ID   MIH_PENJP               Reviewed;         105 AA.
AC   P55847; O02379;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   02-SEP-2026, entry version 96.
DE   RecName: Full=Molt-inhibiting hormone;
DE            Short=MIH;
DE   AltName: Full=PeJ-SGP-IV;
DE   Flags: Precursor;
OS   Penaeus japonicus (Kuruma prawn) (Marsupenaeus japonicus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Communostraca;
OC   Malacostraca; Eumalacostraca; Stomatocarida; Decapoda; Dendrobranchiata;
OC   Penaeoidea; Penaeidae; Penaeus.
OX   NCBI_TaxID=27405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Eyestalk;
RX   PubMed=9450390; DOI=10.2108/zsj.14.785;
RA   Ohira T., Watanabe T., Nagasawa H., Aida K.;
RT   "Molecular cloning of a molt-inhibiting hormone cDNA from the kuruma prawn
RT   Penaeus japonicus.";
RL   Zool. Sci. 14:785-789(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 29-105.
RC   TISSUE=Sinus gland;
RX   PubMed=8801521; DOI=10.1016/0196-9781(95)02122-1;
RA   Yang W.-J., Aida K., Terauchi A., Sonobe H., Nagasawa H.;
RT   "Amino acid sequence of a peptide with molt-inhibiting activity from the
RT   kuruma prawn Penaeus japonicus.";
RL   Peptides 17:197-202(1996).
RN   [3]
RP   STRUCTURE BY NMR OF 28-105, AND DISULFIDE BONDS.
RX   PubMed=12519766; DOI=10.1074/jbc.m212962200;
RA   Katayama H., Nagata K., Ohira T., Yumoto F., Tanokura M., Nagasawa H.;
RT   "The solution structure of molt-inhibiting hormone from the Kuruma prawn
RT   Marsupenaeus japonicus.";
RL   J. Biol. Chem. 278:9620-9623(2003).
CC   -!- FUNCTION: Inhibits Y-organs where molting hormone (ecdysteroid) is
CC       secreted. A molting cycle is initiated when MIH secretion diminishes or
CC       stops. Has little or no hyperglycemic activity.
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 it is 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; AB004652; BAA20432.1; -; mRNA.
DR   PIR; T10473; T10473.
DR   RefSeq; XP_042887187.1; XM_043031253.1.
DR   PDB; 1J0T; NMR; -; A=28-105.
DR   AlphaFoldDB; P55847; -.
DR   MDposit; P55847; -.
DR   SMR; P55847; -.
DR   EnsemblMetazoa; XM_043031253.1; XP_042887187.1; LOC122262976.
DR   GeneID; 122262976; -.
DR   KEGG; pja:122262976; -.
DR   OrthoDB; 6331348at2759; -.
DR   EvolutionaryTrace; P55847; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005184; F:neuropeptide hormone activity; IEA:InterPro.
DR   GO; GO:0007623; P:circadian rhythm; IEA:TreeGrafter.
DR   Gene3D; 1.10.2010.10; Crustacean CHH/MIH/GIH neurohormone; 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   PANTHER; PTHR35981; ION TRANSPORT PEPTIDE, ISOFORM C; 1.
DR   PANTHER; PTHR35981:SF2; ION TRANSPORT PEPTIDE, ISOFORM C; 1.
DR   Pfam; PF01147; Crust_neurohorm; 1.
DR   PRINTS; PR00549; HYPRGLYCEMC2.
DR   PRINTS; PR00550; HYPRGLYCEMIC.
DR   SUPFAM; SSF81778; Crustacean CHH/MIH/GIH neurohormone; 1.
DR   PROSITE; PS01250; CHH_MIH_GIH; 1.
DR   PDBsum; 1J0T; -.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Hormone;
KW   Neuropeptide; Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000269|PubMed:8801521"
FT   PEPTIDE         29..105
FT                   /note="Molt-inhibiting hormone"
FT                   /id="PRO_0000019081"
FT   DISULFID        35..72
FT                   /evidence="ECO:0000269|PubMed:12519766"
FT   DISULFID        52..68
FT                   /evidence="ECO:0000269|PubMed:12519766"
FT   DISULFID        55..81
FT                   /evidence="ECO:0000269|PubMed:12519766"
FT   CONFLICT        44..45
FT                   /note="IY -> YN (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          31..33
FT                   /evidence="ECO:0007829|PDB:1J0T"
FT   TURN            38..40
FT                   /evidence="ECO:0007829|PDB:1J0T"
FT   HELIX           44..55
FT                   /evidence="ECO:0007829|PDB:1J0T"
FT   HELIX           56..60
FT                   /evidence="ECO:0007829|PDB:1J0T"
FT   HELIX           62..68
FT                   /evidence="ECO:0007829|PDB:1J0T"
FT   HELIX           77..83
FT                   /evidence="ECO:0007829|PDB:1J0T"
FT   HELIX           91..100
FT                   /evidence="ECO:0007829|PDB:1J0T"
SQ   SEQUENCE   105 AA;  12150 MW;  4467E2FD324D5626 CRC64;
     MYRLAMRTWL AIVIVVVGTS LLFDTASASF IDNTCRGVMG NRDIYKKVVR VCEDCTNIFR
     LPGLDGMCRN RCFYNEWFLI CLKAANREDE IEKFRVWISI LNAGQ
//