ID   CHH1_PENJP              Reviewed;         120 AA.
AC   O15980;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Crustacean hyperglycemic hormones 1;
DE   AltName: Full=Pej-SGP-I;
DE   Contains:
DE     RecName: Full=CHH precursor-related peptide 1;
DE              Short=CPRP 1;
DE   Contains:
DE     RecName: Full=Crustacean hyperglycemic hormone 1;
DE              Short=CHH 1;
DE   Flags: Precursor;
OS   Penaeus japonicus (Kuruma prawn) (Marsupenaeus japonicus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC   Penaeoidea; Penaeidae; Penaeus.
OX   NCBI_TaxID=27405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Eyestalk;
RA   Ohira T., Watanabe T., Nagasawa H., Aida K.;
RT   "Molecular cloning of cDNAs encoding four crustacean hyperglycemic hormones
RT   and a molt-inhibiting hormone from the kuruma prawn Penaeus japonicus.";
RL   (In) Proceedings of the XIII international congress of comparative
RL   endocrinology, pp.83-86, Yokohama (1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 47-118, AND AMIDATION AT VAL-118.
RC   TISSUE=Sinus gland;
RX   PubMed=9210164; DOI=10.1016/s0196-9781(96)00332-4;
RA   Yang W.-J., Aida K., Nagasawa H.;
RT   "Amino acid sequences and activities of multiple hyperglycemic hormones
RT   from the kuruma prawn, Penaeus japonicus.";
RL   Peptides 18:479-485(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 47-101.
RC   TISSUE=Sinus gland;
RA   Yang W.-J., Aida K., Nagasawa H.;
RT   "Amino acid sequences of a hyperglycaemic hormone and its related peptides
RT   from the kuruma prawn, Penaeus japonicus.";
RL   Aquaculture 135:205-212(1995).
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.
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}.
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DR   EMBL; AB007507; BAA22560.1; -; mRNA.
DR   PDB; 5B5I; X-ray; 1.60 A; A/B=47-119.
DR   PDBsum; 5B5I; -.
DR   AlphaFoldDB; O15980; -.
DR   SMR; O15980; -.
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   1: Evidence at protein level;
KW   3D-structure; Amidation; Carbohydrate metabolism;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Glucose metabolism; Hormone; Neuropeptide; Secreted;
KW   Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         25..44
FT                   /note="CHH precursor-related peptide 1"
FT                   /id="PRO_0000019051"
FT   PEPTIDE         47..118
FT                   /note="Crustacean hyperglycemic hormone 1"
FT                   /id="PRO_0000019052"
FT   MOD_RES         118
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000269|PubMed:9210164"
FT   DISULFID        53..89
FT                   /evidence="ECO:0000250"
FT   DISULFID        69..85
FT                   /evidence="ECO:0000250"
FT   DISULFID        72..98
FT                   /evidence="ECO:0000250"
FT   HELIX           59..72
FT                   /evidence="ECO:0007829|PDB:5B5I"
FT   TURN            75..77
FT                   /evidence="ECO:0007829|PDB:5B5I"
FT   HELIX           79..86
FT                   /evidence="ECO:0007829|PDB:5B5I"
FT   HELIX           88..90
FT                   /evidence="ECO:0007829|PDB:5B5I"
FT   HELIX           93..107
FT                   /evidence="ECO:0007829|PDB:5B5I"
SQ   SEQUENCE   120 AA;  13298 MW;  CEC6BE04483897ED CRC64;
     MIAFRAVWSA LLASLLLLLL APSASPVDAF SPPEASLTGG QSLSKRSLFD PSCTGVFDRQ
     LLRRLGRVCD DCFNVFREPN VATECRSNCY NNPVFRQCMA YVVPAHLHNE HREAVQMVGK