ID   CHH4_PENMO              Reviewed;         120 AA.
AC   O97386;
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 4;
DE   AltName: Full=Pm-SGP-IV;
DE   Contains:
DE     RecName: Full=CHH precursor-related peptide 4;
DE              Short=CPRP 4;
DE   Contains:
DE     RecName: Full=Crustacean hyperglycemic hormone 4;
DE              Short=CHH 4;
DE   Flags: Precursor;
GN   Name=CHH4;
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}.
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DR   EMBL; AF104389; AAC84145.1; -; mRNA.
DR   AlphaFoldDB; O97386; -.
DR   SMR; O97386; -.
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   2: Evidence at transcript level;
KW   Amidation; Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Disulfide bond; Glucose metabolism; Hormone; Neuropeptide; Secreted;
KW   Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         27..44
FT                   /note="CHH precursor-related peptide 4"
FT                   /id="PRO_0000019067"
FT   PEPTIDE         47..118
FT                   /note="Crustacean hyperglycemic hormone 4"
FT                   /id="PRO_0000019068"
FT   MOD_RES         118
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        53..89
FT                   /evidence="ECO:0000250"
FT   DISULFID        69..85
FT                   /evidence="ECO:0000250"
FT   DISULFID        72..98
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   120 AA;  12987 MW;  D04F39BDF7C4C1B9 CRC64;
     MVALNTLSAV SAALLVLAAS PSPASARSLD ASPSSAFSGN HSLSKRSLFD PACTGIYDRQ
     LLGKLGRLCD DCYNVFREPK VATGCRSNCY YNLIFLDCLE YLIPSHLQEE HMEALQTVGK