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P55847 (MIH_PENJP) Reviewed, UniProtKB/Swiss-Prot

Last modified March 8, 2011. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Molt-inhibiting hormone

Short name=MIH
Alternative name(s):
PeJ-SGP-IV
OrganismPenaeus japonicus (Kuruma prawn) (Marsupenaeus japonicus)
Taxonomic identifier27405 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaCrustaceaMalacostracaEumalacostracaEucaridaDecapodaDendrobranchiataPenaeoideaPenaeidaeMarsupenaeus

Protein attributes

Sequence length105 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibits Y-organs where molting hormone (ecdysteroid) is secreted. A molting cycle is initiated when MIH secretion diminishes or stops. Has little or no hyperglycemic activity.

Subcellular location

Secreted.

Tissue specificity

Produced by the medulla terminalis X-organ in the eyestalks and transported to the sinus gland where it is stored and released.

Sequence similarities

Belongs to the arthropod CHH/MIH/GIH/VIH hormone family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHormone
Neuropeptide
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processneuropeptide signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionneuropeptide hormone activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Ref.2
Peptide29 – 10577Molt-inhibiting hormone Ref.2
PRO_0000019081

Amino acid modifications

Disulfide bond35 ↔ 72 Ref.3
Disulfide bond52 ↔ 68 Ref.3
Disulfide bond55 ↔ 81 Ref.3

Experimental info

Sequence conflict44 – 452IY → YN AA sequence Ref.2

Secondary structure

.............. 105
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P55847 [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: 4467E2FD324D5626

FASTA10512,150
        10         20         30         40         50         60 
MYRLAMRTWL AIVIVVVGTS LLFDTASASF IDNTCRGVMG NRDIYKKVVR VCEDCTNIFR 

        70         80         90        100 
LPGLDGMCRN RCFYNEWFLI CLKAANREDE IEKFRVWISI LNAGQ 

« Hide

References

[1]"Molecular cloning of a molt-inhibiting hormone cDNA from the kuruma prawn Penaeus japonicus."
Ohira T., Watanabe T., Nagasawa H., Aida K.
Zool. Sci. 14:785-789(1997) [PubMed: 9450390] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Eyestalk.
[2]"Amino acid sequence of a peptide with molt-inhibiting activity from the kuruma prawn Penaeus japonicus."
Yang W.-J., Aida K., Terauchi A., Sonobe H., Nagasawa H.
Peptides 17:197-202(1996) [PubMed: 8801521] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-105.
Tissue: Sinus gland.
[3]"The solution structure of molt-inhibiting hormone from the Kuruma prawn Marsupenaeus japonicus."
Katayama H., Nagata K., Ohira T., Yumoto F., Tanokura M., Nagasawa H.
J. Biol. Chem. 278:9620-9623(2003) [PubMed: 12519766] [Abstract]
Cited for: STRUCTURE BY NMR OF 28-105, DISULFIDE BONDS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB004652 mRNA. Translation: BAA20432.1.
PIRT10473.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1J0TNMR-A28-105[»]
ProteinModelPortalP55847.
SMRP55847. Positions 28-105.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001166. Crust_neurhormone.
IPR018251. Crust_neurhormone_CS.
IPR001262. Crust_neurhormone_MIH/MOIH/GIH.
[Graphical view]
Gene3DG3DSA:1.10.2010.10. CHH_MIH_GIH. 1 hit.
PfamPF01147. Crust_neurohorm. 1 hit.
[Graphical view]
PRINTSPR00549. HYPRGLYCEMC2.
PR00550. HYPRGLYCEMIC.
SUPFAMSSF81778. Crust_neurhormone. 1 hit.
PROSITEPS01250. CHH_MIH_GIH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMIH_PENJP
AccessionPrimary (citable) accession number: P55847
Secondary accession number(s): O02379
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1999
Last modified: March 8, 2011
This is version 58 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families