Family with sequence similarity 186 member B.

Outer dense fiber protein 2; Seems to be a major component of sperm tail outer dense fibers (ODF). ODFs are filamentous structures located on the outside of the axoneme in the midpiece and principal piece of the mammalian sperm tail and may help to maintain the passive elastic structures and elastic recoil of the sperm tail. May have a modulating influence on sperm motility. Functions as a general scaffold protein that is specifically localized at the distal/subdistal appendages of mother centrioles. Component of the centrosome matrix required for the localization of PLK1 and NIN to th [...]

Fascin homolog 3, actin-bundling protein, testicular (Strongylocentrotus purpuratus).

Isoaspartyl peptidase/L-asparaginase alpha chain; Has both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp- L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, [...]

Phosphatidylethanolamine binding protein 4.

Ropporin-1; Important for male fertility. With ROPN1L, involved in fibrous sheath integrity and sperm motility, plays a role in PKA- dependent signaling processes required for spermatozoa capacitation. Belongs to the ropporin family.

F-actin-capping protein subunit alpha; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.

Ubiquilin like.

F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. The isoform beta-3 may play a role in spermatogenesis. Alternatively, may play a role in later maturation steps such as capacitation and fertilization which involve changes of membrane domains. May play a role in the regulation of cell morphology and cytoskeletal organization.