ID   MIH_FAXLI               Reviewed;         106 AA.
AC   P83636;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Molt-inhibiting hormone;
DE            Short=MIH;
DE   Flags: Precursor;
OS   Faxonius limosus (Spinycheek crayfish) (Orconectes limosus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC   Astacoidea; Cambaridae; Faxonius.
OX   NCBI_TaxID=28379;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 30-104, FUNCTION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, AND AMIDATION
RP   AT ALA-104.
RC   TISSUE=Sinus gland {ECO:0000269|PubMed:16269348};
RX   PubMed=16269348; DOI=10.1016/j.peptides.2005.03.005;
RA   Bulau P., Okuno A., Thome E., Schmitz T., Peter-Katalinic J., Keller R.;
RT   "Characterization of a molt-inhibiting hormone (MIH) of the crayfish,
RT   Orconectes limosus, by cDNA cloning and mass spectrometric analysis.";
RL   Peptides 26:2129-2136(2005).
CC   -!- FUNCTION: Inhibits Y-organs where molting hormone (ecdysteroid) is
CC       secreted. A molting cycle is initiated when MIH secretion diminishes or
CC       stops. {ECO:0000269|PubMed:16269348}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16269348}.
CC   -!- TISSUE SPECIFICITY: Sinus gland of the eyestalk.
CC       {ECO:0000269|PubMed:16269348}.
CC   -!- MASS SPECTROMETRY: Mass=8664.29; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:16269348};
CC   -!- SIMILARITY: Belongs to the arthropod CHH/MIH/GIH/VIH hormone family.
CC       {ECO:0000255}.
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DR   AlphaFoldDB; P83636; -.
DR   SMR; P83636; -.
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   Amidation; Direct protein sequencing; Disulfide bond; Hormone;
KW   Neuropeptide; Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000269|PubMed:16269348"
FT   CHAIN           30..104
FT                   /note="Molt-inhibiting hormone"
FT                   /evidence="ECO:0000269|PubMed:16269348"
FT                   /id="PRO_0000209864"
FT   PROPEP          105..106
FT                   /evidence="ECO:0000269|PubMed:16269348"
FT                   /id="PRO_0000232593"
FT   MOD_RES         104
FT                   /note="Alanine amide"
FT                   /evidence="ECO:0000269|PubMed:16269348"
FT   DISULFID        36..73
FT                   /evidence="ECO:0000250|UniProtKB:P83627"
FT   DISULFID        53..69
FT                   /evidence="ECO:0000250|UniProtKB:P83627"
FT   DISULFID        56..82
FT                   /evidence="ECO:0000250|UniProtKB:P83627"
SQ   SEQUENCE   106 AA;  12135 MW;  F6254BCBEE15ED97 CRC64;
     MVNQVAQCFT VRRVWLVVVV GLLVHQTTAR YVFEECPGVM GNRALHGKVT RVCEDCYNVF
     RDTDVLAGCR KGCFSSEMFK LCLLAMERVE EFPDFKRWIG ILNAGR