ID   GIH_HOMAM               Reviewed;         112 AA.
AC   P55320; Q25013;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 81.
DE   RecName: Full=Gonad-inhibiting hormone;
DE            Short=GIH;
DE   AltName: Full=Vitellogenesis-inhibiting hormone;
DE            Short=VIH;
DE   Flags: Precursor;
OS   Homarus americanus (American lobster).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Communostraca;
OC   Malacostraca; Eumalacostraca; Stomatocarida; Decapoda; Pleocyemata;
OC   Astacidea; Nephropoidea; Nephropidae; Homarus.
OX   NCBI_TaxID=6706;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Eyestalk;
RX   PubMed=7957869; DOI=10.1016/0014-5793(94)01055-2;
RA   de Kleijn D.P.V., Sleutels F.J.G.T., Martens G.J.M., van Herp F.;
RT   "Cloning and expression of mRNA encoding prepro-gonad-inhibiting hormone
RT   (GIH) in the lobster Homarus americanus.";
RL   FEBS Lett. 353:255-258(1994).
RN   [2]
RP   PROTEIN SEQUENCE OF 32-108, AND MASS SPECTROMETRY.
RC   TISSUE=Sinus gland;
RX   PubMed=1791922; DOI=10.1016/0143-4179(91)90036-i;
RA   Soyez D., Le Caer J.-P., Noel P.Y., Rossier J.;
RT   "Primary structure of two isoforms of the vitellogenesis inhibiting hormone
RT   from the lobster Homarus americanus.";
RL   Neuropeptides 20:25-32(1991).
CC   -!- FUNCTION: Inhibits vitellogenesis in female animals. Plays a prominent
CC       role in the regulation of reproduction/molting processes.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Produced in the eyestalk X-organ sinus gland
CC       complex of male and female lobsters.
CC   -!- MASS SPECTROMETRY: Mass=9135; Method=FAB;
CC       Evidence={ECO:0000269|PubMed:1791922};
CC   -!- SIMILARITY: Belongs to the arthropod CHH/MIH/GIH/VIH hormone family.
CC       {ECO:0000305}.
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DR   EMBL; X87192; CAA60644.1; -; mRNA.
DR   PIR; A45586; A45586.
DR   PIR; S48747; S48747.
DR   AlphaFoldDB; P55320; -.
DR   SMR; P55320; -.
DR   EnsemblMetazoa; XM_042378882.1; XP_042234816.1; LOC121874652.
DR   OrthoDB; 6365952at2759; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005184; F:neuropeptide hormone activity; IEA:InterPro.
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   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.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond; Hormone;
KW   Neuropeptide; Secreted; Signal.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000269|PubMed:1791922"
FT   PEPTIDE         32..109
FT                   /note="Gonad-inhibiting hormone"
FT                   /id="PRO_0000019075"
FT   MOD_RES         109
FT                   /note="Alanine amide"
FT                   /evidence="ECO:0000255"
FT   DISULFID        41..78
FT                   /evidence="ECO:0000250"
FT   DISULFID        58..74
FT                   /evidence="ECO:0000250"
FT   DISULFID        61..87
FT                   /evidence="ECO:0000250"
FT   CONFLICT        83
FT                   /note="D -> W (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   112 AA;  12841 MW;  8C1955EF737747F6 CRC64;
     MVTRVGSGFS VQRVWLLLVI VVVLCGSVTQ QASAWFTNDE CPGVMGNRDL YEKVAWVCND
     CANIFRNNDV GVMCKKDCFH TMDFLWCVYA TERHGEIDQF RKWVSILRAG RK
//