SAG S-antigen visual arrestin [Bos taurus (domestic cattle)] - Gene

Summary

Official Symbol: SAGprovided by VGNC
Official Full Name: S-antigen visual arrestinprovided by VGNC
Primary source: VGNC:VGNC:34263
See related: BGD:BT16557; Ensembl:ENSBTAG00000021480
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Bos taurus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos
Also known as: S-AG
Orthologs: human mouse all
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Location:: chromosome: 3

Exon count:: 17

Annotation release	Status	Assembly	Chr	Location
RS_2023_09	current	ARS-UCD2.0 (GCF_002263795.3)	3	NC_037330.1 (113012794..113054216)

Chromosome 3 - NC_037330.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:: NC_037330.1 Chromosome 3 Reference ARS-UCD2.0 Primary Assembly

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Data suggest functionality for mutant R171 in stabilizing the inactive arrestin-1 conformation as well as the rhodopsin-arrestin-1 complex.
Title: Arrestin-1 engineering facilitates complex stabilization with native rhodopsin.
Data indicate molecular dynamics simulations and site-directed fluorescence experiments on arrestin-1 interactions with rhodopsin, showing that loops within the C-edge of arrestin function as a membrane anchor.
Title: C-edge loops of arrestin function as a membrane anchor.
Conformational changes are involved in the arrestin-rhodopsin binding interface through multiple docking modes.
Title: Rhodopsin TM6 can interact with two separate and distinct sites on arrestin: evidence for structural plasticity and multiple docking modes in arrestin-rhodopsin binding.
K2A mutations in arrestin-1, -2, and -3 significantly reduced their binding to active phosphorhodopsin.
Title: Role of receptor-attached phosphates in binding of visual and non-visual arrestins to G protein-coupled receptors.
maintenance of low levels of the active monomer is the biological role of arrestin-1 self-association
Title: Robust self-association is a common feature of mammalian visual arrestin-1.
We hypothesize that, although arrestin requires at least a single Rho*P to bind the membrane, a single arrestin can actually interact with a pair of receptors
Title: Arrestin-rhodopsin binding stoichiometry in isolated rod outer segment membranes depends on the percentage of activated receptors.
variant form of arrestin-1 binds rod outer segment membranes
Title: A variant of arrestin-1 binds rod outer segment membranes in a light-independent manner.
Alpha-helix I plays an indirect role in receptor binding, likely keeping beta-strand I, which carries several phosphate-binding residues, in a position favorable for its interaction with receptor-attached phosphates.
Title: The role of arrestin alpha-helix I in receptor binding.
Models suggest that the phosphorylated carboxy-terminal region of rhodopsin, Rh(330-348), undergoes significant conformational changes and becomes structured upon binding to arrestin.
Title: The arrestin-bound conformation and dynamics of the phosphorylated carboxy-terminal region of rhodopsin.
arrestin and p44 bind differently to different phosphorylated rhodopsin species and that this may be due to a structural difference between p44's and arrestin's basal states.
Title: Differential phosphorylation of the rhodopsin cytoplasmic tail mediates the binding of arrestin and its splice variant, p44.

Submit: New GeneRIF Correction

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Gene Ontology Provided by RefSeq

Function	Evidence Code	Pubs
enables G protein-coupled receptor binding	IEA Inferred from Electronic Annotation more info	PubMed

Process	Evidence Code	Pubs
involved_in G protein-coupled receptor internalization	IEA Inferred from Electronic Annotation more info	PubMed
involved_in signal transduction	IEA Inferred from Electronic Annotation more info	PubMed

Component	Evidence Code	Pubs
located_in photoreceptor inner segment	IEA Inferred from Electronic Annotation more info	PubMed
located_in photoreceptor outer segment	IEA Inferred from Electronic Annotation more info	PubMed

General protein information

Go to the top of the page Help

Preferred Names: S-arrestin

Names: 48 kDa protein; S-antigen; retina and pineal gland (arrestin); arrestin1; retinal S-antigen; rod photoreceptor arrestin

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_181000.2 → NP_851343.1 S-arrestin

See identical proteins and their annotated locations for NP_851343.1

Status: PROVISIONAL

Source sequence(s)

U08346

UniProtKB/TrEMBL

A0A452DJ49

Related

ENSBTAP00000055008.3, ENSBTAT00000065854.3

Conserved Domains (2) summary

smart01017
Location:199 → 360

Arrestin_C; Arrestin (or S-antigen), C-terminal domain

pfam00339
Location:22 → 180

Arrestin_N; Arrestin (or S-antigen), N-terminal domain