CHH2_PENJP
ID CHH2_PENJP Reviewed; 120 AA.
AC Q9U5D2; P81681;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Crustacean hyperglycemic hormones 2;
DE AltName: Full=Pej-SGP-II;
DE Contains:
DE RecName: Full=CHH precursor-related peptide 2;
DE Short=CPRP 2;
DE Contains:
DE RecName: Full=Crustacean hyperglycemic hormone 2;
DE Short=CHH 2;
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., Aida K., Nagasawa H.;
RT "Crustacean hyperglycemic hormone of kuruma prawn Penaeus japonicus.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
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).
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 -!- 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; AB035724; BAA88339.1; -; mRNA.
DR AlphaFoldDB; Q9U5D2; -.
DR SMR; Q9U5D2; -.
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; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PEPTIDE 28..44
FT /note="CHH precursor-related peptide 2"
FT /id="PRO_0000019053"
FT PEPTIDE 47..118
FT /note="Crustacean hyperglycemic hormone 2"
FT /id="PRO_0000019054"
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"
SQ SEQUENCE 120 AA; 13467 MW; C2D96499D1231585 CRC64;
MIAFHMVWSA LLASLLLLLL APSASPVDAF SPPEASLTGG QSLSKRSLFD PSCTGVFDRQ
LLRRLGRVCD DCFNVFREPN VAMECRSNCY NNPVFRQCME YLLPAHLHDE YRLAVQMVGK
