Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
Molecular cloning of a novel membrane glycoprotein, pal, specifically expressed in photoreceptor cells of the retina and containing leucine-rich repeat.
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Rat Pal/Lrit1 is a type-I transmembrane LRR-Ig-FN3 protein expressed specifically in retina and localized to photoreceptor outer-segment disk membranes.
"Pal immunoreactivity was distributed diffusely on the disk membrane in the lamellar regions."
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The study tested rat Pal topology in HeLa cells using GRP78 as an ER marker.
"To confirm the subcellular localization of Pal, double staining of Pal and GRP78 was performed."
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The study cloned a human homolog but did not establish its retinal localization or physiological function.
"The human homolog of Pal was mapped to chromosome 10q23.2–23.3 using fluorescence in situ hybridization."
Lrit1, a Retinal Transmembrane Protein, Regulates Selective Synapse Formation in Cone Photoreceptor Cells and Visual Acuity.
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Mouse Lrit1 localizes to photoreceptor terminals and supports the selective cone-to-cone-ON-bipolar synaptic connection.
"Here, we found that Lrit1, a
leucine-rich transmembrane protein, localizes to the photoreceptor synaptic
terminal and regulates the synaptic connection between cone photoreceptors and
cone ON-bipolar cells."
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Mouse Lrit1 loss alters cone-pedicle morphology and impairs cone-to-ON-bipolar signal transmission.
"Lrit1-deficient retinas exhibit an aberrant morphology of
cone photoreceptor pedicles, as well as an impairment of signal transmission
from cone photoreceptors to cone ON-bipolar cells."
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Mouse Lrit1 interacts with both the photoreceptor scaffold Frmpd2 and the ON-bipolar glutamate receptor mGluR6.
"Furthermore, we demonstrated
that Lrit1 interacts with Frmpd2, a photoreceptor scaffold protein, and with
mGluR6, an ON-bipolar cell-specific glutamate receptor."
LRIT1 Modulates Adaptive Changes in Synaptic Communication of Cone Photoreceptors.
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Mouse LRIT1 binds mGluR6 in native retina and reciprocal heterologous co-immunoprecipitation assays.
"Together, these findings establish LRIT1 as a binding partner of mGluR6."
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Mouse LRIT1 is concentrated at photoreceptor synapses and is prominent in the cone synaptic cleft.
"Overall, these data indicate that LRIT1 is produced by both rod and cone photoreceptors and ON-bipolar cells and is transported to the synapse where it is prominently present in the cone synaptic cleft."
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Mouse Lrit1 knockout increases cone-synapse sensitivity while impairing background adaptation and temporally demanding photopic vision.
"Knockout
of LRIT1 in mice increases the sensitivity of cone synaptic signaling while
impairing its ability to adapt to background light without overtly influencing
the morphology or molecular composition of photoreceptor synapses."