Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
AAT-1, a novel testis-specific AMY-1-binding protein, forms a quaternary complex with AMY-1, A-kinase anchor protein 84, and a regulatory subunit of cAMP-dependent protein kinase and is phosphorylated by its kinase.
Structure and characterization of AAT-1 isoforms.
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Long isoforms are diffusely cytoplasmic and short isoforms mitochondria-like in transfected cells.
"While AAT-1L and AAT-1M were found to be localized diffusely in the cytoplasm, AAT-1S, like AAT-1alpha, was found to be localized in the mitochondria-like structure"
Biallelic variants in MAATS1 encoding CFAP91, a calmodulin-associated and spoke-associated complex protein, cause severe astheno-teratozoospermia and male infertility.
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Biallelic MAATS1 variants cause MMAF with radial spoke and central pair defects.
"TEM and immunostaining experiments in sperm cells showed severe central pair complex (CPC) and radial spokes defects"
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CFAP251 (WDR66) partners with CFAP91 in the CSC.
"we confirmed that the WDR66 protein is a physical and functional partner of CFAP91 into the CSC"
A reference map of the human binary protein interactome.
Proximity labeling of axonemal protein CFAP91 identifies EFCAB5 that regulates sperm motility.
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Cfap91 knockout mice have impaired sperm flagellum formation.
"Cfap91 knockout (KO) mice exhibit impaired sperm flagellum formation and male infertility"
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CFAP91 scaffolds RS3 assembly.
"CFAP91 immunoprecipitates with RS3 proteins CFAP251 and LRRC23, whose localization is disrupted in Cfap91 KO sperm flagella"
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Motile cilia elongate normally without CFAP91.
"ciliary elongation was endurable in Cfap91-/- mice in contrast to disrupted sperm flagellum formation"
Cfap91-Dependent Stability of the RS2 and RS3 Base Proteins and Adjacent Inner Dynein Arms in Tetrahymena Cilia.
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Cfap91 is needed for stable docking of RS3 and the RS2 base, and for motility.
"lack of Tetrahymena Cfap91 protein affects stable docking/positioning of the radial spoke RS3 and the base of RS2, and adjacent inner dynein arms"
Axonemal structures reveal mechanoregulatory and disease mechanisms.
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CFAP91 spans from the RS2 base via the N-DRC to the RS3 base subunits.
"CFAP91, which begins at the base of RS2, interacts with the N-DRC"
A conserved CaM- and radial spoke associated complex mediates regulation of flagellar dynein activity.
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FAP91 binds RSP3 at the spoke base.
"FAP91 directly interacts with radial spoke protein 3 (an AKAP), which is located at the base of the spoke"
The CSC is required for complete radial spoke assembly and wild-type ciliary motility.
The CSC connects three major axonemal complexes involved in dynein regulation.
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The CSC links RS2, the N-DRC and RS3S.
"the CSC connects three major axonemal complexes involved in dynein regulation: RS2, the nexin-dynein regulatory complex (N-DRC), and RS3S"
CCDC113 stabilizes sperm axoneme and head-tail coupling apparatus to ensure male fertility.