ID   CHH_MACLE               Reviewed;         135 AA.
AC   O77220;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Crustacean hyperglycemic hormones;
DE   Contains:
DE     RecName: Full=CHH precursor-related peptide;
DE              Short=CPRP;
DE   Contains:
DE     RecName: Full=Crustacean hyperglycemic hormone;
DE              Short=CHH;
DE   Flags: Precursor;
GN   Name=CHH;
OS   Macrobrachium lanchesteri (Freshwater prawn) (Palaemon lanchesteri).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Caridea;
OC   Palaemonoidea; Palaemonidae; Macrobrachium.
OX   NCBI_TaxID=82204;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Ju B., Khoo H.-W.;
RT   "Characterization of crustacean hyperglycemic hormone (CHH) mRNA
RT   transcripts and genomic sequences in Macrobrachium lanchesteri (de Man).";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
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   -!- TISSUE SPECIFICITY: Produced by the medulla terminalis X-organ in the
CC       eyestalks and transported to the sinus gland where they are stored and
CC       released.
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; AF088854; AAC36310.1; -; Genomic_DNA.
DR   AlphaFoldDB; O77220; -.
DR   SMR; O77220; -.
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..58
FT                   /note="CHH precursor-related peptide"
FT                   /id="PRO_0000019043"
FT   PEPTIDE         62..133
FT                   /note="Crustacean hyperglycemic hormone"
FT                   /id="PRO_0000019044"
FT   MOD_RES         133
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        68..104
FT                   /evidence="ECO:0000250"
FT   DISULFID        84..100
FT                   /evidence="ECO:0000250"
FT   DISULFID        87..113
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   135 AA;  15198 MW;  72BE61304FFA03DB CRC64;
     MIRSSVMGPT MFLVVLLLIA SHQTSAWSLD GLARIEKLLS TSSSASAASP TRGQALNLKK
     RAILDQSCKG IFDRELFKKL DRVCDDCYNL YRKPYVAIDC REGCYQNLVF RQCIQDLQLM
     DQLDEYANAV QIVGK