<unk>  is caused by an X-linked recessive allele, meaning that the gene responsible is only present on the X chromosome. Given that it is recessive, this means that the condition can only be inherited if the alleles for both X-chromosomes have the deficiency if the patient is female (xx) or if patient only has one X chromosome, as with male patients (xY). This means that a female could be heterozygous for the allele (Xx) and not express the weakened immune system, as individuals with partial<unk>  have been shown to function effectively the same as healthy individuals. This also means that any male patient that receives the recessive allele from their mother will inherit the deficiency, regardless of the genotype of their father, as the father must have passed the Y chromosome to them, which plays no part in genes with x-linked inheritance. The gene responsible for the production of<unk> , Complement Factor<unk>  (CFP), lies on the X-chromosome at the coordinates: GRCh38: X:47,623,281-47,630,304. There are 3 types of<unk> , which are caused by different mutations in the exons of the CFP gene. Type I<unk>  can be the result of a nonsense mutation on exon 5 of the CDP gene, caused by a C-to-T transition at position 2767, which results in an early termination of the sequence and the production of an immature<unk>  protein. Type I can also be the result of a G-T transversion at position 3511 in exon 7, causing an amino acid substitution from gly271 to valine, which renders the protein non-functional. Finally, Type I can alternatively be caused by a C-to-G transversion on exon 6 at position 3041, converting a serine codon to a stop codon. Type II<unk>  is thought to be caused by one or both of two mutations on the CFP gene. One of the mutations is a C-to-T transition at position 2124, located on exon 4, which converted an arginine to a tryptophan, resulting in an improper protein fold. The second mutation is a G-to-A transition at position 827 in intron 3, which is hypothesized to cause a cryptic splice site, resulting in improper splicing of the mRNA. Type III<unk>  is caused by a T-to-G mutation on exon 9, resulting in a conversion of tyr387 to aspartic acid, resulting in an ineffective protein. Type I and type II<unk>  result in an absence or extremely low presence of<unk> , whereas type III results in the presence of a dysfunctional<unk>  protein structure. Ultimately, all three types have the same basic effect, reducing defensive capabilities against bacteria, especially those previously mentioned.
Properdin deficiency
Vitamin K deficiency
Factor I deficiency
Familial isolated vitamin E deficiency
Folate deficiency
Hypodysfibrinogenemia
Factor XIII deficiency
Factor X deficiency