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 16-JUN-2009, entry version 48. 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; Arthropoda; Crustacea; Malacostraca; OC Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea; OC Nephropoidea; Nephropidae; Homarus. OX NCBI_TaxID=6706; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Eyestalk; RX MEDLINE=95046270; 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 RT hormone (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 MEDLINE=92168329; 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 RT hormone from the lobster Homarus americanus."; RL Neuropeptides 20:25-32(1991). CC -!- FUNCTION: Inhibits vitellogenesis in female animals. Plays a CC prominent role in the regulation of reproduction/molting CC 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; Range=32-109; CC Source=PubMed:1791922; CC -!- SIMILARITY: Belongs to the arthropod CHH/MIH/GIH/VIH hormone CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X87192; CAA60644.1; -; mRNA. DR PIR; A45586; A45586. DR PIR; S48747; S48747. DR HSSP; P55847; 1J0T. 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 InterPro; IPR001166; Crust_neurhormone. DR InterPro; IPR018251; Crust_neurhormone_CS. DR InterPro; IPR001262; Crust_neurhormone_MIH/MOIH/GIH. DR Gene3D; G3DSA:1.10.2010.10; CHH_MIH_GIH; 1. DR Pfam; PF01147; Crust_neurohorm; 1. DR PRINTS; PR00549; HYPRGLYCEMC2. DR PRINTS; PR00550; HYPRGLYCEMIC. 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 PEPTIDE 32 109 Gonad-inhibiting hormone. FT /FTId=PRO_0000019075. FT MOD_RES 109 109 Alanine amide (Potential). FT DISULFID 41 78 By similarity. FT DISULFID 58 74 By similarity. FT DISULFID 61 87 By similarity. FT CONFLICT 83 83 D -> W (in Ref. 2; AA sequence). SQ SEQUENCE 112 AA; 12841 MW; 8C1955EF737747F6 CRC64; MVTRVGSGFS VQRVWLLLVI VVVLCGSVTQ QASAWFTNDE CPGVMGNRDL YEKVAWVCND CANIFRNNDV GVMCKKDCFH TMDFLWCVYA TERHGEIDQF RKWVSILRAG RK //