ID   MIH_CARMA               Reviewed;         113 AA.
AC   Q27225;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Molt-inhibiting hormone;
DE            Short=MIH;
DE   Flags: Precursor;
GN   Name=MIH;
OS   Carcinus maenas (Common shore crab) (Green crab).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC   Eubrachyura; Portunoidea; Carcinidae; Carcinus.
OX   NCBI_TaxID=6759;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Eyestalk;
RX   PubMed=8224217; DOI=10.1016/0014-5793(93)81699-z;
RA   Klein J.M., Mangerich S., de Kleijn D.P.V., Keller R., Weidemann W.M.;
RT   "Molecular cloning of crustacean putative molt-inhibiting hormone (MIH)
RT   precursor.";
RL   FEBS Lett. 334:139-142(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 36-113.
RC   TISSUE=Sinus gland;
RX   PubMed=1679945; DOI=10.1098/rspb.1991.0078;
RA   Webster S.G.;
RT   "Amino acid sequence of putative moult-inhibiting hormone from the crab
RT   Carcinus maenas.";
RL   Proc. R. Soc. B 244:247-252(1991).
CC   -!- FUNCTION: Inhibits Y-organs where molting hormone (ecdysteroid) is
CC       secreted. A molting cycle is initiated when MIH secretion diminishes or
CC       stops.
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; X75995; CAA53591.1; -; mRNA.
DR   PIR; S39031; S39031.
DR   AlphaFoldDB; Q27225; -.
DR   SMR; Q27225; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005184; F:neuropeptide hormone activity; IEA:InterPro.
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; IPR001262; Hyperglycemic2.
DR   Pfam; PF01147; Crust_neurohorm; 1.
DR   PRINTS; PR00549; HYPRGLYCEMC2.
DR   PRINTS; PR00550; HYPRGLYCEMIC.
DR   SUPFAM; SSF81778; SSF81778; 1.
DR   PROSITE; PS01250; CHH_MIH_GIH; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hormone; Neuropeptide; Secreted;
KW   Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         36..113
FT                   /note="Molt-inhibiting hormone"
FT                   /id="PRO_0000019078"
FT   DISULFID        42..79
FT   DISULFID        59..75
FT                   /evidence="ECO:0000250"
FT   DISULFID        62..88
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   113 AA;  13092 MW;  165895540B0D7623 CRC64;
     MMSRANSRFS CQRTWLLSVV VLAALWSFGV HRAAARVIND ECPNLIGNRD LYKKVEWICE
     DCSNIFRKTG MASLCRRNCF FNEDFVWCVH ATERSEELRD LEEWVGILGA GRD