BXA2_BOMMO
ID BXA2_BOMMO Reviewed; 89 AA.
AC P15411;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Bombyxin A-2;
DE Short=BBX-A2;
DE AltName: Full=4K-prothoracicotropic hormone;
DE Short=4K-PTTH;
DE Contains:
DE RecName: Full=Bombyxin A-2 B chain;
DE Contains:
DE RecName: Full=Bombyxin A-2 A chain;
DE Flags: Precursor;
GN Name=BBXA2;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2708384; DOI=10.1016/s0021-9258(18)83288-4;
RA Adachi T., Takiya S., Suzuki Y., Iwami M., Kawakami A., Takahashi S.Y.,
RA Ishizaki H., Nagasawa H., Suzuki A.;
RT "cDNA structure and expression of bombyxin, an insulin-like brain secretory
RT peptide of the silkmoth Bombyx mori.";
RL J. Biol. Chem. 264:7681-7685(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2674935; DOI=10.1073/pnas.86.18.6843;
RA Kawakami A., Iwami M., Nagasawa H., Suzuki A., Ishizaki H.;
RT "Structure and organization of four clustered genes that encode bombyxin,
RT an insulin-related brain secretory peptide of the silkmoth Bombyx mori.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:6843-6847(1989).
RN [3]
RP STRUCTURE BY NMR OF 70-89, AND DISULFIDE BOND.
RX PubMed=7473749; DOI=10.1006/jmbi.1995.0588;
RA Nagata K., Hatanaka H., Kohda D., Kataoka H., Nagasawa H., Isogai A.,
RA Ishizaki H., Suzuki A., Inagaki F.;
RT "Three-dimensional solution structure of bombyxin-II an insulin-like
RT peptide of the silkmoth Bombyx mori: structural comparison with insulin and
RT relaxin.";
RL J. Mol. Biol. 253:749-758(1995).
CC -!- FUNCTION: Brain peptide responsible for activation of prothoracic
CC glands to produce ecdysone in insects.
CC -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC disulfide bonds.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- MISCELLANEOUS: Silk worm has two kinds of PTTH: 4K-PTTH and 22K-PTTH;
CC there are many forms of 4K-PTTH.
CC -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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; J04727; AAA27822.1; -; mRNA.
DR EMBL; M26068; AAA27825.1; -; Genomic_DNA.
DR PIR; A41391; IPMTA2.
DR RefSeq; NP_001103771.1; NM_001110301.1.
DR PDB; 1BOM; NMR; -; A=70-89.
DR PDB; 1BON; NMR; -; A=70-89.
DR PDBsum; 1BOM; -.
DR PDBsum; 1BON; -.
DR AlphaFoldDB; P15411; -.
DR SMR; P15411; -.
DR STRING; 7091.BGIBMGA014494-TA; -.
DR EnsemblMetazoa; BGIBMGA014494-RA; BGIBMGA014494-TA; BGIBMGA014494.
DR GeneID; 693012; -.
DR KEGG; bmor:693012; -.
DR CTD; 693012; -.
DR HOGENOM; CLU_125164_2_0_1; -.
DR InParanoid; P15411; -.
DR OrthoDB; 1644517at2759; -.
DR EvolutionaryTrace; P15411; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0008083; F:growth factor activity; IEA:InterPro.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR InterPro; IPR017097; Bombyxin.
DR InterPro; IPR030680; Bombyxin_A.
DR InterPro; IPR016179; Insulin-like.
DR InterPro; IPR036438; Insulin-like_sf.
DR InterPro; IPR022353; Insulin_CS.
DR InterPro; IPR022352; Insulin_family.
DR Pfam; PF00049; Insulin; 2.
DR PIRSF; PIRSF037038; Bombyxin; 1.
DR PIRSF; PIRSF500312; Bombyxin_A; 1.
DR PRINTS; PR02003; BOMBYXIN.
DR PRINTS; PR00276; INSULINFAMLY.
DR SMART; SM00078; IlGF; 1.
DR SUPFAM; SSF56994; SSF56994; 1.
DR PROSITE; PS00262; INSULIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cleavage on pair of basic residues; Disulfide bond; Hormone;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT PEPTIDE 20..47
FT /note="Bombyxin A-2 B chain"
FT /id="PRO_0000015965"
FT PROPEP 50..68
FT /note="C peptide like"
FT /id="PRO_0000015966"
FT PEPTIDE 70..89
FT /note="Bombyxin A-2 A chain"
FT /id="PRO_0000015967"
FT MOD_RES 20
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT DISULFID 29..76
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000250"
FT DISULFID 41..89
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000250"
FT DISULFID 75..80
FT /evidence="ECO:0000269|PubMed:7473749"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:1BOM"
FT TURN 81..88
FT /evidence="ECO:0007829|PDB:1BOM"
SQ SEQUENCE 89 AA; 9979 MW; F9CB238086BD748A CRC64;
MKILLAIALM LSTVMWVSTQ QPQEVHTYCG RHLARTMADL CWEEGVDKRS DAQFASYGSA
WLMPYSAGRG IVDECCLRPC SVDVLLSYC