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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}.
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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
 
 
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