ID   CHHL_BOMMO              Reviewed;         110 AA.
AC   Q9NL55;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=CHH-like protein;
DE   AltName: Full=BmCHHL;
DE   Flags: Precursor;
GN   Name=CHHL;
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].
RC   TISSUE=Brain;
RX   PubMed=10745158; DOI=10.1016/s0965-1748(99)00129-0;
RA   Endo H., Nagasawa H., Watanabe T.;
RT   "Isolation of a cDNA encoding a CHH-family peptide from the silkworm Bombyx
RT   mori.";
RL   Insect Biochem. Mol. Biol. 30:355-361(2000).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- DEVELOPMENTAL STAGE: Expressed in five or six cells (per hemisphere) in
CC       the frontal area of the brain in day 4 fifth instar larvae.
CC   -!- SIMILARITY: Belongs to the arthropod CHH/MIH/GIH/VIH hormone family.
CC       {ECO:0000305}.
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DR   EMBL; AB031074; BAA90831.1; -; mRNA.
DR   RefSeq; NP_001106139.1; NM_001112669.1.
DR   RefSeq; XP_012544169.1; XM_012688715.1.
DR   AlphaFoldDB; Q9NL55; -.
DR   SMR; Q9NL55; -.
DR   STRING; 7091.BGIBMGA004168-TA; -.
DR   EnsemblMetazoa; BGIBMGA004168-RA; BGIBMGA004168-TA; BGIBMGA004168.
DR   GeneID; 100127118; -.
DR   KEGG; bmor:100127118; -.
DR   CTD; 37921; -.
DR   eggNOG; ENOG502S3WA; Eukaryota.
DR   HOGENOM; CLU_147120_1_0_1; -.
DR   InParanoid; Q9NL55; -.
DR   OMA; QHYLKVI; -.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005184; F:neuropeptide hormone activity; IEA:InterPro.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.2010.10; -; 1.
DR   InterPro; IPR018251; Crust_neurhormone_CS.
DR   InterPro; IPR031098; Crust_neurohorm.
DR   InterPro; IPR035957; Crust_neurohorm_sf.
DR   InterPro; IPR001166; Hyperglycemic.
DR   PANTHER; PTHR35981; PTHR35981; 1.
DR   Pfam; PF01147; Crust_neurohorm; 1.
DR   PRINTS; PR00550; HYPRGLYCEMIC.
DR   SUPFAM; SSF81778; SSF81778; 1.
DR   PROSITE; PS01250; CHH_MIH_GIH; 1.
PE   2: Evidence at transcript level;
KW   Amidation; Cleavage on pair of basic residues; Disulfide bond; Hormone;
KW   Neuropeptide; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..35
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000019090"
FT   PEPTIDE         36..107
FT                   /note="CHH-like protein"
FT                   /id="PRO_0000019091"
FT   MOD_RES         107
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000255"
FT   DISULFID        42..78
FT                   /evidence="ECO:0000250"
FT   DISULFID        58..74
FT                   /evidence="ECO:0000250"
FT   DISULFID        61..87
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   110 AA;  12541 MW;  150AD9E49706BA97 CRC64;
     MHLSSVQFAW AALVALAVSA AGALPSSAPH HVERRSFFTL ECKGVFDAAI FARLDRICDD
     CFNLFREPQL YTLCRAECFT TPYFKGCMES LYLYDEKEQI DQMIDFVGKR