Editing Hemocyanin (section)

== The hemocyanin superfamily ==
The arthropod hemocyanin [[superfamily (proteins)|superfamily]] is composed of [[phenoloxidase]]s, [[hexamerin]]s, [[pseudohemocyanin]]s or [[cryptocyanin]]s, and ([[diptera]]n) hexamerin receptors.<ref>{{cite journal | vauthors = Burmester T | title = Origin and evolution of arthropod hemocyanins and related proteins | journal = Journal of Comparative Physiology B: Biochemical, Systemic, and Environmental Physiology | volume = 172 | issue = 2 | pages = 95–107 | date = February 2002 | pmid = 11916114 | doi = 10.1007/s00360-001-0247-7 | s2cid = 26023927 }}</ref>

Phenoloxidase are copper-containing tyrosinases. These proteins are involved in the process of sclerotization of arthropod cuticle, in wound healing, and humoral immune defense. Phenoloxidase is synthesized by [[Zymogen|zymogens]] and are activated by cleaving an [[N-terminus|N-terminal]] [[peptide]].<ref>{{cite journal | vauthors = Cerenius L, Söderhäll K | title = The prophenoloxidase-activating system in invertebrates | journal = Immunological Reviews | volume = 198 | issue = 1 | pages = 116–126 | date = April 2004 | pmid = 15199959 | doi = 10.1111/j.0105-2896.2004.00116.x | s2cid = 10614298 }}</ref>

Hexamerins are storage proteins commonly found in insects. These proteins are synthesized by the larval [[fat body]] and are associated with molting cycles or nutritional conditions.<ref>{{Cite journal|vauthors=Terwilliger NB|date=1999|title=Hemolymph Proteins and Molting in Crustaceans and Insects|journal=American Zoologist|volume=39|issue=3|pages=589–599|doi=10.1093/icb/39.3.589|doi-access=free}}</ref>

Pseudohemocyanin and cryptocyanins genetic sequences are closely related to hemocyanins in crustaceans. These proteins have a similar structure and function, but lack the [[copper]] binding sites.<ref>{{cite journal | vauthors = Terwilliger NB, Dangott L, Ryan M | title = Cryptocyanin, a crustacean molting protein: evolutionary link with arthropod hemocyanins and insect hexamerins | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 96 | issue = 5 | pages = 2013–2018 | date = March 1999 | pmid = 10051586 | pmc = 26728 | doi = 10.1073/pnas.96.5.2013 | doi-access = free | bibcode = 1999PNAS...96.2013T }}</ref>

The evolutionary changes within the phylogeny of the hemocyanin superfamily are closely related to the emergence of these different proteins in various species. The proteins within this superfamily would not be well understood without the extensive studies of hemocyanin in arthropods.<ref name= Burmester>{{cite journal | vauthors = Burmester T | title = Molecular evolution of the arthropod hemocyanin superfamily | journal = Molecular Biology and Evolution | volume = 18 | issue = 2 | pages = 184–195 | date = February 2001 | pmid = 11158377 | doi = 10.1093/oxfordjournals.molbev.a003792 | doi-access = free }}</ref>