Reviewed, UniProtKB/Swiss-Prot P55847 (MIH_PENJP)

Names and origin

Protein names	Recommended name:     Molt-inhibiting hormone       Short name=MIH Alternative name(s):     PeJ-SGP-IV
Organism	Penaeus japonicus (Kuruma prawn)
Taxonomic identifier	27405 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Arthropoda › Crustacea › Malacostraca › Eumalacostraca › Eucarida › Decapoda › Dendrobranchiata › Penaeoidea › Penaeidae › Marsupenaeus

Protein attributes

Sequence length	105 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Secreted
Domain	Signal
Molecular function	Hormone Neuropeptide
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	neuropeptide signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	neuropeptide hormone activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

28

Ref.2

Peptide

29 – 105

77

Molt-inhibiting hormone

PRO_0000019081

Amino acid modifications

Disulfide bond

35 ↔ 72

By similarity

Disulfide bond

52 ↔ 68

By similarity

Disulfide bond

55 ↔ 81

By similarity

Experimental info

Sequence conflict

44 – 45

2

IY → YN AA sequence Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

105

Helix Strand Turn

Details...

Beta strand

31 – 33

3

Turn

38 – 40

3

Helix

44 – 59

16

Turn

62 – 64

3

Helix

65 – 68

4

Helix

77 – 83

7

Helix

91 – 100

10

Sequences

	Sequence		Length	Mass (Da)
	P55847-1 [UniParc]. Last modified July 15, 1999. Version 2. Checksum: 4467E2FD324D5626	FASTA	105	12,150
	10 20 30 40 50 60 MYRLAMRTWL AIVIVVVGTS LLFDTASASF IDNTCRGVMG NRDIYKKVVR VCEDCTNIFR 70 80 90 100 LPGLDGMCRN RCFYNEWFLI CLKAANREDE IEKFRVWISI LNAGQ

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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AB004652 mRNA. Translation: BAA20432.1.

PIR

T10473.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1J0T	NMR	-	A	28-105	[»]

ModBase

Search...

Family and domain databases

InterPro

IPR001166. Crust_neurhormone.
IPR018251. Crust_neurhormone_CS.
IPR001262. Crust_neurhormone_MIH/MOIH/GIH.
[Graphical view]

Gene3D

G3DSA:1.10.2010.10. CHH_MIH_GIH. 1 hit.

PANTHER

PTHR21188. CHH_MIH_GIH. 1 hit.

Pfam

PF01147. Crust_neurohorm. 1 hit.
[Graphical view]

PRINTS

PR00549. HYPRGLYCEMC2.
PR00550. HYPRGLYCEMIC.

PROSITE

PS01250. CHH_MIH_GIH. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

MIH_PENJP

Accession

Primary (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:	June 16, 2009
This is version 52 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)