Sac1p is a type II transmembrane protein that localizes to the Golgi and the ER. This subcompartmentalization of the phosphatase determines which processes it regulates (16, 3, 13). Golgi-localized Sac1p is involved in Golgi trafficking and cell wall maintenance, while ER-localized Sac1p participates in ATP uptake into the ER, ER-based secretion and protein processing, and vacuolar function (4, 16, 13 and references therein). Localization of Sac1p is regulated by growth conditions as well as interactions with proteins such as Dpm1p (17). Expression of SAC1 is regulated in response to changing levels of PtdIns[4]P (18). SAC1 was originally identified as a suppressor of the temperature-conditional act1-1 allele, and thus some of the phenotypes seen in the sac1 mutant are similar to those of actin mutants, such as defects in actin cytoskeleton polarization and abnormal chitin deposition (6). sac1 null phenotypes also include cold sensitivity, inositol auxotrophy, fragmented vacuoles, accumulation of lipid droplets, elevated levels of PtdIns[4]P, calcofluor white sensitivity, and constitutively-activated unfolded protein response (6, and reviewed in 10). Sac1p is the founding member of a family of PtdIns phosphatases that share a catalytic domain known as the Sac1-like domain. In S. cerevisiae, this family includes the phosphatases Fig4p, Inp51p, Inp52p, and Inp53p, all of partially overlapping function. All of the Sac1-like domain containing proteins are highly conserved from yeast to human; mammalian members of this protein family include synaptojanin-1 (SYNJ1) and synaptojanin -2 (SYNJ2) (reviewed in 10). The phosphorylated products of phosphatidylinositol (PtdIns, PI), collectively referred to as phosphoinositides or phosphatidylinositol phosphates (PtdInsPs, PIPs), are membrane-bound lipids that function as structural components of membranes, as well as regulators of many cellular processes in eukaryotes, including vesicle-mediated membrane trafficking, cell wall integrity, and actin cytoskeleton organization (reviewed in 10 and 11). PtdInsPs are also precursors of the water-soluble inositol phosphates (IPs), an important class of intracellular signaling molecules (reviewed in 12, 14 and 15). The inositol ring of the membrane phospholipids and the water-soluble IPs are readily phosphorylated and dephosphorylated at a number of positions making them well suited as key regulators. PtdIns can be phosphorylated at one or a combination of positions (3', 4', or 5') on the inositol headgroup, generating a set of unique stereoisomers that have specific biological functions (reviewed in 10). These stereoisomers have been shown to be restricted to certain membranes (reviewed in 10). Phosphatidylinositol 4-phosphate (PtdIns4P) is the major PtdInsP species of the Golgi apparatus, where it plays a role in the vesicular trafficking of secretory proteins from the Golgi to the plasma membrane (reviewed in 10). Phosphatidylinositol 4,5-bisphosphate (PtdIns[4,5]P2) is the major species found at the plasma membrane and is involved in the regulation of actin cytoskeleton organization, as well as cell wall integrity, and heat shock response pathways (reviewed in 10). Phosphatidylinositol 3-phosphate (PtdIns3P) is found predominantly at endosomal membranes and in multivesicular bodies (MVB), where it plays a role in endosomal and vacuolar membrane trafficking. Phosphatidylinositol 3,5-bisphosphate (PtdIns[3,5]P2) is found on vacuolar membranes where it plays an important role in the MVB sorting pathway (reviewed in 10). Phosphorylation and dephosphorylation of the inositol headgroups of PtdInsPs at specific membrane locations signals the recruitment of certain proteins essential for vesicular transport (11, and reviewed in 10). PtdInsPs recruit proteins that contain PtdInsP-specific binding domains, such as the well-studied pleckstrin homology (PH) domain that recognizes the phosphorylation pattern of specific PtdInsP inositol headgroups (reviewed in 10). A number of kinases and phosphatases are involved in the generation and interconversions of PtdInsPs, the majority of which have been well conserved during evolution (reviewed in 10). The PtdInsP kinases, in contrast to the lipid phosphatases, have a higher degree of specificity. While each kinase appears to phosphorylate only one substrate, many of the lipid phosphatases can dephosphorylate a number of substrates.", "date_edited": "2008-06-26"}, "literature_overview": {"primary_count": 87, "additional_count": 80, "review_count": 51, "go_count": 15, "phenotype_count": 35, "disease_count": 0, "interaction_count": 131, "regulation_count": 2, "ptm_count": 5, "funComplement_count": 1, "htp_count": 79, "total_count": 374}, "disease_overview": {"manual_disease_terms": [], "htp_disease_terms": [], "computational_annotation_count": 0, "date_last_reviewed": null}, "ecnumbers": [{"display_name": "3.1.3.64", "link": "/ecnumber/EC:3.1.3.64"}], "URS_ID": null, "main_strain": "S288C", "genetic_position": -153.8, "regulation_overview": {"regulator_count": 6, "target_count": 0}, "reference_mapping": {"552023": 1, "600779": 2, "645278": 3, "564119": 4, "629925": 5, "648891": 6, "478135": 7, "394014": 8, "2218025": 9, "503360": 10, "575124": 11, "502465": 12, "586006": 13, "493843": 14, "501717": 15, "502727": 16, "534667": 17, "492141": 18, "617384": 19}, "history": [{"category": "Name", "history_type": "LSP", "note": "Name: RSD1", "date_created": "2010-02-16", "references": [{"id": 617384, "display_name": "Cleves AE, et al. (1989)", "citation": "Cleves AE, et al. (1989) Mutations in the SAC1 gene suppress defects in yeast Golgi and yeast actin function. J Cell Biol 109(6 Pt 1):2939-50", "pubmed_id": 2687291, "link": "/reference/S000050014", "year": 1989, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1083/jcb.109.6.2939"}, {"display_name": "PMC full text", "link": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2115899/"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/2687291"}]}]}, {"category": "Name", "history_type": "LSP", "note": "Name: SAC1", "date_created": "2000-05-19", "references": [{"id": 552023, "display_name": "Mortimer RK, et al. (1989)", "citation": "Mortimer RK, et al. (1989) Genetic map of Saccharomyces cerevisiae, edition 10. Yeast 5(5):321-403", "pubmed_id": 2678811, "link": "/reference/S000073208", "year": 1989, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1002/yea.320050503"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/2678811"}]}]}], "complexes": [{"format_name": "CPX-3158", "display_name": "SPOTS complex"}]},
tabs: {"id": 1268650, "protein_tab": true, "interaction_tab": true, "summary_tab": true, "go_tab": true, "sequence_section": true, "expression_tab": true, "phenotype_tab": true, "literature_tab": true, "wiki_tab": false, "regulation_tab": true, "sequence_tab": true, "history_tab": true, "homology_tab": true, "disease_tab": false}
};
The S. cerevisiae Reference Genome sequence is derived from laboratory strain
S288C. Download DNA or protein sequence, view genomic context and
coordinates. Click "Sequence Details" to view all sequence information for this locus, including that
for other strains.
BLASTN |
BLASTP |
Design Primers |
Restriction Fragment Map |
Restriction Fragment Sizes |
Six-Frame Translation
BLASTN vs. fungi |
BLASTP at NCBI |
BLASTP vs. fungi
Basic sequence-derived (length, molecular weight, isoelectric point) and experimentally-determined (median abundance, median absolute deviation) protein information. Click "Protein Details" for further information about the protein such as half-life, abundance, domains, domains shared with other proteins, protein sequence retrieval for various strains, physico-chemical properties, protein modification sites, and external identifiers for the protein.
Curated mutant alleles for the specified gene, listed alphabetically. Click on the allele name to open the allele page. Click "SGD search" to view all alleles in search results.
View all SAC1 alleles in SGD search
GO Annotations consist of four mandatory components: a gene product, a term from one of the three
Gene Ontology (GO) controlled vocabularies
(Molecular Function,
Biological Process, and
Cellular Component), a reference, and an
evidence code. SGD has manually curated and high-throughput GO Annotations, both derived from the
literature, as well as computational, or predicted, annotations. Click "Gene Ontology Details" to view
all GO information and evidence for this locus as well as biological processes it shares with other genes.
View computational annotations
Macromolecular complex annotations are imported from the Complex Portal. These annotations have been derived from physical molecular interaction evidence extracted from the literature and cross-referenced in the entry, or by curator inference from information on homologs in closely related species or by inference from scientific background.
Phenotype annotations for a gene are curated single mutant phenotypes that require an observable
(e.g., "cell shape"), a qualifier (e.g., "abnormal"), a mutant type (e.g., null), strain background,
and a reference. In addition, annotations are classified as classical genetics or high-throughput
(e.g., large scale survey, systematic mutation set). Whenever possible, allele information and
additional details are provided. Click "Phenotype Details" to view all phenotype annotations and
evidence for this locus as well as phenotypes it shares with other genes.
Interaction annotations are curated by BioGRID and include physical
or genetic interactions observed
between at least two genes. An interaction annotation is composed of the interaction type, name of the
interactor, assay type (e.g., Two-Hybrid), annotation type (e.g., manual or high-throughput), and a
reference, as well as other experimental details. Click "Interaction Details" to view all interaction
annotations and evidence for this locus, including an interaction visualization.
1666 total interactions for 1098 unique genes
The number of putative Regulators (genes that regulate it) and Targets (genes it regulates) for the
given locus, based on experimental evidence. This evidence includes data generated through
high-throughput techniques. Click "Regulation Details" to view all regulation annotations, shared GO
enrichment among regulation Targets, and a regulator/target diagram for the locus.
Expression data are derived from records contained in the
Gene Expression Omnibus (GEO), and are first log2
transformed and normalized. Referenced datasets may contain one or more condition(s), and as a result
there may be a greater number of conditions than datasets represented in a single clickable histogram
bar. The histogram division at 0.0 separates the down-regulated (green) conditions and datasets from
those that are up-regulated (red). Click "Expression Details" to view all expression annotations and
details for this locus, including a visualization of genes that share a similar expression pattern.
A summary of the locus, written by SGD Biocurators following a thorough review of the literature. Links
to gene names and curated GO terms are included within the Summary Paragraphs.
Last Updated: 2008-06-26
All manually curated literature for the specified gene, organized into topics according to their
relevance to the gene (Primary Literature, Additional Literature, or Review). Click "Literature Details"
to view all literature information for this locus, including shared literature between genes.
SAC1 / YKL212W Overview
Sequence
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Protein
Alleles
Gene Ontology
Molecular Function
Biological Process
Cellular Component
Complex
Pathways
Phenotype
Classical Genetics
Large-scale Survey
Interaction
Physical Interactions
Genetic Interactions
Regulation
Expression
Summary Paragraph
Literature
Resources