ID   CHH3_PENMO              Reviewed;         102 AA.
AC   O97385;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Crustacean hyperglycemic hormones 3;
DE   AltName: Full=Pm-SGP-III;
DE   Contains:
DE     RecName: Full=CHH precursor-related peptide 3;
DE              Short=CPRP 3;
DE   Contains:
DE     RecName: Full=Crustacean hyperglycemic hormone 3;
DE              Short=CHH 3;
DE   Flags: Precursor;
GN   Name=CHH3;
OS   Penaeus monodon (Giant tiger prawn).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC   Penaeoidea; Penaeidae; Penaeus.
OX   NCBI_TaxID=6687;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Eyestalk;
RX   PubMed=10804243; DOI=10.1007/s101269900011;
RA   Davey M.L., Hall M.R., Willis R.H., Oliver R.W.A., Thurn M.J., Wilson K.J.;
RT   "Five crustacean hyperglycemic family hormones of Penaeus monodon:
RT   complementary DNA sequence and identification in single sinus glands by
RT   electrospray ionization-Fourier transform mass spectrometry.";
RL   Mar. Biotechnol. 2:80-91(2000).
CC   -!- FUNCTION: Hormone found in the sinus gland of isopods and decapods
CC       which controls the blood sugar level. Has a secretagogue action over
CC       the amylase released from the midgut gland. May act as a stress hormone
CC       and may be involved in the control of molting and reproduction (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the arthropod CHH/MIH/GIH/VIH hormone family.
CC       {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; AF104388; AAC84144.1; -; mRNA.
DR   AlphaFoldDB; O97385; -.
DR   SMR; O97385; -.
DR   PRIDE; O97385; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005184; F:neuropeptide hormone activity; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
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   InterPro; IPR000346; Hyperglycemic1.
DR   PANTHER; PTHR35981; PTHR35981; 1.
DR   Pfam; PF01147; Crust_neurohorm; 1.
DR   PRINTS; PR00548; HYPRGLYCEMC1.
DR   PRINTS; PR00550; HYPRGLYCEMIC.
DR   SUPFAM; SSF81778; SSF81778; 1.
DR   PROSITE; PS01250; CHH_MIH_GIH; 1.
PE   3: Inferred from homology;
KW   Amidation; Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Disulfide bond; Glucose metabolism; Hormone; Neuropeptide; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         23..26
FT                   /note="CHH precursor-related peptide 3"
FT                   /id="PRO_0000019065"
FT   PEPTIDE         29..100
FT                   /note="Crustacean hyperglycemic hormone 3"
FT                   /id="PRO_0000019066"
FT   MOD_RES         100
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        35..71
FT                   /evidence="ECO:0000250"
FT   DISULFID        51..67
FT                   /evidence="ECO:0000250"
FT   DISULFID        54..80
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   102 AA;  11621 MW;  F5FEB21B7AB60112 CRC64;
     MIALRLIAVT LVVAMAASTT WARSFNKRAN FDPSCAGVYN RELLGRLSRL CDDCYNVFRE
     PKVATECRNN CFYNPVFVQC LEYLIPADLH EEYQAHVQTV GK