TRPL_DROME
ID TRPL_DROME Reviewed; 1124 AA.
AC P48994; C6TPC1; Q0E9E3; Q8IH62; Q8MKU9; Q9V5B2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Transient-receptor-potential-like protein;
GN Name=trpl; ORFNames=CG18345;
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], CALMODULIN-BINDING, AND TISSUE SPECIFICITY.
RC STRAIN=Oregon-R;
RX PubMed=1314616; DOI=10.1016/0896-6273(92)90085-r;
RA Phillips A.M., Bull A.L., Kelly L.E.;
RT "Identification of a Drosophila gene encoding a calmodulin-binding protein
RT with homology to the trp phototransduction gene.";
RL Neuron 8:631-642(1992).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP CALMODULIN-BINDING.
RX PubMed=8670063; DOI=10.1042/bj3140497;
RA Warr C.G., Kelly L.E.;
RT "Identification and characterization of two distinct calmodulin-binding
RT sites in the Trpl ion-channel protein of Drosophila melanogaster.";
RL Biochem. J. 314:497-503(1996).
RN [7]
RP INTERACTION WITH TRP.
RX PubMed=9215637; DOI=10.1016/s0092-8674(00)80302-5;
RA Xu X.-Z.S., Li H.-S., Guggino W.B., Montell C.;
RT "Coassembly of TRP and TRPL produces a distinct store-operated
RT conductance.";
RL Cell 89:1155-1164(1997).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TRP-713 AND TRP-814.
RX PubMed=9494079; DOI=10.1042/bj3301149;
RA Lan L., Brereton H., Barritt G.J.;
RT "The role of calmodulin-binding sites in the regulation of the Drosophila
RT TRPL cation channel expressed in Xenopus laevis oocytes by ca2+, inositol
RT 1,4,5-trisphosphate and GTP-binding proteins.";
RL Biochem. J. 330:1149-1158(1998).
RN [9]
RP CALMODULIN-BINDING.
RX PubMed=10371201; DOI=10.1016/s0014-5793(99)00588-8;
RA Trost C., Marquart A., Zimmer S., Philipp S., Cavalie A., Flockerzi V.;
RT "Ca2+-dependent interaction of the trpl cation channel and calmodulin.";
RL FEBS Lett. 451:257-263(1999).
RN [10]
RP FUNCTION.
RX PubMed=9930700; DOI=10.1038/16703;
RA Chyb S., Raghu P., Hardie R.C.;
RT "Polyunsaturated fatty acids activate the Drosophila light-sensitive
RT channels TRP and TRPL.";
RL Nature 397:255-259(1999).
RN [11]
RP FUNCTION.
RX PubMed=10908615; DOI=10.1523/jneurosci.20-15-05748.2000;
RA Agam K., von Campenhausen M., Levy S., Ben-Ami H.C., Cook B.,
RA Kirschfeld K., Minke B.;
RT "Metabolic stress reversibly activates the Drosophila light-sensitive
RT channels TRP and TRPL in vivo.";
RL J. Neurosci. 20:5748-5755(2000).
RN [12]
RP FUNCTION.
RX PubMed=8918461; DOI=10.1002/j.1460-2075.1996.tb00970.x;
RA Obukhov A.G., Harteneck C., Zobel A., Harhammer R., Kalkbrenner F.,
RA Leopoldt D., Luckhoff A., Nurnberg B., Schultz G.;
RT "Direct activation of trpl cation channels by G alpha11 subunits.";
RL EMBO J. 15:5833-5838(1996).
RN [13]
RP INTERACTION WITH TRPGAMMA.
RX PubMed=10896160; DOI=10.1016/s0896-6273(00)81201-5;
RA Xu X.-Z.S., Chien F., Butler A., Salkoff L., Montell C.;
RT "TRPgamma, a Drosophila TRP-related subunit, forms a regulated cation
RT channel with TRPL.";
RL Neuron 26:647-657(2000).
RN [14]
RP INTERACTION WITH FKBP59, IDENTIFICATION IN A COMPLEX WITH INAD, AND
RP MUTAGENESIS OF PRO-702 AND PRO-709.
RX PubMed=11514552; DOI=10.1074/jbc.m104125200;
RA Goel M., Garcia R., Estacion M., Schilling W.P.;
RT "Regulation of Drosophila TRPL channels by immunophilin FKBP59.";
RL J. Biol. Chem. 276:38762-38773(2001).
RN [15]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11931743; DOI=10.1016/s0896-6273(02)00630-x;
RA Baehner M., Frechter S., Da Silva N., Minke B., Paulsen R., Huber A.;
RT "Light-regulated subcellular translocation of Drosophila TRPL channels
RT induces long-term adaptation and modifies the light-induced current.";
RL Neuron 34:83-93(2002).
RN [16]
RP REVIEW.
RX PubMed=11707492; DOI=10.1242/jeb.204.20.3403;
RA Hardie R.C.;
RT "Phototransduction in Drosophila melanogaster.";
RL J. Exp. Biol. 204:3403-3409(2001).
CC -!- FUNCTION: A light-sensitive calcium channel that is required for
CC inositide-mediated Ca(2+) entry in the retina during phospholipase C
CC (PLC)-mediated phototransduction. Required for vision in the dark and
CC in dim light. Binds calmodulin. Trp and trpl act together in the light
CC response, although it is unclear whether as heteromultimers or distinct
CC units. Also forms a functional cation channel with Trpgamma. Activated
CC by fatty acids, metabolic stress, inositols and GTP-binding proteins.
CC {ECO:0000269|PubMed:10908615, ECO:0000269|PubMed:11931743,
CC ECO:0000269|PubMed:8918461, ECO:0000269|PubMed:9494079,
CC ECO:0000269|PubMed:9930700}.
CC -!- SUBUNIT: Forms heteromultimers with Trpgamma and, to a lower extent,
CC with trp. Interacts with Fkbp59 in vivo and is found in the inaD
CC signaling complex. {ECO:0000269|PubMed:10896160,
CC ECO:0000269|PubMed:11514552, ECO:0000269|PubMed:9215637}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11931743,
CC ECO:0000269|PubMed:9494079}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11931743, ECO:0000269|PubMed:9494079}. Note=In the
CC dark, there is 20 fold more rhabdomeral trpl protein forming plasma
CC membrane channels than in the light. In the light, the protein
CC translocates to an intracellular compartment. Protein levels remain
CC unchanged in light and dark conditions.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the rhabdomeres of
CC photoreceptor cells. {ECO:0000269|PubMed:1314616}.
CC -!- DOMAIN: Binding of calmodulin to binding site 1 is Ca(2+) dependent,
CC whereas binding of calmodulin to site 2 is Ca(2+) independent.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. STrpC
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN71152.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; M88185; AAA28979.1; -; mRNA.
DR EMBL; AE013599; AAF58904.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68793.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68794.2; -; Genomic_DNA.
DR EMBL; BT001397; AAN71152.1; ALT_SEQ; mRNA.
DR EMBL; BT099607; ACU45760.1; -; mRNA.
DR PIR; JH0588; JH0588.
DR RefSeq; NP_476895.1; NM_057547.5.
DR RefSeq; NP_724822.1; NM_165694.3.
DR RefSeq; NP_724823.2; NM_165695.2.
DR AlphaFoldDB; P48994; -.
DR SMR; P48994; -.
DR BioGRID; 61834; 10.
DR IntAct; P48994; 2.
DR STRING; 7227.FBpp0290876; -.
DR TCDB; 1.A.4.1.8; the transient receptor potential ca(2+) channel (trp-cc) family.
DR PaxDb; P48994; -.
DR PRIDE; P48994; -.
DR EnsemblMetazoa; FBtr0088471; FBpp0087555; FBgn0005614.
DR EnsemblMetazoa; FBtr0088473; FBpp0087557; FBgn0005614.
DR EnsemblMetazoa; FBtr0301662; FBpp0290876; FBgn0005614.
DR GeneID; 36003; -.
DR KEGG; dme:Dmel_CG18345; -.
DR UCSC; CG18345-RA; d. melanogaster.
DR CTD; 36003; -.
DR FlyBase; FBgn0005614; trpl.
DR VEuPathDB; VectorBase:FBgn0005614; -.
DR eggNOG; KOG3609; Eukaryota.
DR GeneTree; ENSGT01050000244985; -.
DR HOGENOM; CLU_005716_0_1_1; -.
DR InParanoid; P48994; -.
DR OMA; MCAPNCR; -.
DR OrthoDB; 824310at2759; -.
DR PhylomeDB; P48994; -.
DR BioGRID-ORCS; 36003; 0 hits in 3 CRISPR screens.
DR ChiTaRS; trpl; fly.
DR GenomeRNAi; 36003; -.
DR PRO; PR:P48994; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0005614; Expressed in head capsule and 12 other tissues.
DR ExpressionAtlas; P48994; baseline and differential.
DR Genevisible; P48994; DM.
DR GO; GO:0034703; C:cation channel complex; IPI:FlyBase.
DR GO; GO:0030425; C:dendrite; IDA:FlyBase.
DR GO; GO:0016027; C:inaD signaling complex; IPI:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0016028; C:rhabdomere; IDA:FlyBase.
DR GO; GO:0035997; C:rhabdomere microvillus membrane; IDA:FlyBase.
DR GO; GO:0005262; F:calcium channel activity; IDA:FlyBase.
DR GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0005261; F:cation channel activity; IDA:FlyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:FlyBase.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IBA:GO_Central.
DR GO; GO:0015075; F:ion transmembrane transporter activity; NAS:UniProtKB.
DR GO; GO:0010461; F:light-activated ion channel activity; IDA:FlyBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0015279; F:store-operated calcium channel activity; IBA:GO_Central.
DR GO; GO:0007589; P:body fluid secretion; IMP:FlyBase.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IGI:FlyBase.
DR GO; GO:0006816; P:calcium ion transport; IDA:FlyBase.
DR GO; GO:0019722; P:calcium-mediated signaling; IMP:FlyBase.
DR GO; GO:0006812; P:cation transport; IDA:FlyBase.
DR GO; GO:0071454; P:cellular response to anoxia; IGI:FlyBase.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; ISS:UniProtKB.
DR GO; GO:0006811; P:ion transport; NAS:UniProtKB.
DR GO; GO:0006828; P:manganese ion transport; IBA:GO_Central.
DR GO; GO:0007603; P:phototransduction, visible light; IMP:FlyBase.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0009416; P:response to light stimulus; TAS:FlyBase.
DR GO; GO:0007605; P:sensory perception of sound; IMP:FlyBase.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR013555; TRP_dom.
DR InterPro; IPR002153; TRPC_channel.
DR PANTHER; PTHR10117; PTHR10117; 1.
DR Pfam; PF13606; Ank_3; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF08344; TRP_2; 1.
DR PRINTS; PR01097; TRNSRECEPTRP.
DR SMART; SM00248; ANK; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Calcium; Calcium channel; Calcium transport;
KW Calmodulin-binding; Ion channel; Ion transport; Membrane;
KW Reference proteome; Repeat; Sensory transduction; Transmembrane;
KW Transmembrane helix; Transport; Vision.
FT CHAIN 1..1124
FT /note="Transient-receptor-potential-like protein"
FT /id="PRO_0000215359"
FT TOPO_DOM 1..340
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..373
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..431
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..512
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 534..548
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 549..569
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 570..645
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 646..666
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 667..1124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 40..69
FT /note="ANK 1"
FT REPEAT 78..107
FT /note="ANK 2"
FT REPEAT 152..181
FT /note="ANK 3"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..728
FT /note="Calmodulin-binding 1"
FT REGION 853..895
FT /note="Calmodulin-binding 2"
FT REGION 978..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1072
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 702
FT /note="P->Q: Abolishes interaction with Fkbp59."
FT /evidence="ECO:0000269|PubMed:11514552"
FT MUTAGEN 709
FT /note="P->Q: Abolishes interaction with Fkbp59."
FT /evidence="ECO:0000269|PubMed:11514552"
FT MUTAGEN 713
FT /note="W->G: Disrupts Ca(2+) inflow through the channel.
FT Calmodulin has little effect on Ca(2+) flow."
FT /evidence="ECO:0000269|PubMed:9494079"
FT MUTAGEN 814
FT /note="W->G: Does not abolish Ca(2+) inflow through the
FT channel. Calmodulin has no effect on initial rates."
FT /evidence="ECO:0000269|PubMed:9494079"
FT CONFLICT 228..229
FT /note="II -> SS (in Ref. 1; AAA28979)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1124 AA; 127750 MW; AF6323BA27626583 CRC64;
MGRKKKLPTG VSSGVSHASS APKSVGGCCV PLGLPQPLLL EEKKFLLAVE RGDMPNVRRI
LQKALRHQHI NINCMDPLGR RALTLAIDNE NLEMVELLVV MGVETKDALL HAINAEFVEA
VELLLEHEEL IYKEGEPYSW QKVDINTAMF APDITPLMLA AHKNNFEILR ILLDRGAAVP
VPHDIRCGCE ECVRLTAEDS LRHSLSRVNI YRALCSPSLI CLTSNDPIIT AFQLSWELRN
LALTEQECKS EYMDLRRQCQ KFAVDLLDQT RTSNELAIIL NYDPQMSSYE PGDRMSLTRL
VQAISYKQKK FVAHSNIQQL LSSIWYDGLP GFRRKSIVDK VICIAQVAVL FPLYCLIYMC
APNCRTGQLM RKPFMKFLIH ASSYLFFLFI LILVSQRADD DFVRIFGTTR MKKELAEQEL
RQRGQTPSKL ELIVVMYVIG FVWEEVQEIF AVGMKSYLRN MWNFIDFLRN SLYVSVMCLR
AFAYIQQATE IARDPQMAYI PREKWHDFDP QLIAEGLFAA ANVFSALKLV HLFSINPHLG
PLQISLGRMV IDIVKFFFIY TLVLFAFACG LNQLLWYFAA LEKSKCYVLP GGEADWGSHG
DSCMKWRRFG NLFESSQSLF WASFGMVGLD DFELSGIKSY TRFWGLLMFG SYSVINVIVL
LNLLIAMMSN SYAMIDEHSD TEWKFARTKL WMSYFEDSAT LPPPFNVLPS VKWVIRIFRK
SSKTIDRQRS KKRKEQEQFS EYDNIMRSLV WRYVAAMHRK FENNPVSEDD INEVKSEINT
MRYEMLEIFE NSGMDVSSAN KKERQPRPRR IKVWERRLMK GFQVAPVQNG CELDAFGNVN
GQGEMQEIKV ESIPSKPAKE TAKERFQRVA RTVLLQSTTH KWNVVLRAAK DSQIGRCTKN
ERKSLQNLGR AIEEAKRLIM LNPGCPSGRE SPIRIEFEDE KTSTLLELLN QISAEISDSE
KPKIRPIWRP PLKTVPARAM AANNTRSLTA PELKISRKSS PAPTPTPTPG VSHTALSQFR
NRELPLCPSK LIANSAPSAP TAPPKKSAPT APTPTYKPTT HAPFSVEGGN RENTRASDGV
RSDNSNFDIH VVDLDEKGGH LGRDNVSDIS SIASTSPQRP KHRN
