PBURS_DROME
ID PBURS_DROME Reviewed; 141 AA.
AC Q9VJS7; D4G7E2;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Partner of bursicon;
DE AltName: Full=Bursicon subunit beta;
DE Flags: Precursor;
GN Name=Pburs {ECO:0000312|FlyBase:FBgn0264810}; Synonyms=burs-beta;
GN ORFNames=CG15284;
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:CAH74224.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH BURS.
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 [2] {ECO:0000305, ECO:0000312|EMBL:AAX18442.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH BURS, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, 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).
RN [3] {ECO:0000312|EMBL:AAF53396.1}
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAF53396.1}
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 MRNA].
RC STRAIN=Berkeley; TISSUE=Testis;
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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:15703293, ECO:0000269|PubMed:15811337}.
CC -!- SUBUNIT: Heterodimer with Burs; 2 cystine knot polypeptides.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15703293}.
CC -!- TISSUE SPECIFICITY: Coexpressed with CCAP in most CCAP-specific
CC neurons. Coexpressed with Burs in 4 bilateral neurons in thoracic and
CC abdominal neuromeres of the ventral nervous system.
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}.
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DR EMBL; AJ862524; CAH74224.1; -; mRNA.
DR EMBL; AY823257; AAX18442.1; -; mRNA.
DR EMBL; AE014134; AAF53396.1; -; Genomic_DNA.
DR EMBL; BT122094; ADE06700.1; -; mRNA.
DR RefSeq; NP_609712.1; NM_135868.2.
DR AlphaFoldDB; Q9VJS7; -.
DR BioGRID; 60869; 5.
DR IntAct; Q9VJS7; 2.
DR STRING; 7227.FBpp0080207; -.
DR PaxDb; Q9VJS7; -.
DR DNASU; 34845; -.
DR EnsemblMetazoa; FBtr0080634; FBpp0080207; FBgn0264810.
DR GeneID; 34845; -.
DR KEGG; dme:Dmel_CG15284; -.
DR CTD; 34845; -.
DR FlyBase; FBgn0264810; Pburs.
DR VEuPathDB; VectorBase:FBgn0264810; -.
DR eggNOG; ENOG502S111; Eukaryota.
DR HOGENOM; CLU_145016_0_0_1; -.
DR InParanoid; Q9VJS7; -.
DR OMA; SKECYCC; -.
DR OrthoDB; 1461272at2759; -.
DR PhylomeDB; Q9VJS7; -.
DR BioGRID-ORCS; 34845; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34845; -.
DR PRO; PR:Q9VJS7; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0264810; Expressed in neuron and 3 other tissues.
DR Genevisible; Q9VJS7; DM.
DR GO; GO:0031395; C:bursicon neuropeptide hormone complex; IDA:FlyBase.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IDA:UniProtKB.
DR GO; GO:0005184; F:neuropeptide hormone activity; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0007593; P:chitin-based cuticle sclerotization; IMP:UniProtKB.
DR GO; GO:0018990; P:ecdysis, chitin-based cuticle; IMP:FlyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR034441; Bursicon_suB.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR PANTHER; PTHR41151; PTHR41151; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Hormone; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..141
FT /note="Partner of bursicon"
FT /evidence="ECO:0000255"
FT /id="PRO_0000223891"
FT DOMAIN 32..127
FT /note="CTCK"
FT /evidence="ECO:0000255"
FT DISULFID 32..90
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID 56..105
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID 65..131
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID 69..133
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID 87..136
FT /evidence="ECO:0000250|UniProtKB:P04275"
FT DISULFID 89
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P04275"
SQ SEQUENCE 141 AA; 16049 MW; E9C3802FFC97D41E CRC64;
MHVQELLFVA AILVPQCLRA LRYSQGTGDE NCETLKSEIH LIKEEFDELG RMQRTCNADV
IVNKCEGLCN SQVQPSVITP TGFLKECYCC RESFLKEKVI TLTHCYDPDG TRLTSPEMGS
MDIRLREPTE CKCFKCGDFT R
