MIH_PENJP
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 25-MAY-2022, entry version 88.
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; 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;
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 PDB; 1J0T; NMR; -; A=28-105.
DR PDBsum; 1J0T; -.
DR AlphaFoldDB; P55847; -.
DR SMR; P55847; -.
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: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 PANTHER; PTHR35981; PTHR35981; 1.
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 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..59
FT /evidence="ECO:0007829|PDB:1J0T"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:1J0T"
FT HELIX 65..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