TMC_DROME
ID TMC_DROME Reviewed; 2036 AA.
AC A0A0U1QT59; M9NDN5;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Transmembrane channel-like protein {ECO:0000303|PubMed:27298354};
GN Name=Tmc {ECO:0000303|PubMed:27298354, ECO:0000312|FlyBase:FBgn0267796};
GN ORFNames=CG46121 {ECO:0000312|FlyBase:FBgn0267796};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27478019; DOI=10.1016/j.neuron.2016.07.013;
RA Zhang Y.V., Aikin T.J., Li Z., Montell C.;
RT "The Basis of Food Texture Sensation in Drosophila.";
RL Neuron 91:863-877(2016).
RN [4] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=27298354; DOI=10.1073/pnas.1606537113;
RA Guo Y., Wang Y., Zhang W., Meltzer S., Zanini D., Yu Y., Li J., Cheng T.,
RA Guo Z., Wang Q., Jacobs J.S., Sharma Y., Eberl D.F., Goepfert M.C.,
RA Jan L.Y., Jan Y.N., Wang Z.;
RT "Transmembrane channel-like (tmc) gene regulates Drosophila larval
RT locomotion.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:7243-7248(2016).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30853433; DOI=10.1016/j.cub.2019.02.025;
RA He L., Gulyanon S., Mihovilovic Skanata M., Karagyozov D., Heckscher E.S.,
RA Krieg M., Tsechpenakis G., Gershow M., Tracey W.D. Jr.;
RT "Direction Selectivity in Drosophila Proprioceptors Requires the
RT Mechanosensory Channel Tmc.";
RL Curr. Biol. 29:945-956(2019).
RN [6] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=31184585; DOI=10.7554/elife.46165;
RA Wu S.F., Ja Y.L., Zhang Y.J., Yang C.H.;
RT "Sweet neurons inhibit texture discrimination by signaling TMC-expressing
RT mechanosensitive neurons in Drosophila.";
RL Elife 8:0-0(2019).
RN [7] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=32649914; DOI=10.1016/j.cub.2020.05.076;
RA Zhang L., Yu J., Guo X., Wei J., Liu T., Zhang W.;
RT "Parallel Mechanosensory Pathways Direct Oviposition Decision-Making in
RT Drosophila.";
RL Curr. Biol. 30:3075-3088(2020).
CC -!- FUNCTION: Probable ion channel (PubMed:27478019, PubMed:30853433,
CC PubMed:31184585, PubMed:32649914). Component of mechanosensitive
CC neurons that participates in proprioception, sensing food texture, and
CC directing egg-laying site selection (oviposition) (PubMed:27478019,
CC PubMed:27298354, PubMed:30853433, PubMed:31184585, PubMed:32649914).
CC Component of multi-dendritic neurons of the labellum (md-L) where it is
CC required for sensing the hardness and viscosity of their food, enabling
CC them to behaviorally discriminate their preferred softness and
CC smoothness from harder and stickier food options (PubMed:27478019).
CC Required as part of oviposition site selection process to relay
CC mechanosensory and chemosensory information on the hardness and
CC sweetness of potential egg-laying substrates, thus ensuring females
CC select the most optimal site for their eggs survival (PubMed:31184585,
CC PubMed:32649914). Females determine the softest substrate for their
CC eggs first by making a coarse evaluation of substrate hardness using
CC mechanosensitive channels nan and Piezo in the leg tarsal bristles,
CC followed by a much finer assessment using nan, iav and Tmc
CC mechanosensitive channels on the labellum (PubMed:31184585,
CC PubMed:32649914). This protein is required to sense subtle differences
CC in substrate stiffness (between 0.25% and 0.3% agarose), likely acting
CC in the md-L neurons (PubMed:32649914). Also required in neurons on the
CC labellum, including the md-Ls, and possibly in the brain, to inhibit
CC discrimination of egg-laying substrates of different hardness if the
CC substrate contains sucrose (PubMed:32649914). During oviposition
CC evaluation, activation of sweet neurons by sucrose enhances the
CC activity of the Tmc neurons resulting in females losing their softness
CC preference in favor of egg-laying sites that contain sucrose
CC (PubMed:32649914). Acts in the larvae peripheral sensory neurons, to
CC contribute to proprioception and sensory feedback for normal forward
CC crawling behavior (PubMed:27298354, PubMed:30853433). Required for the
CC normal activity of the proprioceptive sensory dendrites, ddaE which
CC show preferential responses to forward locomotion, and ddaD which show
CC preferential responses to backward locomotion (PubMed:30853433).
CC {ECO:0000269|PubMed:27298354, ECO:0000269|PubMed:27478019,
CC ECO:0000269|PubMed:30853433, ECO:0000269|PubMed:31184585,
CC ECO:0000269|PubMed:32649914}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}. Cell projection, dendrite
CC {ECO:0000269|PubMed:27478019}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=C {ECO:0000312|FlyBase:FBgn0267796};
CC IsoId=A0A0U1QT59-1; Sequence=Displayed;
CC Name=D {ECO:0000312|FlyBase:FBgn0267796};
CC IsoId=A0A0U1QT59-2; Sequence=VSP_061215;
CC -!- TISSUE SPECIFICITY: Expressed in multi-dendritic neurons of the
CC labellum (md-L), which extend elaborate dendritic arbors innervating
CC the bases of taste hairs (at protein level) (PubMed:27478019). In
CC larvae, expressed in class I and class II dendritic arborization (da)
CC neurons and bipolar dendrite (bd) neurons (at protein level)
CC (PubMed:27298354). In adults, expressed in various sensory neurons
CC including those in the mouth parts, olfactory neurons in the antenna,
CC wing bristle neurons, haltere neurons, arista neurons, and many other
CC sensory neurons, including a subset of chordotonal (Cho) neurons
CC (PubMed:27478019, PubMed:27298354). Expressed in md-L axon terminals,
CC including those that project into the subesophageal zone (SEZ)
CC (PubMed:27478019, PubMed:31184585). Also expressed in a small number of
CC local neurons in the adult ventral nerve cord (VNC), and projections
CC extending from a few neurons in the legs or wing hinges
CC (PubMed:27478019). In the adult mouth, expressed in a few multi-
CC dendritic neurons of the ventral cibarial sensory organ (VCSO); the
CC multiple elaborate dendritic branches form a brush-like structure that
CC faces the luminal side of the food-passing tunnel (PubMed:27478019).
CC Also expressed in the oviduct and uterus of adult females
CC (PubMed:32649914). {ECO:0000269|PubMed:27298354,
CC ECO:0000269|PubMed:27478019, ECO:0000269|PubMed:31184585,
CC ECO:0000269|PubMed:32649914}.
CC -!- DISRUPTION PHENOTYPE: Viable and appear morphologically normal
CC (PubMed:27478019). Adults display a significant reduction in the
CC electrophysiological responses of multi-dendritic neurons of the
CC labellum (md-L) to mechanical stimuli (PubMed:27478019). Adults are
CC unable to discriminate between the preferred softness (1% agarose) or
CC smoothness (sucrose solution only) from harder or stickier food options
CC (PubMed:27478019). Adult females display a reduced ability to
CC discriminate between small differences in egg-laying substrate
CC stiffness (PubMed:32649914). Larvae display abnormal locomotion
CC behaviors that likely result from the loss of proprioceptive feedback
CC (PubMed:27298354, PubMed:30853433). Displays reduced sensitivity to
CC movement direction due to decreased activity of the dorsal
CC proprioceptors neurons ddaD, which are activated during backward
CC movement, and ddaE neurons which are activated during forward movement
CC (PubMed:30853433). As a consequence, larvae crawling speed is reduced
CC due to increased head curl behavior and increased backward locomotion
CC (PubMed:27298354). No obvious defects in larvae dendrite morphology of
CC class I da neurons or axon targeting of neurons in the ventral nerve
CC cord (PubMed:27298354). Adults display a normal avoidance of bitter
CC tastes such as quinine, denatonium, strychnine and berberine, and L4
CC and S6 sensilla display normal electrophysiological responses to salt,
CC sucrose and caffeine (PubMed:27478019). {ECO:0000269|PubMed:27298354,
CC ECO:0000269|PubMed:27478019, ECO:0000269|PubMed:30853433,
CC ECO:0000269|PubMed:32649914}.
CC -!- SIMILARITY: Belongs to the TMC family. {ECO:0000305}.
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DR EMBL; AE014296; AAF50239.5; -; Genomic_DNA.
DR EMBL; AE014296; AFH04369.1; -; Genomic_DNA.
DR RefSeq; NP_001303362.1; NM_001316433.1.
DR AlphaFoldDB; A0A0U1QT59; -.
DR STRING; 7227.FBpp0293143; -.
DR TCDB; 1.A.17.4.9; the calcium-dependent chloride channel (ca-clc) family.
DR EnsemblMetazoa; FBtr0347573; FBpp0312604; FBgn0267796. [A0A0U1QT59-1]
DR EnsemblMetazoa; FBtr0347574; FBpp0312605; FBgn0267796. [A0A0U1QT59-2]
DR GeneID; 26067066; -.
DR KEGG; dme:Dmel_CG46121; -.
DR CTD; 26067066; -.
DR FlyBase; FBgn0267796; Tmc.
DR VEuPathDB; VectorBase:FBgn0267796; -.
DR eggNOG; ENOG502QQGX; Eukaryota.
DR GeneTree; ENSGT01050000244894; -.
DR HOGENOM; CLU_001915_0_0_1; -.
DR OMA; FPVKEPH; -.
DR OrthoDB; 73310at2759; -.
DR BioGRID-ORCS; 26067066; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 26067066; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0267796; Expressed in mouthpart and 1 other tissue.
DR ExpressionAtlas; A0A0U1QT59; baseline and differential.
DR GO; GO:0030425; C:dendrite; IMP:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0008381; F:mechanosensitive ion channel activity; IBA:GO_Central.
DR GO; GO:0007635; P:chemosensory behavior; IMP:UniProtKB.
DR GO; GO:0001582; P:detection of chemical stimulus involved in sensory perception of sweet taste; IMP:UniProtKB.
DR GO; GO:0050974; P:detection of mechanical stimulus involved in sensory perception; IMP:UniProtKB.
DR GO; GO:0008345; P:larval locomotory behavior; IMP:FlyBase.
DR GO; GO:0019232; P:perception of rate of movement; IMP:UniProtKB.
DR GO; GO:1905792; P:positive regulation of mechanosensory behavior; IMP:UniProtKB.
DR GO; GO:0019230; P:proprioception; IMP:FlyBase.
DR GO; GO:1905790; P:regulation of mechanosensory behavior; IMP:UniProtKB.
DR GO; GO:0046662; P:regulation of oviposition; IMP:UniProtKB.
DR InterPro; IPR038900; TMC.
DR InterPro; IPR012496; TMC_dom.
DR PANTHER; PTHR23302; PTHR23302; 1.
DR Pfam; PF07810; TMC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Ion channel;
KW Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..2036
FT /note="Transmembrane channel-like protein"
FT /id="PRO_0000453924"
FT TOPO_DOM 1..353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..395
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 396..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..432
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..526
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 548..567
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 568..588
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 589..599
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 600..620
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 621..1308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1309..1329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1330..1358
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1359..1379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1380..1423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1424..1444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1445..2036
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 1..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 996..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1186..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1527..1572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1592..1841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1859..1990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..965
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1027
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1187..1205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1527..1570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1598..1613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1616..1645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1724..1745
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1779..1793
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1804..1840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..104
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_061215"
SQ SEQUENCE 2036 AA; 227308 MW; 942BE7480672B0C3 CRC64;
MQNDEEPAAA AGTSGLSNGE SLRSPPAPAP RRPKPGILRL DIGKPRRSSG GSVDFRCVGS
SSSNGNTSNV ATGANSENNS GVTSPHQLSV TWAPPCDLDR GGWQMQSSAD AKREFYKGQR
GRRAASQEDH RSYELNDFPL QNQSSDAESC HQEPHFAHQR SPGIGFDEDG GGGDIDDEES
YTISVSAIMQ RRASVRGYRG KRGSRSSRRA SSPMDHVLDS VERRRSSVYT TSSEEGTNQE
STQEQIFENI RLHKEVIQSV KLQPWPIRKK LKLVRQAKTY VARHEGALQE RFAMSRSTRD
LWARFKILMA ARWRHWKRET ASFLTVLIPW ELRIKEIESH FGSGVASYFT FLRWLMWVNI
MIAIPLVAFV IGPEYFATKH GETDPRKRMS DPEARVAGNL FTFWEFEGYL KYSPMFYGYY
SSTSGISTSG YKLPLAYFLT AVLVYIYSFV ATLRKMAENS RNSKLSSKDD ECVFSWKLFT
GWDFMIGHAE TAHNRIASVV VGFKEALLEE AEKKKDNRNW RVILQRILVN ILVMGLLGLS
GATVVLLVNH SEDLAKHDNW LSRNAVNVTM TLLSFFLPMI FEALGLFENW HPRQQLRLQL
ARIMILNMLN LYSLMFSFIY KINSKEKPLQ MLKLENETNT MELKNLLSSI EALRAMTPTT
SLYGESTSDG LFDDSTSTAT WGEDGGGLFS TTAAAALIST TVQRLKCYNM TVKCSKLRRN
IISGKHLATT LMVLNLTTPA MVPPTLPTTL PTTFPTTLPT TLPTTLPTAL PTTLPTTLPT
TLPSTLATTT ATTSSIWSTT EETSPTTTTT SPWTTLPPST TTTEATTTTE RATTTTEATS
TTTLKITTAE INSTLSDTTK PLGKSIDTEI PNSTTNSATL STIPATLNTT NLPLNSTTKL
TTTTSTEKPQ GEDNFIYTTG EDEGSYDYGS DSTSDAPDNN SYSDITDYSS EPSEIEDFDE
QESTDQADDP LAKVLEQLDE NETKGRRKRA LAESPFFTSK YSRRHRNESA VSAGQPRETT
ESVNATPSRW PFNWASFRQT TPRTTTTRRV PSGILTKEEW ERLRRLRGRI TTTTSTSTTS
TTTRRPRWRY RTTTTELTST TEEESSTTES STDSSSPGST TNAFDSSSST TEEDEYTTTE
GSENRPYYVG YVDISEMGST IYYDGDSEFL EECVITICPK GDDFFGSTTE SPDSTTQSSD
SKQLTTVKLT PLERKQKRLK EVQLAIKQIQ TNLTTMCWET SLGQELSKVI VFDGLMSIVA
PLCIDFLRAL FVRYVNQNWC WDMEKTFPQY GDFKIAENIL TLINNQGQVW MGIFFSPGLV
LINLVKLMIM MYFRSWIVLT CNVPHEVVFK ASKSNNFYLS LLLTMLFLCV LPVGYAIVWL
RPSWHCGPFS EYNRIAEFIT NTTRNALPKQ LHEPLDYLTS SSTVIPLLLL LILIIYYLVS
LTGALREANQ DLRTQLQKER EEERKKIFKV PEVKQAEPTA TTLTNRWRKV LEASSPVTPT
QPPDFDTEEY KNQARKELIS RIMKKALRKG SATSDEDSFV RRDDDDTDTE HQDSLPHDEE
AKDKRFGLSR LQQIRRTRKP SLVDIVQIAK QERARAGSIV AGTSSSGTGN FPIKETHPKS
RFKVEKHERK DRGSMKDKKD TRHRQSPQQQ QQPPPYESPK DNEHDPDTNS RIVSASLLRR
HKEQAEGEEP PTTPDAPQTP NSPVEPVEQA LEESTPETPT LAKSKFHIVD EKKPPPHEVE
DKPLPTPKES GSGGGSLGKF KFRKHKFKSN NVAAVKPEPE VFKFDERSVE RSSDVPATHA
AEYLNNEPSG TEEQDRSLPS PTPSQGQGHH QRQLSVLSRQ GRKKIGNLLA LVREAVNLKK
DDVEQAGSDE SPGPTTPTYL AYTPPPPPSV LSSVSSSTAL EMPPTPEPES PTPSAPLHFG
SSTSSRAPSK PPKPPMVPAS ATAPTATMDD LEELDTAGPI TFPRRSDSHR RRTMRQDSQS
SIWSDNIPTI TISTTGSDEC IVDAAAPQNG LPDPRSASPE PTVNIIRIDI ENEHEK
