ID   PBURS_BOMMO             Reviewed;         137 AA.
AC   Q566B2;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Partner of bursicon;
DE   AltName: Full=Bursicon subunit beta;
DE   Flags: Precursor;
GN   Name=pburs {ECO:0000250|UniProtKB:Q9VJS7};
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:0000312|EMBL:AAX18445.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
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   [2] {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   [3] {ECO:0000305, ECO:0000312|EMBL:CAH89261.1}
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:Q9VJS7}.
CC   -!- SUBUNIT: Heterodimer of burs and pburs. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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DR   EMBL; AY823260; AAX18445.1; -; mRNA.
DR   EMBL; BAAB01029150; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BN000690; CAH89261.1; -; mRNA.
DR   RefSeq; NP_001037289.1; NM_001043824.1.
DR   AlphaFoldDB; Q566B2; -.
DR   SMR; Q566B2; -.
DR   STRING; 7091.BGIBMGA011086-TA; -.
DR   EnsemblMetazoa; BGIBMGA011086-RA; BGIBMGA011086-TA; BGIBMGA011086.
DR   GeneID; 692730; -.
DR   KEGG; bmor:692730; -.
DR   CTD; 34845; -.
DR   eggNOG; ENOG502S111; Eukaryota.
DR   HOGENOM; CLU_145016_0_0_1; -.
DR   InParanoid; Q566B2; -.
DR   OMA; SKECYCC; -.
DR   OrthoDB; 1461272at2759; -.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
DR   GO; GO:0031395; C:bursicon neuropeptide hormone complex; IEA:InterPro.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IEA:InterPro.
DR   GO; GO:0005184; F:neuropeptide hormone activity; IEA:InterPro.
DR   Gene3D; 2.10.90.10; -; 1.
DR   InterPro; IPR034441; Bursicon_suB.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   PANTHER; PTHR41151; PTHR41151; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Hormone; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..137
FT                   /note="Partner of bursicon"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000223890"
FT   DOMAIN          28..123
FT                   /note="CTCK"
FT                   /evidence="ECO:0000255"
FT   DISULFID        28..86
FT                   /evidence="ECO:0000250|UniProtKB:P04275"
FT   DISULFID        52..101
FT                   /evidence="ECO:0000250|UniProtKB:P04275"
FT   DISULFID        61..127
FT                   /evidence="ECO:0000250|UniProtKB:P04275"
FT   DISULFID        65..129
FT                   /evidence="ECO:0000250|UniProtKB:P04275"
FT   DISULFID        83..132
FT                   /evidence="ECO:0000250|UniProtKB:P04275"
FT   DISULFID        85
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:P04275"
SQ   SEQUENCE   137 AA;  15835 MW;  27E01DDFC3B71BF2 CRC64;
     MNIMITKIFF LVQLFYIVVS KSSAEENCET VASEVHVTKE EYDEMGRLLR SCSGEVSVNK
     CEGMCNSQVH PSISSPTGFQ KECFCCREKF LRERLVTLTH CYDPDGIRFE DEENALMEVR
     LREPDECECY KCGDFSR