BURS_BOMMO
ID BURS_BOMMO Reviewed; 160 AA.
AC Q566B1;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=Bursicon;
DE AltName: Full=Bursicon subunit alpha;
DE AltName: Full=Cuticle-tanning hormone;
DE Flags: Precursor;
GN Name=burs {ECO:0000250|UniProtKB:Q9VD83};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p50T {ECO:0000269|PubMed:15141943};
RX PubMed=15141943; DOI=10.1093/dnares/11.1.27;
RA Mita K., Kasahara M., Sasaki S., Nagayasu Y., Yamada T., Kanamori H.,
RA Namiki N., Kitagawa M., Yamashita H., Yasukochi Y., Kadono-Okuda K.,
RA Yamamoto K., Ajimura M., Ravikumar G., Shimomura M., Nagamura Y.,
RA Shin-I T., Abe H., Shimada T., Morishita S., Sasaki T.;
RT "The genome sequence of silkworm, Bombyx mori.";
RL DNA Res. 11:27-35(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAH89262.2}
RP IDENTIFICATION.
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).
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.
CC {ECO:0000250|UniProtKB:Q9VD83}.
CC -!- SUBUNIT: Heterodimer of burs and pburs. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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DR EMBL; BAAB01143969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BN000691; CAH89262.2; -; mRNA.
DR RefSeq; NP_001091845.1; NM_001098375.1.
DR AlphaFoldDB; Q566B1; -.
DR STRING; 7091.BGIBMGA011022-TA; -.
DR GeneID; 100049169; -.
DR KEGG; bmor:100049169; -.
DR CTD; 42560; -.
DR eggNOG; KOG0029; Eukaryota.
DR eggNOG; KOG1216; Eukaryota.
DR InParanoid; Q566B1; -.
DR OrthoDB; 1517793at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Disulfide bond; Hormone; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..160
FT /note="Bursicon"
FT /id="PRO_0000223887"
FT DOMAIN 38..131
FT /note="CTCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT DISULFID 41..90
FT /evidence="ECO:0000250|UniProtKB:P04275,
FT ECO:0000255|PROSITE-ProRule:PRU00039"
FT DISULFID 55..104
FT /evidence="ECO:0000250|UniProtKB:P04275,
FT ECO:0000255|PROSITE-ProRule:PRU00039"
FT DISULFID 65..125
FT /evidence="ECO:0000250|UniProtKB:P04275,
FT ECO:0000255|PROSITE-ProRule:PRU00039"
FT DISULFID 69..127
FT /evidence="ECO:0000250|UniProtKB:P04275,
FT ECO:0000255|PROSITE-ProRule:PRU00039"
FT DISULFID 87..130
FT /evidence="ECO:0000250|UniProtKB:P04275,
FT ECO:0000255|PROSITE-ProRule:PRU00039"
FT DISULFID 89
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P04275,
FT ECO:0000255|PROSITE-ProRule:PRU00039"
SQ SEQUENCE 160 AA; 17901 MW; B3D33F0E16FD4961 CRC64;
MSVLNTFLVI VALILCYVND FPVTGHEVQL PPGTKFFCQE CQMTAVIHVL KHRGCKPKAI
PSFACIGKCT SYVQVSGSKI WQMERTCNCC QESGEREATV VLFCPDAQNE EKRFRKVSTK
APLQCMCRPC GSIEESSIIP QEVAGYSEEG PLYNHFRKSL