ADGB
Domain
The globin domain is circularly permuted. The globin domain, which normally consists of eight consecutive alpha-helices from A (N-terminal) to H (C-terminal), is circularly permutated and split into two parts. The part containing helices A and B is shifted C-terminally and is separated from the main globin sequence (helices C-H) by a potential calmodulin-binding IQ domain.
Function
Probable chimeric globin with a bis-histidyl six-coordinate heme-iron atom through which it could bind dioxygen, carbon monoxide and nitric oxide (PubMed:22115833). Required for sperm flagellum formation and maturation of elongating spermatids, thus playing an essential role in male fertility (PubMed:36995441).
Involvement in disease
Defects in ADGB may be the cause of asthenozoospermia, a condition in which the percentage of progressively motile sperm is abnormally low.
Sequence Similarities
In the central section; belongs to the globin family.
In the N-terminal section; belongs to the peptidase C2 family.
Cellular localization
- Cell projection
- Cilium
- Flagellum
- Expressed within the midpiece and along the whole sperm flagellum. Detected in the annulus of the sperm flagellum in S12 and S15 spermatids and mature sperm.
Alternative names
C6orf103, ADGB, CAPN7L, Androglobin