ID   KCNAE_DROME             Reviewed;        1174 AA.
AC   Q02280; Q9VXZ6;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   27-MAR-2024, entry version 197.
DE   RecName: Full=Potassium voltage-gated channel protein eag;
DE   AltName: Full=Ether-a-go-go protein;
GN   Name=eag; ORFNames=CG10952;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   TISSUE=Head;
RX   PubMed=1840699; DOI=10.1126/science.1840699;
RA   Warmke J., Drysdale R.A., Ganetzky B.;
RT   "A distinct potassium channel polypeptide encoded by the Drosophila eag
RT   locus.";
RL   Science 252:1560-1562(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=10934243; DOI=10.1523/jneurosci.20-16-05958.2000;
RA   Wang J.W., Humphreys J.M., Phillips J.P., Hilliker A.J., Wu C.F.;
RT   "A novel leg-shaking Drosophila mutant defective in a voltage-gated
RT   K(+)current and hypersensitive to reactive oxygen species.";
RL   J. Neurosci. 20:5958-5964(2000).
RN   [5]
RP   FUNCTION.
RX   PubMed=11517334; DOI=10.1073/pnas.191107698;
RA   Yager J., Richards S., Hekmat-Scafe D.S., Hurd D.D., Sundaresan V.,
RA   Caprette D.R., Saxton W.M., Carlson J.R., Stern M.;
RT   "Control of Drosophila perineurial glial growth by interacting
RT   neurotransmitter-mediated signaling pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:10445-10450(2001).
RN   [6]
RP   FUNCTION, PHOSPHORYLATION AT THR-787, MUTAGENESIS OF THR-787, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=11980904; DOI=10.1074/jbc.m201949200;
RA   Wang Z., Wilson G.F., Griffith L.C.;
RT   "Calcium/calmodulin-dependent protein kinase II phosphorylates and
RT   regulates the Drosophila eag potassium channel.";
RL   J. Biol. Chem. 277:24022-24029(2002).
RN   [7]
RP   FUNCTION, INTERACTION WITH CASK, AND SUBCELLULAR LOCATION.
RX   PubMed=15901771; DOI=10.1523/jneurosci.4566-04.2005;
RA   Marble D.D., Hegle A.P., Snyder E.D. II, Dimitratos S., Bryant P.J.,
RA   Wilson G.F.;
RT   "Camguk/CASK enhances Ether-a-go-go potassium current by a phosphorylation-
RT   dependent mechanism.";
RL   J. Neurosci. 25:4898-4907(2005).
CC   -!- FUNCTION: Structural component of a potassium channel. Mediates the
CC       potassium permeability of membranes; potassium current is regulated by
CC       CaMKII and CASK. Has a role in growth of the perineurial glial layer of
CC       the larval peripheral nerve. {ECO:0000269|PubMed:11517334,
CC       ECO:0000269|PubMed:11980904, ECO:0000269|PubMed:15901771,
CC       ECO:0000269|PubMed:1840699}.
CC   -!- SUBUNIT: The voltage-dependent potassium channel is a heterotetramer of
CC       potassium channel proteins (By similarity). Interaction with CASK.
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q02280; Q24210: CASK; NbExp=10; IntAct=EBI-85304, EBI-214423;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15901771}; Multi-
CC       pass membrane protein {ECO:0000269|PubMed:15901771}. Note=Eag recruits
CC       CASK to the plasma membrane.
CC   -!- TISSUE SPECIFICITY: Expressed in the axon and the terminal boutons of
CC       motor neurons. {ECO:0000269|PubMed:11980904}.
CC   -!- PTM: When in complex with CASK, the efficiency of Thr-787
CC       phosphorylation is increased. {ECO:0000269|PubMed:11980904}.
CC   -!- DISRUPTION PHENOTYPE: Increased growth of the perineurial glial layer
CC       of the larval peripheral nerve (PubMed:1840699). Hyperexcitability at
CC       the larval neuromuscular junction (NMJ) and memory formation defects in
CC       the adult (PubMed:1840699). Hypersensitivity to reactive oxygen species
CC       generated by the redox-cycling agent paraquat (PubMed:10934243).
CC       {ECO:0000269|PubMed:10934243, ECO:0000269|PubMed:1840699}.
CC   -!- MISCELLANEOUS: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at every
CC       third position.
CC   -!- MISCELLANEOUS: The segment H5 is thought to line the channel pore.
CC   -!- SIMILARITY: Belongs to the potassium channel family. H (Eag)
CC       (TC 1.A.1.20) subfamily. Eag sub-subfamily. {ECO:0000305}.
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DR   EMBL; M61157; AAA28495.1; -; mRNA.
DR   EMBL; AE014298; AAF48410.1; -; Genomic_DNA.
DR   PIR; A40853; A40853.
DR   RefSeq; NP_511158.2; NM_078603.4.
DR   PDB; 5FG8; X-ray; 1.96 A; B=768-820.
DR   PDB; 5H9B; X-ray; 2.25 A; B=770-820.
DR   PDB; 5HU3; X-ray; 1.89 A; B=768-820.
DR   PDBsum; 5FG8; -.
DR   PDBsum; 5H9B; -.
DR   PDBsum; 5HU3; -.
DR   AlphaFoldDB; Q02280; -.
DR   SMR; Q02280; -.
DR   BioGRID; 58786; 8.
DR   IntAct; Q02280; 3.
DR   STRING; 7227.FBpp0110308; -.
DR   TCDB; 1.A.1.20.6; the voltage-gated ion channel (vic) superfamily.
DR   GlyCosmos; Q02280; 3 sites, No reported glycans.
DR   GlyGen; Q02280; 3 sites.
DR   iPTMnet; Q02280; -.
DR   PaxDb; 7227-FBpp0110308; -.
DR   EnsemblMetazoa; FBtr0073955; FBpp0073772; FBgn0000535.
DR   GeneID; 32428; -.
DR   KEGG; dme:Dmel_CG10952; -.
DR   AGR; FB:FBgn0000535; -.
DR   CTD; 32428; -.
DR   FlyBase; FBgn0000535; eag.
DR   VEuPathDB; VectorBase:FBgn0000535; -.
DR   eggNOG; KOG0501; Eukaryota.
DR   GeneTree; ENSGT00940000155793; -.
DR   HOGENOM; CLU_005746_3_1_1; -.
DR   InParanoid; Q02280; -.
DR   PhylomeDB; Q02280; -.
DR   Reactome; R-DME-1296072; Voltage gated Potassium channels.
DR   BioGRID-ORCS; 32428; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 32428; -.
DR   PRO; PR:Q02280; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0000535; Expressed in brain and 7 other cell types or tissues.
DR   ExpressionAtlas; Q02280; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IPI:FlyBase.
DR   GO; GO:0044325; F:transmembrane transporter binding; IPI:FlyBase.
DR   GO; GO:0022843; F:voltage-gated monoatomic cation channel activity; IDA:FlyBase.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:FlyBase.
DR   GO; GO:0048150; P:behavioral response to ether; NAS:FlyBase.
DR   GO; GO:0007619; P:courtship behavior; TAS:FlyBase.
DR   GO; GO:0007612; P:learning; IMP:FlyBase.
DR   GO; GO:0007611; P:learning or memory; NAS:FlyBase.
DR   GO; GO:0042066; P:perineurial glial growth; IGI:FlyBase.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006813; P:potassium ion transport; TAS:FlyBase.
DR   GO; GO:0008016; P:regulation of heart contraction; NAS:FlyBase.
DR   GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR   GO; GO:0007608; P:sensory perception of smell; NAS:FlyBase.
DR   CDD; cd00038; CAP_ED; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.1200.260; -; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003949; K_chnl_volt-dep_EAG.
DR   InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR10217:SF435; POTASSIUM VOLTAGE-GATED CHANNEL PROTEIN EAG; 1.
DR   PANTHER; PTHR10217; VOLTAGE AND LIGAND GATED POTASSIUM CHANNEL; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR01463; EAGCHANLFMLY.
DR   PRINTS; PR01464; EAGCHANNEL.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   Genevisible; Q02280; DM.
PE   1: Evidence at protein level;
KW   3D-structure; Developmental protein; Differentiation; Glycoprotein;
KW   Ion channel; Ion transport; Membrane; Neurogenesis; Phosphoprotein;
KW   Potassium; Potassium channel; Potassium transport; Reference proteome;
KW   Repeat; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   CHAIN           1..1174
FT                   /note="Potassium voltage-gated channel protein eag"
FT                   /id="PRO_0000053964"
FT   TOPO_DOM        1..226
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        227..246
FT                   /note="Helical; Name=Segment S1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        247..268
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        269..291
FT                   /note="Helical; Name=Segment S2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        292..313
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        314..335
FT                   /note="Helical; Name=Segment S3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        336..342
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        343..369
FT                   /note="Helical; Voltage-sensor; Name=Segment S4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        370..371
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        372..393
FT                   /note="Helical; Name=Segment S5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        394..441
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        442..467
FT                   /note="Pore-forming; Name=Segment H5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        468..470
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        471..493
FT                   /note="Helical; Name=Segment S6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        494..1174
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          43..97
FT                   /note="PAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          113..165
FT                   /note="PAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT   REGION          742..763
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          778..842
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          865..884
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          930..977
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1022..1097
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1115..1174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           453..458
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        818..832
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        867..883
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1071..1095
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1115..1166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         571..688
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT   MOD_RES         787
FT                   /note="Phosphothreonine; by CaMK2"
FT                   /evidence="ECO:0000269|PubMed:11980904"
FT   CARBOHYD        262
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        412
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        424
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         787
FT                   /note="T->A: Reduced eag channel amplitude and accelerated
FT                   inactivation. Does not affect binding with CASK."
FT                   /evidence="ECO:0000269|PubMed:11980904"
FT   CONFLICT        548
FT                   /note="Y -> C (in Ref. 1; AAA28495)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        567
FT                   /note="N -> D (in Ref. 1; AAA28495)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        571
FT                   /note="A -> T (in Ref. 1; AAA28495)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        699
FT                   /note="K -> R (in Ref. 1; AAA28495)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        769
FT                   /note="F -> L (in Ref. 1; AAA28495)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        894
FT                   /note="I -> V (in Ref. 1; AAA28495)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        934
FT                   /note="G -> S (in Ref. 1; AAA28495)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1015
FT                   /note="N -> D (in Ref. 1; AAA28495)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1042
FT                   /note="R -> G (in Ref. 1; AAA28495)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1049
FT                   /note="K -> E (in Ref. 1; AAA28495)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1088
FT                   /note="T -> A (in Ref. 1; AAA28495)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1142
FT                   /note="T -> I (in Ref. 1; AAA28495)"
FT                   /evidence="ECO:0000305"
FT   STRAND          788..791
FT                   /evidence="ECO:0007829|PDB:5FG8"
SQ   SEQUENCE   1174 AA;  126371 MW;  B8F86ACBB5627FD3 CRC64;
     MPGGRRGLVA PQNTFLENII RRSNSQPDSS FLLANAQIVD FPIVYCNESF CKISGYNRAE
     VMQKSCRYVC GFMYGELTDK ETVGRLEYTL ENQQQDQFEI LLYKKNNLQC GCALSQFGKA
     QTQETPLWLL LQVAPIRNER DLVVLFLLTF RDITALKQPI DSEDTKGVLG LSKFAKLARS
     VTRSRQFSAH LPTLKDPTKQ SNLAHMMSLS ADIMPQYRQE APKTPPHILL HYCAFKAIWD
     WVILCLTFYT AIMVPYNVAF KNKTSEDVSL LVVDSIVDVI FFIDIVLNFH TTFVGPGGEV
     VSDPKVIRMN YLKSWFIIDL LSCLPYDVFN AFDRDEDGIG SLFSALKVVR LLRLGRVVRK
     LDRYLEYGAA MLILLLCFYM LVAHWLACIW YSIGRSDADN GIQYSWLWKL ANVTQSPYSY
     IWSNDTGPEL VNGPSRKSMY VTALYFTMTC MTSVGFGNVA AETDNEKVFT ICMMIIAALL
     YATIFGHVTT IIQQMTSATA KYHDMLNNVR EFMKLHEVPK ALSERVMDYV VSTWAMTKGL
     DTEKVLNYCP KDMKADICVH LNRKVFNEHP AFRLASDGCL RALAMHFMMS HSAPGDLLYH
     TGESIDSLCF IVTGSLEVIQ DDEVVAILGK GDVFGDQFWK DSAVGQSAAN VRALTYCDLH
     AIKRDKLLEV LDFYSAFANS FARNLVLTYN LRHRLIFRKV ADVKREKELA ERRKNEPQLP
     QNQDHLVRKI FSKFRRTPQV QAGSKELVGG SGQSDVEKGD GEVERTKVFP KAPKLQASQA
     TLARQDTIDE GGEVDSSPPS RDSRVVIEGA AVSSATVGPS PPVATTSSAA AGAGVSGGPG
     SGGTVVAIVT KADRNLALER ERQIEMASSR ATTSDTYDTG LRETPPTLAQ RDLIATVLDM
     KVDVRLELQR MQQRIGRIED LLGELVKRLA PGAGSGGNAP DNSSGQTTPG DEICAGCGAG
     GGGTPTTQAP PTSAVTSPVD TVITISSPGA SGSGSGTGAG AGSAVAGAGG AGLLNPGATV
     VSSAGGNGLG PLMLKKRRSK SRKAPAPPKQ TLASTAGTAT AAPAGVAGSG MTSSAPASAD
     QQQQHQSTAD QSPTTPGAEL LHLRLLEEDF TAAQLPSTSS GGAGGGGGSG SGATPTTPPP
     TTAGGSGSGT PTSTTATTTP TGSGTATRGK LDFL
//