ID USP_DROME Reviewed; 508 AA.
AC P20153; Q9W535;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 27-MAR-2024, entry version 236.
DE RecName: Full=Protein ultraspiracle;
DE AltName: Full=Chorion factor 1;
DE AltName: Full=Nuclear receptor subfamily 2 group B member 4;
DE AltName: Full=XR2C;
GN Name=usp; Synonyms=Cf1, NR2B4; ORFNames=CG4380;
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].
RC TISSUE=Larva;
RX PubMed=2169594; DOI=10.1038/347298a0;
RA Oro A.E., McKeown M., Evans R.M.;
RT "Relationship between the product of the Drosophila ultraspiracle locus and
RT the vertebrate retinoid X receptor.";
RL Nature 347:298-301(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Canton-S;
RX PubMed=2165589; DOI=10.1093/nar/18.14.4143;
RA Henrich V.C., Sliter T.J., Lubahn D.B., Macintyre A., Gilbert L.I.;
RT "A steroid/thyroid hormone receptor superfamily member in Drosophila
RT melanogaster that shares extensive sequence similarity with a mammalian
RT homologue.";
RL Nucleic Acids Res. 18:4143-4148(1990).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-294.
RC TISSUE=Ovary;
RX PubMed=2120114; DOI=10.1101/gad.4.7.1128;
RA Shea M.J., King D.L., Conboy M.J., Mariani B.D., Kafatos F.C.;
RT "Proteins that bind to Drosophila chorion cis-regulatory elements: a new
RT C2H2 zinc finger protein and a C2C2 steroid receptor-like component.";
RL Genes Dev. 4:1128-1140(1990).
RN [8]
RP SUBUNIT.
RX PubMed=8247157; DOI=10.1038/366476a0;
RA Yao T.-P., Froman B.M., Jiang Z., Cherbas L., Chen J.-D., McKeown M.M.,
RA Cherbas P., Evans R.M.;
RT "Functional ecdysone receptor is the product of EcR and Ultraspiracle
RT genes.";
RL Nature 366:476-479(1993).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Receptor for ecdysone. May be an important modulator of
CC insect metamorphosis. Plays an important part in embryonic and post-
CC embryonic development. Binds to ecdysone response elements (ECRES) such
CC as in the promoter region of s15 chorion gene.
CC -!- SUBUNIT: Heterodimer of USP and ECR. Only the heterodimer is capable of
CC high-affinity binding to ecdysone. {ECO:0000269|PubMed:8247157}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC subfamily. {ECO:0000305}.
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DR EMBL; X53417; CAA37496.1; -; mRNA.
DR EMBL; X52591; CAA36827.1; -; mRNA.
DR EMBL; AE014298; AAF45707.1; -; Genomic_DNA.
DR EMBL; AL031765; CAA21122.1; -; Genomic_DNA.
DR EMBL; AY069393; AAL39538.1; -; mRNA.
DR EMBL; X53379; CAA37459.1; -; mRNA.
DR PIR; A35872; A35872.
DR PIR; T13737; T13737.
DR RefSeq; NP_001259168.1; NM_001272239.2.
DR RefSeq; NP_476781.1; NM_057433.4.
DR PDB; 1HG4; X-ray; 2.40 A; A/B/C/D/E/F=230-508.
DR PDB; 1R0O; X-ray; 2.24 A; A=94-179.
DR PDB; 2HAN; X-ray; 1.95 A; A=94-179.
DR PDBsum; 1HG4; -.
DR PDBsum; 1R0O; -.
DR PDBsum; 2HAN; -.
DR AlphaFoldDB; P20153; -.
DR SMR; P20153; -.
DR BioGRID; 57709; 35.
DR DIP; DIP-645N; -.
DR IntAct; P20153; 3.
DR STRING; 7227.FBpp0305937; -.
DR BindingDB; P20153; -.
DR ChEMBL; CHEMBL2366581; -.
DR iPTMnet; P20153; -.
DR PaxDb; 7227-FBpp0305937; -.
DR EnsemblMetazoa; FBtr0070346; FBpp0070332; FBgn0003964.
DR EnsemblMetazoa; FBtr0333803; FBpp0305937; FBgn0003964.
DR GeneID; 31165; -.
DR KEGG; dme:Dmel_CG4380; -.
DR AGR; FB:FBgn0003964; -.
DR CTD; 31165; -.
DR FlyBase; FBgn0003964; usp.
DR VEuPathDB; VectorBase:FBgn0003964; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000170897; -.
DR HOGENOM; CLU_007368_5_0_1; -.
DR InParanoid; P20153; -.
DR OMA; DEHCRQE; -.
DR OrthoDB; 5400963at2759; -.
DR PhylomeDB; P20153; -.
DR Reactome; R-DME-159418; Recycling of bile acids and salts.
DR Reactome; R-DME-200425; Carnitine metabolism.
DR Reactome; R-DME-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR Reactome; R-DME-381340; Transcriptional regulation of white adipocyte differentiation.
DR Reactome; R-DME-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-DME-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-DME-5362517; Signaling by Retinoic Acid.
DR Reactome; R-DME-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR Reactome; R-DME-9616222; Transcriptional regulation of granulopoiesis.
DR Reactome; R-DME-9623433; NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis.
DR Reactome; R-DME-9707564; Cytoprotection by HMOX1.
DR SignaLink; P20153; -.
DR BioGRID-ORCS; 31165; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; P20153; -.
DR GenomeRNAi; 31165; -.
DR PRO; PR:P20153; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003964; Expressed in cleaving embryo and 27 other cell types or tissues.
DR ExpressionAtlas; P20153; baseline and differential.
DR Genevisible; P20153; DM.
DR GO; GO:0008232; C:activator ecdysone receptor complex; IDA:FlyBase.
DR GO; GO:0030425; C:dendrite; IMP:FlyBase.
DR GO; GO:0008230; C:ecdysone receptor holocomplex; IMP:CAFA.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; NAS:FlyBase.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IMP:CAFA.
DR GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR GO; GO:0042562; F:hormone binding; IDA:FlyBase.
DR GO; GO:0008289; F:lipid binding; IDA:FlyBase.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:FlyBase.
DR GO; GO:0003707; F:nuclear steroid receptor activity; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IMP:CAFA.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IPI:CAFA.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0071390; P:cellular response to ecdysone; IDA:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; NAS:FlyBase.
DR GO; GO:0006697; P:ecdysone biosynthetic process; IMP:FlyBase.
DR GO; GO:0035076; P:ecdysone receptor-mediated signaling pathway; IDA:FlyBase.
DR GO; GO:0007281; P:germ cell development; IMP:FlyBase.
DR GO; GO:0007552; P:metamorphosis; IMP:CACAO.
DR GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
DR GO; GO:0045596; P:negative regulation of cell differentiation; TAS:FlyBase.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; TAS:FlyBase.
DR GO; GO:0016322; P:neuron remodeling; IMP:FlyBase.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0035073; P:pupariation; IMP:FlyBase.
DR GO; GO:0040034; P:regulation of development, heterochronic; TAS:FlyBase.
DR GO; GO:0046620; P:regulation of organ growth; IMP:FlyBase.
DR GO; GO:0035075; P:response to ecdysone; IMP:FlyBase.
DR GO; GO:0042594; P:response to starvation; IMP:FlyBase.
DR CDD; cd06956; NR_DBD_RXR; 1.
DR CDD; cd06943; NR_LBD_RXR_like; 1.
DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR Gene3D; 1.10.565.10; Retinoid X Receptor; 1.
DR IDEAL; IID50250; -.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR000003; Retinoid-X_rcpt/HNF4.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR48092; KNIRPS-RELATED PROTEIN-RELATED; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00545; RETINOIDXR.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Receptor; Reference proteome; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..508
FT /note="Protein ultraspiracle"
FT /id="PRO_0000053582"
FT DOMAIN 239..498
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 104..169
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 104..124
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 140..164
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..103
FT /note="Modulating"
FT /evidence="ECO:0000250"
FT REGION 21..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..223
FT /note="Hinge"
FT REGION 178..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 213
FT /note="G -> E (in Ref. 2; CAA36827)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="Missing (in Ref. 2; CAA36827)"
FT /evidence="ECO:0000305"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:2HAN"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:2HAN"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:2HAN"
FT HELIX 122..134
FT /evidence="ECO:0007829|PDB:2HAN"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:2HAN"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:2HAN"
FT HELIX 157..167
FT /evidence="ECO:0007829|PDB:2HAN"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:2HAN"
FT HELIX 240..253
FT /evidence="ECO:0007829|PDB:1HG4"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:1HG4"
FT HELIX 275..297
FT /evidence="ECO:0007829|PDB:1HG4"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:1HG4"
FT HELIX 307..329
FT /evidence="ECO:0007829|PDB:1HG4"
FT TURN 330..333
FT /evidence="ECO:0007829|PDB:1HG4"
FT STRAND 363..369
FT /evidence="ECO:0007829|PDB:1HG4"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:1HG4"
FT HELIX 374..380
FT /evidence="ECO:0007829|PDB:1HG4"
FT HELIX 383..392
FT /evidence="ECO:0007829|PDB:1HG4"
FT HELIX 394..400
FT /evidence="ECO:0007829|PDB:1HG4"
FT HELIX 404..415
FT /evidence="ECO:0007829|PDB:1HG4"
FT HELIX 426..447
FT /evidence="ECO:0007829|PDB:1HG4"
FT HELIX 454..479
FT /evidence="ECO:0007829|PDB:1HG4"
FT HELIX 487..495
FT /evidence="ECO:0007829|PDB:1HG4"
SQ SEQUENCE 508 AA; 55244 MW; 58BA37A9FD9EBE80 CRC64;
MDNCDQDASF RLSHIKEEVK PDISQLNDSN NSSFSPKAES PVPFMQAMSM VHVLPGSNSA
SSNNNSAGDA QMAQAPNSAG GSAAAAVQQQ YPPNHPLSGS KHLCSICGDR ASGKHYGVYS
CEGCKGFFKR TVRKDLTYAC RENRNCIIDK RQRNRCQYCR YQKCLTCGMK REAVQEERQR
GARNAAGRLS ASGGGSSGPG SVGGSSSQGG GGGGGVSGGM GSGNGSDDFM TNSVSRDFSI
ERIIEAEQRA ETQCGDRALT FLRVGPYSTV QPDYKGAVSA LCQVVNKQLF QMVEYARMMP
HFAQVPLDDQ VILLKAAWIE LLIANVAWCS IVSLDDGGAG GGGGGLGHDG SFERRSPGLQ
PQQLFLNQSF SYHRNSAIKA GVSAIFDRIL SELSVKMKRL NLDRRELSCL KAIILYNPDI
RGIKSRAEIE MCREKVYACL DEHCRLEHPG DDGRFAQLLL RLPALRSISL KCQDHLFLFR
ITSDRPLEEL FLEQLEAPPP PGLAMKLE
//
