KLH1
Domain
The protein is composed of 8 globular functional units (a->h), forming a 'pearl chain'. Each unit is separated from the next by a linker. Since the lengths but not the exact positions are known, lengths are indicated here in free text. Linker lengths in amino acids are: 20 (a->b), 13 (b->c), 19 (c->d), 16 (d->e), 14 (e->f), 17 (f->g), and 17 (g->h).
Function
Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.
Post-translational modifications
Probably N-glycosylated (Probable). Asn-1280 and Asn-2484 are buried deeply in the protein which make them inaccessible for sugar attachment (Probable). Asn-3278 N-glycan is likely to represent a diantennate carbohydrate tree (Probable). The didecamer is almost evenly tagged by a total of 120 sugar trees (Probable).
Sequence Similarities
Belongs to the tyrosinase family. Hemocyanin subfamily.
Tissue Specificity
Hemolymph.
Cellular localization
- Secreted
- Extracellular space
Alternative names
Hemocyanin 1, Keyhole limpet hemocyanin A, KLH-A, KLH1