CLCN2_DROME
ID CLCN2_DROME Reviewed; 1193 AA.
AC Q9VGH7; A4VCL3; A8JQX8; A8JQX9; E1JIJ0; Q7YU63; Q8INJ7; Q8MRL4; Q9VGH8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Chloride channel protein 2;
DE Short=ClC-2;
DE Short=DmClC-2;
DE AltName: Full=Chloride channel-a;
GN Name=ClC-a; ORFNames=CG31116;
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] {ECO:0000312|EMBL:AAF54702.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [2] {ECO:0000305, ECO:0000312|EMBL:AAF54702.3}
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAM50193.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), AND RNA EDITING OF
RP POSITIONS 249; 276; 285 AND 286.
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM50193.1};
RC TISSUE=Head {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAQ22442.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS F AND G).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAQ22442.1}; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kapadia B., Kronmiller B., Li P.W., Liao G.,
RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
RA Celniker S.E.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=15501232; DOI=10.1016/j.ydbio.2004.08.047;
RA Kearney J.B., Wheeler S.R., Estes P., Parente B., Crews S.T.;
RT "Gene expression profiling of the developing Drosophila CNS midline
RT cells.";
RL Dev. Biol. 275:473-492(2004).
RN [6] {ECO:0000305}
RP RNA EDITING OF POSITIONS 249; 276; 285 AND 286.
RX PubMed=17018572; DOI=10.1261/rna.254306;
RA Stapleton M., Carlson J.W., Celniker S.E.;
RT "RNA editing in Drosophila melanogaster: new targets and functional
RT consequences.";
RL RNA 12:1922-1932(2006).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17601953; DOI=10.1242/jeb.006361;
RA Rose U., Derst C., Wanischeck M., Marinc C., Walther C.;
RT "Properties and possible function of a hyperpolarisation-activated chloride
RT current in Drosophila.";
RL J. Exp. Biol. 210:2489-2500(2007).
CC -!- FUNCTION: Voltage-gated chloride channel. Chloride channels have
CC several functions including the regulation of cell volume; membrane
CC potential stabilization, signal transduction and transepithelial
CC transport. {ECO:0000269|PubMed:17601953}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=D {ECO:0000269|PubMed:10731132};
CC IsoId=Q9VGH7-1; Sequence=Displayed;
CC Name=A {ECO:0000269|PubMed:10731132};
CC IsoId=Q9VGH7-2; Sequence=VSP_052366;
CC Name=F; Synonyms=B;
CC IsoId=Q9VGH7-3; Sequence=VSP_052367;
CC Name=C {ECO:0000269|PubMed:10731132};
CC IsoId=Q9VGH7-4; Sequence=VSP_052366, VSP_052367;
CC Name=G;
CC IsoId=Q9VGH7-6; Sequence=VSP_035041, VSP_035042, VSP_052367;
CC Name=H;
CC IsoId=Q9VGH7-7; Sequence=VSP_035041, VSP_035042;
CC -!- TISSUE SPECIFICITY: At embryonic stages 13-16, expressed in a subset of
CC the midline cells of the midline primordium and in all of the midline
CC glia. Expressed along the Z-line of the sarcomere in larval
CC longitudinal muscles. {ECO:0000269|PubMed:15501232,
CC ECO:0000269|PubMed:17601953}.
CC -!- RNA EDITING: Modified_positions=249 {ECO:0000269|PubMed:12537569,
CC ECO:0000269|PubMed:17018572}, 276 {ECO:0000269|PubMed:12537569,
CC ECO:0000269|PubMed:17018572}, 285 {ECO:0000269|PubMed:12537569,
CC ECO:0000269|PubMed:17018572}, 286 {ECO:0000269|PubMed:12537569,
CC ECO:0000269|PubMed:17018572}; Note=Partially edited. Target of Adar.
CC {ECO:0000269|PubMed:17018572};
CC -!- MISCELLANEOUS: The CLC channel family contains both chloride channels
CC and proton-coupled anion transporters that exchange chloride or another
CC anion for protons. The absence of conserved gating glutamate residues
CC is typical for family members that function as channels.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family.
CC {ECO:0000305}.
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DR EMBL; AE014297; AAF54701.3; -; Genomic_DNA.
DR EMBL; AE014297; AAF54702.3; -; Genomic_DNA.
DR EMBL; AE014297; AAN13532.2; -; Genomic_DNA.
DR EMBL; AE014297; ABW08644.2; -; Genomic_DNA.
DR EMBL; AE014297; ABW08645.1; -; Genomic_DNA.
DR EMBL; AE014297; ACZ94889.1; -; Genomic_DNA.
DR EMBL; AY119539; AAM50193.1; -; mRNA.
DR EMBL; BT009973; AAQ22442.1; -; mRNA.
DR EMBL; BT030454; ABP87896.1; -; mRNA.
DR RefSeq; NP_001097751.2; NM_001104281.2. [Q9VGH7-6]
DR RefSeq; NP_001097752.1; NM_001104282.3. [Q9VGH7-3]
DR RefSeq; NP_001163592.1; NM_001170121.1. [Q9VGH7-7]
DR RefSeq; NP_731634.2; NM_169431.3. [Q9VGH7-4]
DR RefSeq; NP_731635.2; NM_169432.3. [Q9VGH7-2]
DR RefSeq; NP_788639.1; NM_176462.2. [Q9VGH7-1]
DR AlphaFoldDB; Q9VGH7; -.
DR SMR; Q9VGH7; -.
DR BioGRID; 66550; 3.
DR IntAct; Q9VGH7; 6.
DR STRING; 7227.FBpp0082002; -.
DR PaxDb; Q9VGH7; -.
DR PRIDE; Q9VGH7; -.
DR DNASU; 41428; -.
DR EnsemblMetazoa; FBtr0082526; FBpp0082000; FBgn0051116. [Q9VGH7-2]
DR EnsemblMetazoa; FBtr0082527; FBpp0082001; FBgn0051116. [Q9VGH7-4]
DR EnsemblMetazoa; FBtr0082528; FBpp0082002; FBgn0051116. [Q9VGH7-1]
DR EnsemblMetazoa; FBtr0113391; FBpp0112303; FBgn0051116. [Q9VGH7-3]
DR EnsemblMetazoa; FBtr0300622; FBpp0289849; FBgn0051116. [Q9VGH7-6]
DR EnsemblMetazoa; FBtr0301023; FBpp0290245; FBgn0051116. [Q9VGH7-7]
DR GeneID; 41428; -.
DR KEGG; dme:Dmel_CG31116; -.
DR UCSC; CG31116-RA; d. melanogaster. [Q9VGH7-1]
DR UCSC; CG31116-RE; d. melanogaster.
DR UCSC; CG31116-RF; d. melanogaster.
DR CTD; 41428; -.
DR FlyBase; FBgn0051116; ClC-a.
DR VEuPathDB; VectorBase:FBgn0051116; -.
DR eggNOG; KOG0476; Eukaryota.
DR GeneTree; ENSGT00940000168847; -.
DR InParanoid; Q9VGH7; -.
DR OMA; ACFMFNN; -.
DR PhylomeDB; Q9VGH7; -.
DR Reactome; R-DME-2672351; Stimuli-sensing channels.
DR SignaLink; Q9VGH7; -.
DR BioGRID-ORCS; 41428; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 41428; -.
DR PRO; PR:Q9VGH7; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0051116; Expressed in adult Malpighian tubule (Drosophila) and 31 other tissues.
DR ExpressionAtlas; Q9VGH7; baseline and differential.
DR Genevisible; Q9VGH7; DM.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
DR GO; GO:0009925; C:basal plasma membrane; IDA:FlyBase.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0005254; F:chloride channel activity; IMP:FlyBase.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; IMP:FlyBase.
DR GO; GO:0006821; P:chloride transport; ISS:UniProtKB.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0003091; P:renal water homeostasis; IMP:FlyBase.
DR GO; GO:0003097; P:renal water transport; IMP:FlyBase.
DR GO; GO:0030321; P:transepithelial chloride transport; IMP:FlyBase.
DR GO; GO:0035377; P:transepithelial water transport; IMP:FlyBase.
DR Gene3D; 3.10.580.10; -; 2.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR014743; Cl-channel_core.
DR InterPro; IPR001807; Cl-channel_volt-gated.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR SUPFAM; SSF54631; SSF54631; 1.
DR SUPFAM; SSF81340; SSF81340; 1.
DR PROSITE; PS51371; CBS; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; CBS domain; Chloride; Chloride channel; Ion channel;
KW Ion transport; Membrane; Reference proteome; Repeat; RNA editing;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..1193
FT /note="Chloride channel protein 2"
FT /id="PRO_0000282953"
FT TOPO_DOM 1..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 169..204
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 213..236
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 245..252
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 261..279
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 286..304
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 320..332
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 336..344
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 356..373
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 402..430
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 439..458
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 511..530
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 536..555
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 576..590
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 591..592
FT /note="Note=Loop between two helices"
FT /evidence="ECO:0000250"
FT INTRAMEM 593..604
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 605..609
FT /note="Note=Loop between two helices"
FT /evidence="ECO:0000250"
FT TRANSMEM 610..626
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 627..1193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 663..723
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 1048..1105
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 76..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 242..246
FT /note="Selectivity filter part_1"
FT /evidence="ECO:0000250"
FT MOTIF 284..288
FT /note="Selectivity filter part_2"
FT /evidence="ECO:0000250"
FT MOTIF 536..540
FT /note="Selectivity filter part_3"
FT /evidence="ECO:0000250"
FT COMPBIAS 848..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 243
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT BINDING 538
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT BINDING 632
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1
FT /note="M -> MKATRNGGQLLIAPSPQTAARLLPLRTYSNASSLGHHHDRSTLSDGD
FT EEEGGLGYTH (in isoform G and isoform H)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_035041"
FT VAR_SEQ 2..107
FT /note="VYFGDRQRDRNRDRSNQKVERIIHDEEFGEENVELVDSEWADFEKFICQLRK
FT RRNSAMSMEEELRHVQRHPKIKSHAFYPCPPPAENARDSDSSDDDDPIGYIDTL -> F
FT NNSHSHQDEYIREYAFEPELLINREDYQRKEERSQKSTAASSASTPVRQRWDEVIAKQK
FT EQQRKQSIEIDPPGDDKNQIEIEIEAFYY (in isoform A and isoform C)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_052366"
FT VAR_SEQ 2..105
FT /note="Missing (in isoform G and isoform H)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_035042"
FT VAR_SEQ 889..1015
FT /note="Missing (in isoform F, isoform C and isoform G)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_052367"
FT VARIANT 249
FT /note="K -> R (in RNA edited version)"
FT /evidence="ECO:0000269|PubMed:17018572"
FT VARIANT 276
FT /note="T -> A (in RNA edited version)"
FT /evidence="ECO:0000269|PubMed:17018572"
FT VARIANT 285
FT /note="K -> R (in RNA edited version)"
FT /evidence="ECO:0000269|PubMed:17018572"
FT VARIANT 286
FT /note="E -> G (in RNA edited version)"
FT /evidence="ECO:0000269|PubMed:17018572"
FT CONFLICT 529
FT /note="S -> P (in Ref. 4; AAQ22442)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1193 AA; 133648 MW; 6CD0508E6DBCB9A6 CRC64;
MVYFGDRQRD RNRDRSNQKV ERIIHDEEFG EENVELVDSE WADFEKFICQ LRKRRNSAMS
MEEELRHVQR HPKIKSHAFY PCPPPAENAR DSDSSDDDDP IGYIDTLMYG RYTKDLGEFA
KDEARKLKIL EKRRKQEDKQ RNKELLGKHS TRAKRVSSWI WRHTVARLGE DWVFLALLGI
IMALLSFIMD KGISICTNAR IWLYRDLTSQ PFVQYIAWVS LPVCLILFSA GFVHLIAPQS
IGSGIPEMKT ILRGVQLKEY LTFKTLVAKV IGLTATLGSG MPLGKEGPFV HIASIVAQLL
SKLVTSFQGI YENESRNSEM LAAACAVGVG ACFAAPVGGV LFSIEVTTTY FAVRNYWRGF
FAAVCGATVF RLLAVWFQNA DTVRALFLTN FTTEFPFDPQ ELFVFALIGL VCGLGGASYV
WVHRRYVLFM RSNKRMNKFL QKNRFLYPGF LALLVSSISF PLGTGQFLAG ELSTHEQVTQ
LFSNFTWSRD DLTVEQAAVV THWMTSYTSV FGNLVIYTLF TFVVSIIAST IPVPSGMFIP
VFKIGAGFGR LVGEFMAVTF PHGVRYGGRL SPIMPGGYAV VGAAAFSGSV THTVSVAVII
FEMTGQITHV VPVMIAVLVA NAVAALLQPS IYDSIILIKK LPYLPDLLPS SSGMYSIFVE
DFMVRDVKYI WHGISYQKLK EVLKLNKTLR SLPLVDSPDN MILLGSVQRY ELIKMIEKHI
GREKRMEVAQ KWQKEAQERA LEEEKKKQEV ELKMRRPSRF EVLPAPDILS LRQIANDEML
PPKKRAETMH GSLAPRKSIL KKTNSFNLKT YAQPMGHSPS ITPYTTITGN SEFRIRSAFE
AIFKKSTTLQ DVQPDPETGS LSPAASNHEV EVPRTPSTPG VSKKVQLPAQ SNWDFVTDQI
MLQVNPISTE SNKMPAEKDF TDKALSNNGD SSKQSPSIKF KANKVADVNR SPQTAKRCSK
IRFANEVGVN GSPTRTKCKI KPENVLGYSI EDVDETTNPE SLAESIQKPK SVRLPRERVI
DMSPEDQKQW ELEEMLKPID LQKANVHIDP SPFQLVERTS ILKVHSLFSM VGINHAYVTK
IGRLVGVVGL KELRKAIEDI NSNSFVPPTR DEDADEKPAV EKPLLSTNSS DKAVDMTVTS
MDSALSNSEN CSDIEMEHIK HTDKGTVSLT MPPQESKQSP SADKSNTENG NHA
