PDFR_DROME
ID PDFR_DROME Reviewed; 669 AA.
AC Q9W4Y2; A0A158RFU8; M9NET6; Q9NEF7; X2JDL2;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=PDF receptor;
DE AltName: Full=Pigment-dispersing factor receptor {ECO:0000312|FlyBase:FBgn0260753};
DE AltName: Full=Protein groom-of-PDF;
GN Name=Pdfr {ECO:0000312|FlyBase:FBgn0260753};
GN Synonyms=gop {ECO:0000312|FlyBase:FBgn0260753},
GN Han {ECO:0000312|FlyBase:FBgn0260753};
GN ORFNames=CG13758 {ECO:0000312|FlyBase:FBgn0260753};
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:AAT84083.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Mertens I., Vandingenen A., De Loof A., Schoofs L.;
RT "Molecular identification of the pigment dispersing factor (PDF) receptor
RT in Drosophila melanogaster.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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 GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16242402; DOI=10.1016/j.neuron.2005.09.009;
RA Mertens I., Vandingenen A., Johnson E.C., Shafer O.T., Li W., Trigg J.S.,
RA De Loof A., Schoofs L., Taghert P.H.;
RT "PDF receptor signaling in Drosophila contributes to both circadian and
RT geotactic behaviors.";
RL Neuron 48:213-219(2005).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16242403; DOI=10.1016/j.neuron.2005.09.008;
RA Lear B.C., Merrill C.E., Lin J.-M., Schroeder A., Zhang L., Allada R.;
RT "A G protein-coupled receptor, groom-of-PDF, is required for PDF neuron
RT action in circadian behavior.";
RL Neuron 48:221-227(2005).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16242407; DOI=10.1016/j.neuron.2005.08.025;
RA Hyun S., Lee Y., Hong S.-T., Bang S., Paik D., Kang J., Shin J., Lee J.,
RA Jeon K., Hwang S., Bae E., Kim J.;
RT "Drosophila GPCR Han is a receptor for the circadian clock neuropeptide
RT PDF.";
RL Neuron 48:267-278(2005).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19038223; DOI=10.1016/j.neuron.2008.10.042;
RA Parisky K.M., Agosto J., Pulver S.R., Shang Y., Kuklin E., Hodge J.J.,
RA Kang K., Kang K., Liu X., Garrity P.A., Rosbash M., Griffith L.C.;
RT "PDF cells are a GABA-responsive wake-promoting component of the Drosophila
RT sleep circuit.";
RL Neuron 60:672-682(2008).
RN [10]
RP FUNCTION.
RX PubMed=19230663; DOI=10.1016/j.cub.2009.01.040;
RA Chung B.Y., Kilman V.L., Keath J.R., Pitman J.L., Allada R.;
RT "The GABA(A) receptor RDL acts in peptidergic PDF neurons to promote sleep
RT in Drosophila.";
RL Curr. Biol. 19:386-390(2009).
CC -!- FUNCTION: Receptor for PDF, a neuropeptide controlling circadian
CC behavioral rhythms. Probably regulates circadian behavioral rhythms
CC through coordination of activities of clock neurons. PDF-binding
CC results in the elevation of cAMP synthesis. Plays a role in sleep
CC regulation and regulates the state transition from sleep to wake
CC (PubMed:19038223, PubMed:19230663). {ECO:0000269|PubMed:16242402,
CC ECO:0000269|PubMed:16242403, ECO:0000269|PubMed:16242407,
CC ECO:0000269|PubMed:19038223, ECO:0000269|PubMed:19230663}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A {ECO:0000312|FlyBase:FBgn0260753};
CC IsoId=Q9W4Y2-1; Sequence=Displayed;
CC Name=C {ECO:0000312|FlyBase:FBgn0260753}; Synonyms=D
CC {ECO:0000312|FlyBase:FBgn0260753};
CC IsoId=Q9W4Y2-2; Sequence=VSP_061203;
CC Name=B {ECO:0000312|FlyBase:FBgn0260753};
CC IsoId=Q9W4Y2-3; Sequence=VSP_061202;
CC -!- TISSUE SPECIFICITY: Mainly present in clock neurons of the brain.
CC Localizes in all 4 s-LNv neurons, 1 LNd neuron, 7 DN1 neurons, and 1
CC DN3 neuron. In addition to the clock neurons, it is also present in
CC approximately 13 pairs of neurons along the ventral nerve cord in third
CC instar larvae, which do not overlap with dopaminergic or serotonergic
CC neurons. Not present in DN2 neurons (at protein level).
CC {ECO:0000269|PubMed:16242402, ECO:0000269|PubMed:16242403,
CC ECO:0000269|PubMed:16242407}.
CC -!- DEVELOPMENTAL STAGE: Not expressed in embryos. Does not exhibit diurnal
CC or circadian variation. {ECO:0000269|PubMed:16242402,
CC ECO:0000269|PubMed:16242407}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in small and large
CC ventral lateral neurons increases total sleep in both the day-time and
CC the nighttime and decreases sleep latency during daytime only.
CC {ECO:0000269|PubMed:19038223}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB72288.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY661807; AAT84083.1; -; mRNA.
DR EMBL; AE014298; AAF45788.2; -; Genomic_DNA.
DR EMBL; AE014298; AHN59297.1; -; Genomic_DNA.
DR EMBL; AE014298; AHN59298.1; -; Genomic_DNA.
DR EMBL; AE014298; AFH07215.1; -; Genomic_DNA.
DR EMBL; AL138972; CAB72288.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BT022705; AAY55121.1; -; mRNA.
DR RefSeq; NP_001245501.1; NM_001258572.1. [Q9W4Y2-3]
DR RefSeq; NP_001284826.1; NM_001297897.1. [Q9W4Y2-2]
DR RefSeq; NP_001284827.1; NM_001297898.1. [Q9W4Y2-2]
DR RefSeq; NP_570007.2; NM_130651.3. [Q9W4Y2-1]
DR AlphaFoldDB; Q9W4Y2; -.
DR SMR; Q9W4Y2; -.
DR BioGRID; 57768; 6.
DR STRING; 7227.FBpp0300789; -.
DR TCDB; 9.A.14.4.2; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; Q9W4Y2; 7 sites.
DR PaxDb; Q9W4Y2; -.
DR DNASU; 31234; -.
DR EnsemblMetazoa; FBtr0070436; FBpp0099841; FBgn0260753. [Q9W4Y2-1]
DR EnsemblMetazoa; FBtr0308565; FBpp0300789; FBgn0260753. [Q9W4Y2-3]
DR EnsemblMetazoa; FBtr0340084; FBpp0309083; FBgn0260753. [Q9W4Y2-2]
DR EnsemblMetazoa; FBtr0340085; FBpp0309084; FBgn0260753. [Q9W4Y2-2]
DR GeneID; 31234; -.
DR KEGG; dme:Dmel_CG13758; -.
DR CTD; 31234; -.
DR FlyBase; FBgn0260753; Pdfr.
DR VEuPathDB; VectorBase:FBgn0260753; -.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00940000167994; -.
DR HOGENOM; CLU_002753_4_7_1; -.
DR InParanoid; Q9W4Y2; -.
DR OrthoDB; 651627at2759; -.
DR PhylomeDB; Q9W4Y2; -.
DR BioGRID-ORCS; 31234; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 31234; -.
DR PRO; PR:Q9W4Y2; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0260753; Expressed in brain and 16 other tissues.
DR ExpressionAtlas; Q9W4Y2; baseline and differential.
DR Genevisible; Q9W4Y2; DM.
DR GO; GO:0016021; C:integral component of membrane; ISS:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0043005; C:neuron projection; IDA:FlyBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004948; F:calcitonin receptor activity; ISS:FlyBase.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0008188; F:neuropeptide receptor activity; IPI:UniProtKB.
DR GO; GO:0017046; F:peptide hormone binding; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0048512; P:circadian behavior; IDA:FlyBase.
DR GO; GO:0007623; P:circadian rhythm; IDA:FlyBase.
DR GO; GO:0042745; P:circadian sleep/wake cycle; IMP:FlyBase.
DR GO; GO:0060086; P:circadian temperature homeostasis; IMP:FlyBase.
DR GO; GO:0055070; P:copper ion homeostasis; IMP:FlyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:FlyBase.
DR GO; GO:0042332; P:gravitaxis; IDA:FlyBase.
DR GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:UniProtKB.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IGI:FlyBase.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:FlyBase.
DR GO; GO:0042749; P:regulation of circadian sleep/wake cycle; IMP:FlyBase.
DR GO; GO:1901562; P:response to paraquat; IMP:FlyBase.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF02793; HRM; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00008; HormR; 1.
DR SUPFAM; SSF111418; SSF111418; 1.
DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Biological rhythms; Cell membrane;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..669
FT /note="PDF receptor"
FT /id="PRO_0000070346"
FT TOPO_DOM 1..244
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..334
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..411
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 433..449
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471..480
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..501
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 502..669
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 24..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1
FT /note="M -> MGAGNRKSETKTKTEAEIEIEMERDQFSIAANACMSMGPMLISKDKA
FT PCSGGRVRHADSLHIYYAVDGKM (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_061202"
FT VAR_SEQ 646..669
FT /note="QKVLRVPSASSVPPESVVFELSEQ -> QKDKCVMPGSQKTQQIFMTSQMPP
FT TSTLAAVATTITTTSTTTTAAKTTIASIATIATMTKSKAKAKAISKSHQIQMPKA (in
FT isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_061203"
SQ SEQUENCE 669 AA; 74485 MW; ACBE93A1A83ABD5D CRC64;
MTLLSNILDC GGCISAQRFT RLLRQSGSSG PSPSAPTAGT FESKSMLEPT SSHSLATGRV
PLLHDFDAST TESPGTYVLD GVARVAQLAL EPTVMDALPD SDTEQVLGNL NSSAPWNLTL
ASAAATNFEN CSALFVNYTL PQTGLYCNWT WDTLLCWPPT PAGVLARMNC PGGFHGVDTR
KFAIRKCELD GRWGSRPNAT EVNPPGWTDY GPCYKPEIIR LMQQMGSKDF DAYIDIARRT
RTLEIVGLCL SLFALIVSLL IFCTFRSLRN NRTKIHKNLF VAMVLQVIIR LTLYLDQFRR
GNKEAATNTS LSVIENTPYL CEASYVLLEY ARTAMFMWMF IEGLYLHNMV TVAVFQGSFP
LKFFSRLGWC VPILMTTVWA RCTVMYMDTS LGECLWNYNL TPYYWILEGP RLAVILLNFC
FLVNIIRVLV MKLRQSQASD IEQTRKAVRA AIVLLPLLGI TNLLHQLAPL KTATNFAVWS
YGTHFLTSFQ GFFIALIYCF LNGEVRAVLL KSLATQLSVR GHPEWAPKRA SMYSGAYNTA
PDTDAVQPAG DPSATGKRIS PPNKRLNGRK PSSASIVMIH EPQQRQRLMP RLQNKAREKG
KDRVEKTDAE AEPDPTISHI HSKEAGSARS RTRGSKWIMG ICFRGQKVLR VPSASSVPPE
SVVFELSEQ
