CAN1 arginine permease CAN1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: CAN1
Official Full Name: arginine permease CAN1
Primary source: SGD:S000000789
Locus tag: YEL063C
See related: AllianceGenome:SGD:S000000789; FungiDB:YEL063C; VEuPathDB:YEL063C
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Enables L-arginine transmembrane transporter activity. Involved in L-arginine transmembrane transport. Located in eisosome and plasma membrane. Human ortholog(s) of this gene implicated in retinitis pigmentosa 68. Orthologous to several human genes including SLC7A1 (solute carrier family 7 member 1); SLC7A14 (solute carrier family 7 member 14); and SLC7A2 (solute carrier family 7 member 2). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See CAN1 in Genome Data Viewer

Location:: chromosome: V

Exon count:: 1

Sequence:: Chromosome: V; NC_001137.3 (31694..33466, complement)

Chromosome V - NC_001137.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001137.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

The arginine transporter Can1 acts as a transceptor for regulation of proline utilization in the yeast Saccharomyces cerevisiae.
Title: The arginine transporter Can1 acts as a transceptor for regulation of proline utilization in the yeast Saccharomyces cerevisiae.
Arginine inhibits Saccharomyces cerevisiae biofilm formation by inducing endocytosis of the arginine transporter Can1.
Title: Arginine inhibits Saccharomyces cerevisiae biofilm formation by inducing endocytosis of the arginine transporter Can1.
Authors report that transport-elicited ubiquitylation of the arginine transporter Can1 is promoted by transition to an inward-facing state. This conformational change unveils a region of the N-terminal cytosolic tail targeted by the Art1 alpha-arrestin, which is activated via the TORC1 kinase complex upon arginine uptake.
Title: Transition of yeast Can1 transporter to the inward-facing state unveils an α-arrestin target sequence promoting its ubiquitylation and endocytosis.
The results presented here suggest some possible synergistic effects of phosphorylated Alp1, Gap1 and Can1 amino acid permeases on regulation of amino acid utilization and metabolism in Saccharomyces cerevisiae.
Title: Effects of three permeases on arginine utilization in Saccharomyces cerevisiae.
study show that Gap1 and Can1 permeases undergo ubiquitin-dependent endocytosis in response to their substrates and that this endocytosis is due to transport catalysis rather than intracellular substrate accumulation.
Title: Substrate-induced ubiquitylation and endocytosis of yeast amino acid permeases.
The ultrastructure of one type of domain, the membrane compartment of Can1 (MCC), was investigated.
Title: Furrow-like invaginations of the yeast plasma membrane correspond to membrane compartment of Can1.
analysis of long-term stability of the subdomains of Can1p: Fur4p (another H+ symporter) and Sur7p (a protein of unknown function) occupy the Can1p subdomain
Title: Distribution of Can1p into stable domains reflects lateral protein segregation within the plasma membrane of living S. cerevisiae cells.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables L-arginine transmembrane transporter activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables amino acid transmembrane transporter activity	IBA Inferred from Biological aspect of Ancestor more info
enables basic amino acid transmembrane transporter activity	IDA Inferred from Direct Assay more info	PubMed
enables transmembrane transporter activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in L-arginine transmembrane transport	IGI Inferred from Genetic Interaction more info	PubMed
involved_in amino acid transmembrane transport	IBA Inferred from Biological aspect of Ancestor more info
involved_in amino acid transport	IEA Inferred from Electronic Annotation more info
involved_in basic amino acid transport	IDA Inferred from Direct Assay more info	PubMed
involved_in transmembrane transport	IDA Inferred from Direct Assay more info	PubMed
involved_in transmembrane transport	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in eisosome	IDA Inferred from Direct Assay more info	PubMed
located_in endoplasmic reticulum	HDA more info	PubMed
located_in endosome	IEA Inferred from Electronic Annotation more info
located_in endosome membrane	IEA Inferred from Electronic Annotation more info
is_active_in membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in membrane	IEA Inferred from Electronic Annotation more info
located_in mitochondrion	HDA more info	PubMed
located_in plasma membrane	IDA Inferred from Direct Assay more info	PubMed
located_in plasma membrane	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: arginine permease CAN1

NP_010851.1

Plasma membrane arginine permease; transceptor that senses extracellular basic amino acids; negative regulator of biofilm formation; requires phosphatidyl ethanolamine (PE) for localization, exclusively associated with lipid rafts; mutation confers canavanine resistance; CAN1 has a paralog, ALP1, that arose from the whole genome duplication