ID   PTTH_BOMMO              Reviewed;         224 AA.
AC   P17219;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Prothoracicotropic hormone;
DE            Short=PTTH;
DE   Contains:
DE     RecName: Full=P2K;
DE   Contains:
DE     RecName: Full=P6K;
DE   Contains:
DE     RecName: Full=Prothoracicotropic hormone;
DE   Flags: Precursor;
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=2315701; DOI=10.1126/science.2315701;
RA   Kawakami A., Kataoka H., Oka T., Mizoguchi A., Kimura-Kawakami M.,
RA   Adachi T., Iwami M., Nagasawa H., Suzuki A., Ishizaki H.;
RT   "Molecular cloning of the Bombyx mori prothoracicotropic hormone.";
RL   Science 247:1333-1335(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Kinshu X Showa; TISSUE=Posterior silk gland;
RX   PubMed=8125124; DOI=10.1111/j.1432-1033.1994.tb18665.x;
RA   Adachi-Yamada T., Iwami M., Kataoka H., Suzuki A., Ishizaki H.;
RT   "Structure and expression of the gene for the prothoracicotropic hormone of
RT   the silkmoth Bombyx mori.";
RL   Eur. J. Biochem. 220:633-643(1994).
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE, AND GLYCOSYLATION AT ASN-156.
RX   PubMed=1368675; DOI=10.1271/bbb1961.55.73;
RA   Kataoka H., Nagasawa H., Isogai A., Ishizaki H., Suzuki A.;
RT   "Prothoracicotropic hormone of the silkworm, Bombyx mori: amino acid
RT   sequence and dimeric structure.";
RL   Agric. Biol. Chem. 55:73-86(1991).
RN   [4]
RP   DISULFIDE BONDS.
RX   PubMed=8180220; DOI=10.1021/bi00185a031;
RA   Ishibashi J., Kataoka H., Isogai A., Kawakami A., Saegusa H., Yagi Y.,
RA   Mizoguchi A., Ishizaki H., Suzuki A.;
RT   "Assignment of disulfide bond location in prothoracicotropic hormone of the
RT   silkworm, Bombyx mori: a homodimeric peptide.";
RL   Biochemistry 33:5912-5919(1994).
CC   -!- FUNCTION: PTTH is a brain secretory polypeptide of insects which
CC       stimulates the prothoracic glands to produce and release ecdysone, the
CC       steroid essential to insect development.
CC   -!- FUNCTION: Peptides P2K and P6K are presumed to be cleaved post-
CC       translationally and may play some unknown physiologically or
CC       developmentally important functions.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:8180220}.
CC   -!- TISSUE SPECIFICITY: PTTH is synthesized by two dorsolateral
CC       neurosecretory cells of the Bombyx brain.
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DR   EMBL; D90082; BAA14119.1; -; mRNA.
DR   EMBL; D90083; BAA14120.1; -; mRNA.
DR   EMBL; X75942; CAA53543.1; -; Genomic_DNA.
DR   PIR; S40125; A40099.
DR   RefSeq; NP_001037349.1; NM_001043884.1.
DR   PDB; 5AOQ; X-ray; 2.70 A; L/M=119-224.
DR   PDBsum; 5AOQ; -.
DR   AlphaFoldDB; P17219; -.
DR   SMR; P17219; -.
DR   STRING; 7091.BGIBMGA000357-TA; -.
DR   iPTMnet; P17219; -.
DR   PRIDE; P17219; -.
DR   GeneID; 692767; -.
DR   KEGG; bmor:692767; -.
DR   CTD; 33238; -.
DR   eggNOG; ENOG502TDG8; Eukaryota.
DR   HOGENOM; CLU_1397733_0_0_1; -.
DR   OrthoDB; 1391421at2759; -.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 2.10.90.10; -; 1.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   SUPFAM; SSF57501; SSF57501; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hormone;
KW   Neuropeptide; Reference proteome; Signal.
FT   SIGNAL          1..29
FT   PEPTIDE         33..53
FT                   /note="P2K"
FT                   /id="PRO_0000022188"
FT   PEPTIDE         56..112
FT                   /note="P6K"
FT                   /id="PRO_0000022189"
FT   CHAIN           116..224
FT                   /note="Prothoracicotropic hormone"
FT                   /id="PRO_0000022190"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:1368675"
FT   DISULFID        130
FT                   /note="Interchain"
FT                   /evidence="ECO:0000269|PubMed:8180220"
FT   DISULFID        132..169
FT                   /evidence="ECO:0000269|PubMed:8180220"
FT   DISULFID        155..211
FT                   /evidence="ECO:0000269|PubMed:8180220"
FT   DISULFID        163..213
FT                   /evidence="ECO:0000269|PubMed:8180220"
FT   STRAND          135..139
FT                   /evidence="ECO:0007829|PDB:5AOQ"
FT   STRAND          145..147
FT                   /evidence="ECO:0007829|PDB:5AOQ"
FT   STRAND          149..154
FT                   /evidence="ECO:0007829|PDB:5AOQ"
FT   STRAND          170..181
FT                   /evidence="ECO:0007829|PDB:5AOQ"
FT   STRAND          194..196
FT                   /evidence="ECO:0007829|PDB:5AOQ"
FT   STRAND          198..212
FT                   /evidence="ECO:0007829|PDB:5AOQ"
SQ   SEQUENCE   224 AA;  26028 MW;  636FBF7CA456F0DF CRC64;
     MITRPIILVI LCYAILMIVQ SFVPKAVALK RKPDVGGFMV EDQRTHKSHN YMMKRARNDV
     LGDKENVRPN PYYTEPFDPD TSPEELSALI VDYANMIRND VILLDNSVET RTRKRGNIQV
     ENQAIPDPPC TCKYKKEIED LGENSVPRFI ETRNCNKTQQ PTCRPPYICK ESLYSITILK
     RRETKSQESL EIPNELKYRW VAESHPVSVA CLCTRDYQLR YNNN