CAC1E_MOUSE
ID CAC1E_MOUSE Reviewed; 2272 AA.
AC Q61290;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Voltage-dependent R-type calcium channel subunit alpha-1E;
DE AltName: Full=Brain calcium channel II;
DE Short=BII;
DE AltName: Full=Calcium channel, L type, alpha-1 polypeptide, isoform 6;
DE AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.3;
GN Name=Cacna1e; Synonyms=Cach6, Cacnl1a6, Cchra1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=8071363; DOI=10.1016/s0021-9258(17)31796-9;
RA Williams M.E., Marubio L.M., Deal C.R., Hans M., Brust P.F.,
RA Philipson L.H., Miller R.J., Johnson E.C., Harpold M.M., Ellis S.B.;
RT "Structure and functional characterization of neuronal alpha 1E calcium
RT channel subtypes.";
RL J. Biol. Chem. 269:22347-22357(1994).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-20; SER-428; THR-441;
RP SER-746; SER-816; SER-856 AND SER-2054, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry
CC of calcium ions into excitable cells and are also involved in a variety
CC of calcium-dependent processes, including muscle contraction, hormone
CC or neurotransmitter release, gene expression, cell motility, cell
CC division and cell death. The isoform alpha-1E gives rise to R-type
CC calcium currents. R-type calcium channels belong to the 'high-voltage
CC activated' (HVA) group and are blocked by nickel. They are however
CC insensitive to dihydropyridines (DHP). Calcium channels containing
CC alpha-1E subunit could be involved in the modulation of firing patterns
CC of neurons which is important for information processing.
CC -!- SUBUNIT: Interacts with EFHC1. Voltage-dependent calcium channels are
CC multisubunit complexes, consisting of alpha-1, alpha-2, beta and delta
CC subunits in a 1:1:1:1 ratio. The channel activity is directed by the
CC pore-forming and voltage-sensitive alpha-1 subunit. In many cases, this
CC subunit is sufficient to generate voltage-sensitive calcium channel
CC activity. The auxiliary subunits beta and alpha-2/delta linked by a
CC disulfide bridge regulate the channel activity.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in neuronal tissues, retina, spleen, and
CC pancreatic islet cells.
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.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. CACNA1E subfamily. {ECO:0000305}.
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DR EMBL; L29346; AAA59206.1; -; mRNA.
DR PIR; C54972; C54972.
DR AlphaFoldDB; Q61290; -.
DR SMR; Q61290; -.
DR IntAct; Q61290; 7.
DR MINT; Q61290; -.
DR STRING; 10090.ENSMUSP00000140937; -.
DR TCDB; 1.A.1.11.3; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; Q61290; 3 sites.
DR iPTMnet; Q61290; -.
DR PhosphoSitePlus; Q61290; -.
DR EPD; Q61290; -.
DR MaxQB; Q61290; -.
DR PaxDb; Q61290; -.
DR PRIDE; Q61290; -.
DR ProteomicsDB; 273884; -.
DR MGI; MGI:106217; Cacna1e.
DR eggNOG; KOG2301; Eukaryota.
DR InParanoid; Q61290; -.
DR PhylomeDB; Q61290; -.
DR Reactome; R-MMU-112308; Presynaptic depolarization and calcium channel opening.
DR Reactome; R-MMU-422356; Regulation of insulin secretion.
DR PRO; PR:Q61290; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q61290; protein.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008331; F:high voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IMP:MGI.
DR GO; GO:0099626; F:voltage-gated calcium channel activity involved in regulation of presynaptic cytosolic calcium levels; ISO:MGI.
DR GO; GO:0022843; F:voltage-gated cation channel activity; ISO:MGI.
DR GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR GO; GO:0048266; P:behavioral response to pain; IMP:MGI.
DR GO; GO:0070509; P:calcium ion import; ISO:MGI.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IMP:MGI.
DR GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0042596; P:fear response; IMP:MGI.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0050877; P:nervous system process; IMP:MGI.
DR GO; GO:0002027; P:regulation of heart rate; IMP:MGI.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:MGI.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0090273; P:regulation of somatostatin secretion; IMP:MGI.
DR GO; GO:0048265; P:response to pain; IMP:MGI.
DR GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR GO; GO:0019226; P:transmission of nerve impulse; IMP:MGI.
DR GO; GO:0008542; P:visual learning; IMP:MGI.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR031649; GPHH_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR014873; VDCC_a1su_IQ.
DR InterPro; IPR005449; VDCC_R_a1su.
DR InterPro; IPR002077; VDCCAlpha1.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR45628:SF5; PTHR45628:SF5; 2.
DR Pfam; PF08763; Ca_chan_IQ; 1.
DR Pfam; PF16905; GPHH; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00167; CACHANNEL.
DR PRINTS; PR01633; RVDCCALPHA1.
DR SMART; SM01062; Ca_chan_IQ; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Calcium channel; Calcium transport; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..2272
FT /note="Voltage-dependent R-type calcium channel subunit
FT alpha-1E"
FT /id="PRO_0000053939"
FT TOPO_DOM 1..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..109
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..128
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..147
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..174
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..186
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..206
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..327
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..351
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352..477
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..497
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 498..510
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 511..530
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 531..539
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 540..558
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 559..568
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 569..587
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 588..606
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 607..626
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 627..679
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 680..704
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 705..1150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1151..1167
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1168..1191
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1192..1211
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1212..1219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1220..1242
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1243..1256
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1257..1274
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1275..1293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1294..1313
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1314..1400
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1401..1424
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1425..1481
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1482..1500
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1501..1515
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1516..1535
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1536..1543
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1544..1562
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1563..1573
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1574..1592
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1593..1611
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1612..1631
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1632..1700
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1701..1726
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1727..2272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 77..355
FT /note="I"
FT REPEAT 463..707
FT /note="II"
FT REPEAT 1143..1429
FT /note="III"
FT REPEAT 1466..1729
FT /note="IV"
FT DOMAIN 1742..1777
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..392
FT /note="Binding to the beta subunit"
FT /evidence="ECO:0000250"
FT REGION 730..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2021..2186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2025..2082
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2083..2116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2155..2185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 427
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 429
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 431
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 433
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 438
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 1755
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 1761
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 1766
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT SITE 310
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 658
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1375
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1666
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 441
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07652"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 794
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07652"
FT MOD_RES 816
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 856
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 948
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07652"
FT MOD_RES 1099
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07652"
FT MOD_RES 2054
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2073
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07652"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1569
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1692
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 2272 AA; 257236 MW; 70D9200B9E0C87A1 CRC64;
MARFGEAVVV GRPGSGDGDS DQSRNRQGTP VPASGPAAAY KQSKAQRART MALYNPIPVR
QNCFTVNRSL FIFGEDNIVR KYAKKLIDWP PFEYMILATI IANCIVLALE QHLPEDDKTP
MSRRLEKTEP YFIGIFCFEA GIKIVALGFI FHKGSYLRNG WNVMDFIVVL SGILATAGTH
FNTHVDLRAL RAVRVLRPLK LVSGIPSLQI VLKSIMKAMV PLLQIGLLLF FAILMFAIIG
LEFYSGKLHR ACFMNNSGIL EGFDPPHPCG VQGCPAGYEC KDWIGPNDGI TQFDNILFAV
LTVFQCITME GWTTVLYNTN DALGATWNWL YFIPLIIIGS FFVLNLVLGV LSGEFAKERE
RVENRRAFMK LRRQQQIERE LNGYRAWIDK AEEVMLAEEN KNSGTSALEV LRRATIKRSR
TEAMTRDSSD EHCVDISSVG TPLARASIKS TKVDGASYFR HKERLLRISI RHMVKSQVFY
WIVLSVVALN TACVAIVHHN QPQWLTHLLY YAEFLFLGLF LLEMSLKMYG MGPRLYFHSS
FNCFDFGVTV GSIFEVVWAI FRPGTSFGIS VLRALRLLRI FKITKYWASL RNLVVSLMSS
MKSIISLLFL LFLFIVVFAL LGMQLFGGRF NFNDGTPSAN FDTFPAAIMT VFQILTGEDW
NEVMYNGIRS QGGVSSGMWS AIYFIVLTLF GNYTLLNVFL AIAVDNLANA QELTKDEQEE
EEAFNQKHAL QKAKEVSPMS APNMPSIERD RRRRHHMSMW EPRSSHLRER RRRHHMSVWE
QRTSQLRRHM QMSSQEALNK EEAPPMNPLN PLNPLSPLNP LNAHPSLYRR PRPIEGLALG
LGLEKCEEER ISRGGSLKGD IGGLTSALDN QRSPLSLGKR EPPWLPRSCH GNCDPIQQEA
GGGETVVTFE DRARHRQSQR RSRHRRVRTE GKDSASASRS RSASQERSLD EGVSVEGEKE
HEPHSSHRSK EPTIHEEERT QDLRRTNSLM VPRGSGLVGA LDEAETPLVQ PQPELEVGKD
AALTEQEAEG SSEQALLGDV QLDVGRGISQ SEPDLSCMTA NMDKATTEST SVTVAIPDVD
PLVDSTVVNI SNKTDGEASP LKEAETKEEE EEVEKKKKQK KEKRETGKAM VPHSSMFIFS
TTNPIRRACH YIVNLRYFEM CILLVIAASS IALAAEDPVL TNSERNKVLR YFDYVFTGVF
TFEMVIKMID QGLILQDGSY FRDLWNILDF VVVVGALVAF ALANALGTNK GRDIKTIKSL
RVLRVLRPLK TIKRLPKLKA VFDCVVTSLK NVFNILIVYK LFMFIFAVIA VQLFKGKFFY
CTDSSKDTEK ECIGNYVDHE KNKMEVKGRE WKRHEFHYDN IIWALLTLFT VSTGEGWPQV
LQHSVDVTEE DRGPSRSNRM EMSIFYVVYF VVFPFFFVNI FVALIIITFQ EQGDKMMEEC
SLEKNERACI DFAISAKPLT RYMPQNRHTF QYRVWHFVVS PSFEYTIMAM IALNTVVLMM
KYYTAPCTYE LALKYLNIAF TMVFSLECVL KVIAFGFLNY FRDTWNIFDF ITVIGSITEI
ILTDSKLVNT SGFNMSFLKL FRAARLIKLL RQGYTIRILL WTFVQSFKAL PYVCLLIAML
FFIYAIIGMQ VFGNIKLDEE SHINRHNNFR SFFGSLMLLF RSATGEAWQE IMLSCLGEKG
CEPDTTAPSG QNESERCGTD LAYVYFVSFI FFCSFLMLNL FVAVIMDNFE YLTRDSSILG
PHHLDEFVRV WAEYDRAACG RIHYTEMYEM LTLMSPPLGL GKRCPSKVAY KRLVLMNMPV
AEDMTVHFTS TLMALIRTAL DIKIAKGGAD RQQLDSELQK ETLAIWPHLS QKMLDLLVPM
PKASDLTVGK IYAAMMIMDY YKQSKVKKQR QQLEEQKNAP MFQRMEPSSL PQEIIANAKA
LPYLQQDPVS GLSGRSGYPS MSPLSPQEIF QLACMDPADD GQFQEQQSLV VTDPSSMRRS
FSTIRDKRSN SSWLEEFSME RSSENTYKSR RRSYHSSLRL SAHRLNSDSG HKSDTHRSGG
RERGRSKERK HLLSPDVSRC NSEERGTQAD WESPERRQSR SPSEGRSQTP NRQGTGSLSE
SSIPSISDTS TPRRSRRQLP PVPPKPRPLL SYSSLMRHTG GISPPPDGSE GGSPLASQAL
ESNSACLTES SNSLHPQQGQ HPSPQHYISE PYLALHEDSH ASDCGEEETL TFEAAVATSL
GRSNTIGSAP PLRHSWQMPN GHYRRRRWGA WAGMMCGAVS DLLSDTEEDD KC
