| Hemerythrin-like family | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Identifiers | |||||||||
| Symbol | Hemerythrin | ||||||||
| Pfam | PF01814 | ||||||||
| InterPro | IPR035938 | ||||||||
| PROSITE | PDOC00476 | ||||||||
| CATH | 1HMO | ||||||||
| SCOP2 | 2HMZ / SCOPe / SUPFAM | ||||||||
| |||||||||
Hemerythrin (also spelled haemerythrin; Ancient Greek: αἷμα, romanized: haîma, lit. 'blood', Ancient Greek: ἐρυθρός, romanized: erythrós, lit. 'red') is an oligomeric protein responsible for oxygen (O2) transport in the marine invertebrate phyla of sipunculids, priapulids, brachiopods, and in a single annelid worm genus, Magelona. Myohemerythrin is a monomeric O2-binding protein found in the muscles of marine invertebrates. Hemerythrin and myohemerythrin are essentially colorless when deoxygenated, but turn a violet-pink in the oxygenated state.
Hemerythrin does not, as the name might suggest, contain a heme. The names of the blood oxygen transporters hemoglobin, hemocyanin, and hemerythrin do not refer to the heme group (only found in globins). Instead, these names are derived from the Greek word for blood. Hemerythrin may also contribute to innate immunity and anterior tissue regeneration in certain worms.[1]
- ^ Coates, C.J., Decker, H. (2017). "Immunological properties of oxygen transport proteins: hemoglobin, hemocyanin and hemerythrin". Cell. Mol. Life Sci. 74 (2): 293–317. doi:10.1007/s00018-016-2326-7. PMC 5219038. PMID 27518203.
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