BURS_DROME
ID BURS_DROME Reviewed; 173 AA.
AC Q9VD83; A0APJ5; Q573B6;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Bursicon;
DE AltName: Full=Bursicon subunit alpha;
DE AltName: Full=Cuticle-tanning hormone;
DE Flags: Precursor;
GN Name=Burs {ECO:0000312|FlyBase:FBgn0038901}; Synonyms=burs-alpha;
GN ORFNames=CG13419;
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:0000305, ECO:0000312|EMBL:AAT72327.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF CYS-115; THR-130 AND GLY-148.
RX PubMed=15242619; DOI=10.1016/j.cub.2004.06.051;
RA Dewey E.M., McNabb S.L., Ewer J., Kuo G.R., Takanishi C.L., Truman J.W.,
RA Honegger H.-W.;
RT "Identification of the gene encoding bursicon, an insect neuropeptide
RT responsible for cuticle sclerotization and wing spreading.";
RL Curr. Biol. 14:1208-1213(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH PBURS.
RX PubMed=15811337; DOI=10.1016/j.febslet.2005.03.006;
RA Mendive F.M., Van Loy T., Claeysen S., Poels J., Williamson M., Hauser F.,
RA Grimmelikhuijzen C.J.P., Vassart G., Vanden Broeck J.J.M.;
RT "Drosophila molting neurohormone bursicon is a heterodimer and the natural
RT agonist of the orphan receptor DLGR2.";
RL FEBS Lett. 579:2171-2176(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ZBMEL131, ZBMEL145, ZBMEL157, ZBMEL186, ZBMEL191, ZBMEL229,
RC ZBMEL377, ZBMEL384, ZBMEL398, ZBMEL82, ZBMEL84, and ZBMEL95;
RX PubMed=16951084; DOI=10.1534/genetics.106.058008;
RA Proeschel M., Zhang Z., Parsch J.;
RT "Widespread adaptive evolution of Drosophila genes with sex-biased
RT expression.";
RL Genetics 174:893-900(2006).
RN [4] {ECO:0000312|EMBL:AAF55915.1}
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 [5]
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 [6]
RP FUNCTION, INTERACTION WITH PBURS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=15703293; DOI=10.1073/pnas.0409916102;
RA Luo C.-W., Dewey E.M., Sudo S., Ewer J., Hsu S.Y., Honegger H.-W.,
RA Hsueh A.J.W.;
RT "Bursicon, the insect cuticle-hardening hormone, is a heterodimeric cystine
RT knot protein that activates G protein-coupled receptor LGR2.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:2820-2825(2005).
CC -!- FUNCTION: Final heterodimeric neurohormone released at the end of the
CC molting cycle, involved in the sclerotization (tanning) of the insect
CC cuticle, melanization and wing spreading. Heterodimer specifically
CC activates the G protein-coupled receptor rk.
CC {ECO:0000269|PubMed:15242619, ECO:0000269|PubMed:15703293,
CC ECO:0000269|PubMed:15811337}.
CC -!- SUBUNIT: Heterodimer of Burs and Pburs.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15242619,
CC ECO:0000269|PubMed:15703293}.
CC -!- TISSUE SPECIFICITY: Expressed in one to two pairs of neurons in each of
CC the thoracic and abdominal neuromeres of the larval CNS. Coexpressed
CC with CCAP in most CCAP-specific neurons. Coexpressed with Pburs in four
CC bilateral neurons in thoracic and abdominal neuromeres of the ventral
CC nervous system. {ECO:0000269|PubMed:15242619,
CC ECO:0000269|PubMed:15703293}.
CC -!- DEVELOPMENTAL STAGE: Expression is low in larval stages and increases
CC before ecdysis; consistent with role in postecdysial cuticle changes.
CC {ECO:0000269|PubMed:15703293}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY672905; AAT72327.1; -; mRNA.
DR EMBL; AY672906; AAT72328.1; -; Genomic_DNA.
DR EMBL; AJ862523; CAH74223.1; -; mRNA.
DR EMBL; AM294583; CAL26566.1; -; Genomic_DNA.
DR EMBL; AM294584; CAL26567.1; -; Genomic_DNA.
DR EMBL; AM294585; CAL26568.1; -; Genomic_DNA.
DR EMBL; AM294586; CAL26569.1; -; Genomic_DNA.
DR EMBL; AM294587; CAL26570.1; -; Genomic_DNA.
DR EMBL; AM294588; CAL26571.1; -; Genomic_DNA.
DR EMBL; AM294589; CAL26572.1; -; Genomic_DNA.
DR EMBL; AM294590; CAL26573.1; -; Genomic_DNA.
DR EMBL; AM294591; CAL26574.1; -; Genomic_DNA.
DR EMBL; AM294592; CAL26575.1; -; Genomic_DNA.
DR EMBL; AM294593; CAL26576.1; -; Genomic_DNA.
DR EMBL; AM294594; CAL26577.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF55915.1; -; Genomic_DNA.
DR RefSeq; NP_650983.1; NM_142726.2.
DR AlphaFoldDB; Q9VD83; -.
DR BioGRID; 67525; 4.
DR STRING; 7227.FBpp0083529; -.
DR PaxDb; Q9VD83; -.
DR DNASU; 42560; -.
DR EnsemblMetazoa; FBtr0084131; FBpp0083529; FBgn0038901.
DR GeneID; 42560; -.
DR KEGG; dme:Dmel_CG13419; -.
DR CTD; 42560; -.
DR FlyBase; FBgn0038901; Burs.
DR VEuPathDB; VectorBase:FBgn0038901; -.
DR eggNOG; KOG1216; Eukaryota.
DR HOGENOM; CLU_132265_0_0_1; -.
DR InParanoid; Q9VD83; -.
DR OMA; FACTGRC; -.
DR OrthoDB; 1517793at2759; -.
DR PhylomeDB; Q9VD83; -.
DR BioGRID-ORCS; 42560; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 42560; -.
DR PRO; PR:Q9VD83; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038901; Expressed in neuron and 8 other tissues.
DR ExpressionAtlas; Q9VD83; baseline and differential.
DR Genevisible; Q9VD83; DM.
DR GO; GO:0031395; C:bursicon neuropeptide hormone complex; IDA:FlyBase.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0043195; C:terminal bouton; IDA:FlyBase.
DR GO; GO:0005179; F:hormone activity; IMP:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0030709; P:border follicle cell delamination; IMP:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0007593; P:chitin-based cuticle sclerotization; IMP:UniProtKB.
DR GO; GO:0048067; P:cuticle pigmentation; IMP:UniProtKB.
DR GO; GO:0036335; P:intestinal stem cell homeostasis; IMP:FlyBase.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR006207; Cys_knot_C.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR004133; DAN.
DR Pfam; PF03045; DAN; 1.
DR PROSITE; PS01225; CTCK_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Hormone; Reference proteome; Secreted; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..173
FT /note="Bursicon"
FT /id="PRO_0000020837"
FT DOMAIN 52..142
FT /note="CTCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT DISULFID 52..101
FT /evidence="ECO:0000250|UniProtKB:P04275,
FT ECO:0000255|PROSITE-ProRule:PRU00039"
FT DISULFID 66..115
FT /evidence="ECO:0000250|UniProtKB:P04275,
FT ECO:0000255|PROSITE-ProRule:PRU00039"
FT DISULFID 76..136
FT /evidence="ECO:0000250|UniProtKB:P04275,
FT ECO:0000255|PROSITE-ProRule:PRU00039"
FT DISULFID 80..138
FT /evidence="ECO:0000250|UniProtKB:P04275,
FT ECO:0000255|PROSITE-ProRule:PRU00039"
FT DISULFID 98..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT DISULFID 100
FT /note="Interchain"
FT /evidence="ECO:0000303|PubMed:15242619"
FT MUTAGEN 115
FT /note="C->Y: In allele Z1091; wing expansion defects,
FT failure to sclerotize cuticle."
FT /evidence="ECO:0000269|PubMed:15242619"
FT MUTAGEN 130
FT /note="T->C: In allele Z1140; wing expansion defects."
FT /evidence="ECO:0000269|PubMed:15242619"
FT MUTAGEN 148
FT /note="G->C: In allele Z5569; wing expansion defects,
FT failure to sclerotize cuticle."
FT /evidence="ECO:0000269|PubMed:15242619"
SQ SEQUENCE 173 AA; 19223 MW; DFAF0EBEE5F162E6 CRC64;
MLRHLLRHEN NKVFVLILLY CVLVSILKLC TAQPDSSVAA TDNDITHLGD DCQVTPVIHV
LQYPGCVPKP IPSFACVGRC ASYIQVSGSK IWQMERSCMC CQESGEREAA VSLFCPKVKP
GERKFKKVLT KAPLECMCRP CTSIEESGII PQEIAGYSDE GPLNNHFRRI ALQ