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C4b is derived from native C4 upon cleavage and release of C4a. 4b is created by cleavage of purified C4 with the classical pathway activated protease C1s enzyme. C4b is essential to the function of 2 of the 3 pathways of complement. Both the classical and lectin pathways of complement activation generate surface-bound active proteases that cleave C4. These enzymes cleave a peptide bond in C4 releasing the anaphylatoxin C4a and activating C4b. C4A and C4B are 2 variants of C4 that are common in man whereas, in animals who have only 1 type usually have C4B.

Abhydrolase Domain Containing 12B, also known as ABHD12B is a part of the serine esterase family. ABHD12B is a protein coding gene.

LIMD2 is a protein-coding gene which holds one LIM zinc-binding domain. LIMD2 is related to illnesses such as intrahepatic cholangiocarcinoma and estrogen-receptor negative breast cancer.

USH1C gene product Harmonin, is a scaffold protein which functions in the assembly of Usher protein complexes. Harmonin is able to attach to various proteins in cell membranes and coordinate their activities. Harmonin contains PDZ domains, a coiled-coil region with a bipartite nuclear localization signal and a PEST degradation sequence. USH1C is expressed in the small intestine, colon, kidney, eye, vestibule of the inner ear and weakly in the pancreas.
Mutations in the USH1C gene cause the Usher syndrome type I which is an autosomal recessive sensory defect involving congenital profound sensorineural deafness, vestibular dysfunction, and blindness due to progressive retinitis pigmentosa. Sensorineural deafness is caused by damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. The 3 types of the Usher syndrome (1- 3) are distinguished by age at onset and differences in auditory and vestibular function. USH1C gene defects cause of non-syndromic sensorineural deafness autosomal recessive type 18 (DFNB18), is a form of sensorineural hearing loss.

C3b is derived from native C3 upon cleavage with the alternative pathway C3 convertase and release of C3a. C3b is essential to the function of all 3complement pathways. Initiation of each pathway generates proteolytic enzyme complexes (C3 convertases) which binds the target surface. These enzymes cleave a peptide bond in C3 releasing the anaphylatoxin C3a and activating C3b. Most of the C3b created during complement activation. Surface-bound C3b is needed in all 3 pathways for effective activation of C5 and formation of C5b-9 complexes which lyse the target cell membrane. Surface-bound C3b and its breakdown products iC3b and C3d are identifyid by various receptors on lymphoid and phagocytic cells which use the C3b ligand to stimulate antigen presentation to cells of the adaptive immune system. It results in an expansion of target-specific B-cell and T-cell populations.

Ankyrin Repeat Family A2, also known as ANKRA2 contains 5 ANK repeats. ANKRA2 assist endocytosis by linking megalin to components of the cytoskeleton or endocytic machinery.

Abhydrolase domain-containing protein 10 (ABHD10) is a member of the AB hydrolase superfamily.

Queuine TRNA-Ribosyltransferase Domain Containing 1, also known as QTRTD1 act together with QTRT1 to form an active queuine tRNA-ribosyltransferase. QTRTD1 exchanges queuine for the guanine at the wobble position of tRNAs along with GUN anticodons (tRNA-Asp,-Asn,-His and -Tyr), in that way forming the hypermodified nucleoside queuosine.