQ SKVKKQRQQL EEQKNAPMFQ RMEPSSLPQE IIANAKALPY
LQQDPVSGLS GRSGYPSMSP LSPQDIFQLA CMDPADDGQF QERQSLEPEV SELKSVQPSN
HGIYLPSDTQ EHAGSGRASS MPRLTVDPQV VTDPSSMRRS FSTIRDKRSN SSWLEEFSME
RSSENTYKSR RRSYHSSLRL SAHRLNSDSG HKSDTHRSGG RERGRSKERK HLLSPDVSRC
NSEERGTQAD WESPERRQSR SPSEGRSQTP NRQGTGSLSE SSIPSVSDTS TPRRSRRQLP
PVPPKPRPLL SYSSLIRHAG SISPPADGSE EGSPLTSQAL ESNNACLTES SNSPHPQQSQ
HASPQRYISE PYLALHEDSH ASDCGEEETL TFEAAVATSL GRSNTIGSAP PLRHSWQMPN
GHYRRRRRGG PGPGMMCGAV NNLLSDTEED DKC


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