[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Eyestalk; DOI=10.1016/0014-5793(94)01055-2; PubMed=7957869 [NCBI, ExPASy, EBI, Israel, Japan] de Kleijn D.P.V., Sleutels F.J.G.T., Martens G.J.M., van Herp F.; "Cloning and expression of mRNA encoding prepro-gonad-inhibiting hormone (GIH) in the lobster Homarus americanus."; FEBS Lett. 353:255-258(1994).
[2]	PROTEIN SEQUENCE OF 32-108, AND MASS SPECTROMETRY. TISSUE=Sinus gland; DOI=10.1016/0143-4179(91)90036-I; PubMed=1791922 [NCBI, ExPASy, EBI, Israel, Japan] Soyez D., Le Caer J.-P., Noel P.Y., Rossier J.; "Primary structure of two isoforms of the vitellogenesis inhibiting hormone from the lobster Homarus americanus."; Neuropeptides 20:25-32(1991).

Comments

FUNCTION: Inhibits vitellogenesis in female animals. Plays a prominent role in the regulation of reproduction/molting processes.
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Produced in the eyestalk X-organ sinus gland complex of male and female lobsters.
MASS SPECTROMETRY: Mass=9135; Method=FAB; Range=32-109; Source=PubMed:1791922;.
SIMILARITY: Belongs to the arthropod CHH/MIH/GIH/VIH hormone family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X87192; CAA60644.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A45586; A45586.
S48747; S48747.

3D structure databases

HSSP

P55847; 1J0T. [HSSP ENTRY / PDB]

ModBase

P55320.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from InterPro).
GO:0005184;	Molecular function: neuropeptide hormone activity (inferred from electronic annotation from InterPro).
GO:0007218;	Biological process: neuropeptide signaling pathway (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001166; Crust_neurhormone.
IPR001262; Crust_neurhormone_MIH/MOIH/GIH.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.2010.10; CHH_MIH_GIH; 1.

Pfam

PF01147; Crust_neurohorm; 1.
Pfam graphical view of domain structure.

PRINTS

PR00549; HYPRGLYCEMC2.
PR00550; HYPRGLYCEMIC.

PROSITE

PS01250; CHH_MIH_GIH; 1.

Other

ProtoNet

P55320.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amidation; Direct protein sequencing; Hormone; Neuropeptide; Secreted; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 31`	`31`
`PEPTIDE`	`32 109`	`78`	`Gonad-inhibiting hormone.`	`PRO_0000019075`
`MOD_RES`	`109 109`		`Alanine amide (Potential).`
`DISULFID`	`41 78`		`By similarity.`
`DISULFID`	`58 74`		`By similarity.`
`DISULFID`	`61 87`		`By similarity.`
`CONFLICT`	`83 83`		`D -> W (in Ref. 2; AA sequence).`

Sequence information

Length: 112 AA [This is the length of the unprocessed precursor]

Molecular weight: 12841 Da [This is the MW of the unprocessed precursor]

CRC64: 8C1955EF737747F6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVTRVGSGFS VQRVWLLLVI VVVLCGSVTQ QASAWFTNDE CPGVMGNRDL YEKVAWVCND 

        70         80         90        100        110 
CANIFRNNDV GVMCKKDCFH TMDFLWCVYA TERHGEIDQF RKWVSILRAG RK

P55320 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools