CHH_PENVA
ID CHH_PENVA Reviewed; 80 AA.
AC Q26181;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 76.
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; Fragment;
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Eyestalk;
RA van Wormhoudt A.;
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 7-44, AND MASS SPECTROMETRY.
RX PubMed=8812330; DOI=10.1006/gcen.1996.0092;
RA Sefiani M., Le Caer J.-P., Soyez D.;
RT "Characterization of hyperglycemic and molt-inhibiting activity from sinus
RT glands of the penaeid shrimp Penaeus vannamei.";
RL Gen. Comp. Endocrinol. 103:41-53(1996).
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 -!- MASS SPECTROMETRY: [Crustacean hyperglycemic hormone]: Mass=8627.2;
CC Mass_error=0.3; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8812330};
CC -!- SIMILARITY: Belongs to the arthropod CHH/MIH/GIH/VIH hormone family.
CC {ECO:0000305}.
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DR EMBL; X99731; CAA68067.1; -; mRNA.
DR AlphaFoldDB; Q26181; -.
DR SMR; Q26181; -.
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 Amidation; Carbohydrate metabolism; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Glucose metabolism; Hormone;
KW Neuropeptide; Secreted.
FT PEPTIDE <1..4
FT /note="CHH precursor-related peptide"
FT /id="PRO_0000019071"
FT PEPTIDE 7..78
FT /note="Crustacean hyperglycemic hormone"
FT /id="PRO_0000019072"
FT MOD_RES 78
FT /note="Valine amide"
FT /evidence="ECO:0000255"
FT DISULFID 13..49
FT /evidence="ECO:0000250"
FT DISULFID 29..45
FT /evidence="ECO:0000250"
FT DISULFID 32..58
FT /evidence="ECO:0000250"
FT CONFLICT 26
FT /note="R -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="S -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="E -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 80 AA; 9447 MW; E72C9C2510B1EF91 CRC64;
AGLTKRSLFD PSCTGVFDRQ LLRRLRRVCD DCFNVFREPN VSTECRSNCY NNEVFRQCME
YLLPPHLHEE HRLAVQMVGK
