O76745 · NP_CIMLE

Function

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).

Miscellaneous

Has some sequence similarity to inositol phosphatases, but no inositol trisphosphate phosphatase activity is detected.

Cofactor

heme b (UniProtKB | Rhea| CHEBI:60344 )

Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.

Features

Showing features for binding site.

130220406080100120140160180200220240260280300
TypeIDPosition(s)Description
Binding site80Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); proximal binding residue

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular space
Molecular Functionheme binding
Molecular Functioniron ion binding
Molecular Functionphosphatidylinositol-4,5-bisphosphate 5-phosphatase activity
Biological Processnitric oxide transport
Biological Processphosphatidylinositol dephosphorylation
Biological Processvasodilation in another organism

Keywords

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Nitrophorin Cim l NP
  • Short names
    NP
  • Alternative names
    • Salivary nitrophorin
    • cNP
  • Allergen name
    Cim l NP

Organism names

Accessions

  • Primary accession
    O76745

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Allergenic properties

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).

Keywords

Protein family/group databases

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-20
ChainPRO_500415979021-302Nitrophorin Cim l NP

Post-translational modification

The N-terminus is blocked.

Expression

Tissue specificity

Expressed in salivary glands.

Family & Domains

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    302
  • Mass (Da)
    33,624
  • Last updated
    1998-11-01 v1
  • Checksum
    B83471EAE2E39290
MKLLLSAGAALAFVLGLCAAGSPPAQLSVHTVSWNSGHERAPTNLEELLGLNSGETPDVIAVAVQGFGFQTDKPQQGPACVKNFQSLLTSKGYTKLKNTITETMGLTVYCLEKHLDQNTLKNETIIVTVDDQKKSGGIVTSFTIYNKRFSFTTSRMSDEDVTSTNTKYAYDTRLDYSKKDDPSDFLFWIGDLNVRVETNATHAKSLVDQNNIDGLMAFDQLKKAKEQKLFDGWTEPQVTFKPTYKFKPNTDEYDLSATPSWTDRALYKSGTGKTIQPLSYNSLTNYKQTEHRPVLAKFRVTL

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict139in Ref. 1; AA sequence

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF079803
EMBL· GenBank· DDBJ
AAC28738.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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