UniProt functional annotation for O76745



	UniProt functional annotation for O76745

UniProt code: O76745.

Organism: Cimex lectularius (Bed bug) (Acanthia lectularia).

Taxonomy: Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera; Cimicomorpha; Cimicidae; Cimex.

Function: Heme-based protein that delivers nitric oxide gas (NO) to the victim while feeding, resulting in vasodilation (Probable). In place of heme, the heme-binding cysteine can also reversibly bind NO when it is present in high concentrations (PubMed:15637157). {ECO:0000269|PubMed:15637157, ECO:0000305}.

Cofactor: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:15637157, ECO:0000305|PubMed:9716517}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. {ECO:0000305|PubMed:15637157};

Subcellular location: Secreted {ECO:0000305|PubMed:16417223, ECO:0000305|PubMed:22305681, ECO:0000305|PubMed:9716517}.

Tissue specificity: Expressed in salivary glands. {ECO:0000269|PubMed:16417223, ECO:0000269|PubMed:9716517}.

Ptm: The N-terminus is blocked. {ECO:0000269|PubMed:9716517}.

Allergen: Causes an allergic reaction in human. Binds to IgE of patients allergic to bed bugs (PubMed:16417223, PubMed:22305681). Binds to IgE in 30% of the 30 adult New York City (NYC) residents tested who had been bitten by the bed bug and had a visible response to it (an itchy raised bump) (PubMed:22305681). {ECO:0000269|PubMed:16417223, ECO:0000269|PubMed:22305681}.

Miscellaneous: Has some sequence similarity to inositol phosphatases, but no inositol trisphosphate phosphatase activity is detected. {ECO:0000269|PubMed:9716517}.

Annotations taken from UniProtKB at the EBI.


Organism:		Cimex lectularius (Bed bug) (Acanthia lectularia).
Taxonomy:		Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera; Cimicomorpha; Cimicidae; Cimex.



Function:		Heme-based protein that delivers nitric oxide gas (NO) to the victim while feeding, resulting in vasodilation (Probable). In place of heme, the heme-binding cysteine can also reversibly bind NO when it is present in high concentrations (PubMed:15637157). {ECO:0000269\|PubMed:15637157, ECO:0000305}.


Cofactor:		Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269\|PubMed:15637157, ECO:0000305\|PubMed:9716517}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. {ECO:0000305\|PubMed:15637157};
Subcellular location:		Secreted {ECO:0000305\|PubMed:16417223, ECO:0000305\|PubMed:22305681, ECO:0000305\|PubMed:9716517}.
Tissue specificity:		Expressed in salivary glands. {ECO:0000269\|PubMed:16417223, ECO:0000269\|PubMed:9716517}.
Ptm:		The N-terminus is blocked. {ECO:0000269\|PubMed:9716517}.
Allergen:		Causes an allergic reaction in human. Binds to IgE of patients allergic to bed bugs (PubMed:16417223, PubMed:22305681). Binds to IgE in 30% of the 30 adult New York City (NYC) residents tested who had been bitten by the bed bug and had a visible response to it (an itchy raised bump) (PubMed:22305681). {ECO:0000269\|PubMed:16417223, ECO:0000269\|PubMed:22305681}.
Miscellaneous:		Has some sequence similarity to inositol phosphatases, but no inositol trisphosphate phosphatase activity is detected. {ECO:0000269\|PubMed:9716517}.