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PROSITE documentation PDOC00184 [for PROSITE entry PS00209]

Arthropod hemocyanins / insect LSPs signatures





Description

Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many molluscs and arthropods [1]. Arthropod hemocyanins consist of hexamer or multi-hexamers with subunits of about 75 Kd. Each of these subunits binds two copper ions.

Larval storage proteins (LSP) [2] are proteins from the hemolymph of insects, which may serve as a store of amino acids for synthesis of adult proteins. There are two classes of LSP's: arylphorins, which are rich in aromatic amino acids, and methionine-rich LSP's. LSP's forms hexameric complexes. LSP's are structurally related to arthropod hemocyanins.

In the lepidopteran Trichoplusia ni a protein has been found [3] which is associated with larval metamorphosis. This protein, which is called acidic juvenile hormone-suppressible protein 1 (AJSP-1) is also structurally related to arthropod hemocyanins.

As signature patterns for these proteins we selected two conserved regions, the first of these regions is located in the N-terminal section of these proteins and include a conserved histidine residue which, in hemocyanins, binds a copper atom. The second pattern is located in the central part of the protein.

Note:

See also the pattern for the copper B binding site of tyrosinase <PDOC00398>; this pattern will also pick up all arthropod and mollusc hemocyanins.

Last update:

November 1997 / Patterns and text revised.

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Technical section

PROSITE methods (with tools and information) covered by this documentation:

HEMOCYANIN_1, PS00209; Arthropod hemocyanins / insect LSPs signature 1  (PATTERN)

HEMOCYANIN_2, PS00210; Arthropod hemocyanins / insect LSPs signature 2  (PATTERN)


References

1AuthorsLinzen B.
TitleBlue blood: structure and evolution of hemocyanin.
SourceNaturwissenschaften 76:206-211(1989).
PubMed ID2664531

2AuthorsWillott E. Wang X.-Y. Wells M.A.
TitlecDNA and gene sequence of Manduca sexta arylphorin, an aromatic amino acid-rich larval serum protein. Homology to arthropod hemocyanins.
SourceJ. Biol. Chem. 264:19052-19059(1989).
PubMed ID2808410

3AuthorsJones G. Brown N. Manczak M. Hiremath S. Kafatos F.C.
TitleMolecular cloning, regulation, and complete sequence of a hemocyanin-related, juvenile hormone-suppressible protein from insect hemolymph.
SourceJ. Biol. Chem. 265:8596-8602(1990).
PubMed ID2341396



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