CAC1E_RAT
ID CAC1E_RAT Reviewed; 2222 AA.
AC Q07652;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Voltage-dependent R-type calcium channel subunit alpha-1E;
DE AltName: Full=BII;
DE AltName: Full=Brain calcium channel II;
DE AltName: Full=Calcium channel, L type, alpha-1 polypeptide, isoform 6;
DE AltName: Full=RBE-II;
DE AltName: Full=RBE2;
DE AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.3;
GN Name=Cacna1e; Synonyms=Cach6, Cacnl1a6;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8388125; DOI=10.1126/science.8388125;
RA Soong T.W., Stea A., Hodson C.D., Dubel S.J., Vincent S.R., Snutch T.P.;
RT "Structure and functional expression of a member of the low voltage-
RT activated calcium channel family.";
RL Science 260:1133-1136(1993).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-687; SER-744; SER-806;
RP SER-898; SER-1049 AND SER-2022, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- INTERACTION:
CC Q07652; P62158: CALM3; Xeno; NbExp=2; IntAct=EBI-15734403, EBI-397435;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in central nervous system and in
CC insulinoma.
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; L15453; AAA40855.1; -; mRNA.
DR PIR; A37490; A37490.
DR PDB; 3DVK; X-ray; 2.30 A; B=1818-1837.
DR PDBsum; 3DVK; -.
DR AlphaFoldDB; Q07652; -.
DR SMR; Q07652; -.
DR DIP; DIP-46236N; -.
DR IntAct; Q07652; 2.
DR STRING; 10116.ENSRNOP00000003928; -.
DR DrugCentral; Q07652; -.
DR GuidetoPHARMACOLOGY; 534; -.
DR CarbonylDB; Q07652; -.
DR GlyGen; Q07652; 4 sites.
DR iPTMnet; Q07652; -.
DR PhosphoSitePlus; Q07652; -.
DR PaxDb; Q07652; -.
DR PRIDE; Q07652; -.
DR UCSC; RGD:2246; rat.
DR RGD; 2246; Cacna1e.
DR eggNOG; KOG2301; Eukaryota.
DR InParanoid; Q07652; -.
DR PhylomeDB; Q07652; -.
DR Reactome; R-RNO-112308; Presynaptic depolarization and calcium channel opening.
DR Reactome; R-RNO-422356; Regulation of insulin secretion.
DR EvolutionaryTrace; Q07652; -.
DR PRO; PR:Q07652; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:RGD.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:RGD.
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:0008332; F:low voltage-gated calcium channel activity; TAS:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:RGD.
DR GO; GO:0099626; F:voltage-gated calcium channel activity involved in regulation of presynaptic cytosolic calcium levels; IDA:SynGO.
DR GO; GO:0022843; F:voltage-gated cation channel activity; ISO:RGD.
DR GO; GO:0001662; P:behavioral fear response; ISO:RGD.
DR GO; GO:0048266; P:behavioral response to pain; ISO:RGD.
DR GO; GO:0070509; P:calcium ion import; IDA:RGD.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; ISO:RGD.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0042596; P:fear response; ISO:RGD.
DR GO; GO:0030317; P:flagellated sperm motility; ISO:RGD.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0050877; P:nervous system process; ISO:RGD.
DR GO; GO:0002027; P:regulation of heart rate; ISO:RGD.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:RGD.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0090273; P:regulation of somatostatin secretion; ISO:RGD.
DR GO; GO:0048265; P:response to pain; ISO:RGD.
DR GO; GO:0019233; P:sensory perception of pain; ISO:RGD.
DR GO; GO:0019226; P:transmission of nerve impulse; ISO:RGD.
DR GO; GO:0008542; P:visual learning; ISO:RGD.
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 3D-structure; Calcium; Calcium channel; Calcium transport; Disulfide bond;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..2222
FT /note="Voltage-dependent R-type calcium channel subunit
FT alpha-1E"
FT /id="PRO_0000053941"
FT TOPO_DOM 1..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..59
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..78
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..97
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..124
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..136
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..156
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..277
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..301
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..447
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 448..460
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 461..480
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 481..489
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 490..508
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 509..518
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 519..537
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 538..556
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 557..576
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 577..629
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 630..654
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 655..1100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1101..1117
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1118..1141
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1142..1161
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1162..1169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1170..1192
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1193..1206
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1207..1224
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1225..1243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1244..1263
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1264..1350
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1351..1374
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1375..1431
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1432..1450
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1451..1467
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1468..1485
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1486..1493
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1494..1512
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1513..1523
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1524..1542
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1543..1561
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1562..1581
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1582..1650
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1651..1676
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1677..2222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 27..305
FT /note="I"
FT REPEAT 413..657
FT /note="II"
FT REPEAT 1092..1378
FT /note="III"
FT REPEAT 1415..1678
FT /note="IV"
FT DOMAIN 1691..1726
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 325..342
FT /note="Binding to the beta subunit"
FT /evidence="ECO:0000250"
FT REGION 680..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 820..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1042..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1970..2135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..934
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1076
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1974..2031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2032..2065
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2104..2134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 377
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 379
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 381
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 383
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 1704
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 1710
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 1715
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT SITE 260
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 608
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1324
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1615
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61290"
FT MOD_RES 391
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q61290"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 696
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61290"
FT MOD_RES 744
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 766
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61290"
FT MOD_RES 806
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 898
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1049
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2003
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61290"
FT MOD_RES 2022
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1641
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT HELIX 1818..1835
FT /evidence="ECO:0007829|PDB:3DVK"
SQ SEQUENCE 2222 AA; 252116 MW; DF6452A2175CEB19 CRC64;
MALYNPIPVR QNCFTVNRSL FIFGEDNIVR KYAKKLIDWP PFEYMILATI IANCIVLALE
QHLPEDDKTP MSRRLEKTEP YFIGIFCFEA GIKIVALGFI FHKGSYLRNG WNVMDFIVVL
SGILATAGTH FNTHVDLRTL 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 IGGLTSVLDN QRSPLSLGKR EPPWLPRSCH
GNCDPTQQET GGGETVVTFE DRARHRQSQR RSRHRRVRTE GKESASASRS RSASQERSLD
EGVSIDGEKE HEPQSSHRSK EPTIHEEERT QDLRRTNSLM VPRGSGLVGA LDEAETPLVQ
PQPELEVGKD AALTEQEAEG SSEQALLADV QLDVGRGISQ SEPDLSCMTT NMDKATTEST
SVTVAIPDVD PLVDSTVVNI SNKTDGEASP LKEAETKEEE EEVEKKKQKK EKRETGKAMV
PHSSMFIFST TNPIRKACHY IVNLRYFEMC ILLVIAASSI ALAAEDPVLT NSERNKVLRY
FDYVFTGVFT FEMVIKMIDQ GLILQDGSYF RDLWNILDFV VVVGALVAFA LANALGTNKG
RDIKTIKSLR VLRVLRPLKT IKRLPKLKAV FDCVVTSLKN VFNILIVYKL FMFIFAVIAV
QLFKGKFFYC TDSSKDTEKE CIGNYVDHEK NKMEVKGREW KRHEFHYDNI IWALLTLFTV
STGEGWPQVL QHSVDVTEED RGPSRSNRME MSIFYVVYFV VFPFFFVNIF VALIIITFQE
QGDKMMEECS LEKNERACID FAISAKPLTR YMPQNRHTFQ YRVWHFVVSP SFEYTIMAMI
ALNTVVLMMK YYSAPWTYEL ALKYLNIAFT MVFSLECVLK VIAFGFLNYF RDTWNIFDFI
TVIGSITEII LTDSKLVNTS GFNMSFLKLF RAARLIKLLR QGYTIRILLW TFVQSFKALP
YVCLLIAMLF FIYAIIGMQV FGNIKLDEES HINRHNNFRS FFGSLMLLFR SATGEAWQEI
MLSCLGEKGC EPDTTAPSGQ NESERCGTDL AYVYFVSFIF FCSFLMLNLF VAVIMDNFEY
LTRDSSILGP HHLDEFVRVW AEYDRAACGR IHYTEMYEML TLMSPPLGLG KRCPSKVAYK
RLVLMNMPVA EDMTVHFTST LMALIRTALD IKIAKGGADR QQLDSELQKE TLAIWPHLSQ
KMLDLLVPMP KASDLTVGKI YAAMMIMDYY KQSKVKKQRQ QLEEQKNAPM FQRMEPSSLP
QEIISNAKAL PYLQQDPVSG LSGRSGYPSM SPLSPQEIFQ LACMDPADDG QFQEQQSLVV
TDPSSMRRSF STIRDKRSNS SWLEEFSMER SSENTYKSRR RSYHSSLRLS AHRLNSDSGH
KSDTHRSGGR ERGRSKERKH LLSPDVSRCN SEERGTQADW ESPERRQSRS PSEGRSQTPN
RQGTGSLSES SIPSISDTST PRRSRRQLPP VPPKPRPLLS YSSLMRHTGG ISPPPDGSEG
GSPLASQALE SNSACLTESS NSLHPQQGQH PSPQHYISEP YLALHEDSHA SDCGEEETLT
FEAAVATSLG RSNTIGSAPP LRHSWQMPNG HYRRRRLGGL GLAMMCGAVS DLLSDTEEDD
KC
