P32798 · COT1_YEAST
- ProteinVacuolar zinc transporter COT1
- GeneCOT1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids439 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Vacuolar transporter that regulates zinc homeostasis by mediating zinc transport and storage into the vacuole (PubMed:10856230, PubMed:12556516, PubMed:9712830).
Plays a role in resistance to zinc shock resulting from sudden influx of zinc into cytoplasm (PubMed:12556516).
May also participate in the regulation of cobalt levels under normal physiological conditions and may be important in the supply of metal that is required for metalloenzyme or cofactor synthesis (PubMed:1508175, PubMed:18930916).
Involved in the resistance to cobalt and rhodium ions (PubMed:1508175).
Plays a role in resistance to zinc shock resulting from sudden influx of zinc into cytoplasm (PubMed:12556516).
May also participate in the regulation of cobalt levels under normal physiological conditions and may be important in the supply of metal that is required for metalloenzyme or cofactor synthesis (PubMed:1508175, PubMed:18930916).
Involved in the resistance to cobalt and rhodium ions (PubMed:1508175).
Miscellaneous
Present with 2070 molecules/cell in log phase SD medium.
COT1 has a paralog, ZRC1, that arose from the whole genome duplication.
Catalytic activity
- Zn2+(in) = Zn2+(out)This reaction proceeds in the forward direction.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | fungal-type vacuole | |
Cellular Component | fungal-type vacuole membrane | |
Cellular Component | membrane raft | |
Cellular Component | mitochondrion | |
Molecular Function | cobalt ion transmembrane transporter activity | |
Molecular Function | zinc ion transmembrane transporter activity | |
Biological Process | cobalt ion transport | |
Biological Process | intracellular zinc ion homeostasis | |
Biological Process | zinc ion transmembrane transport | |
Biological Process | zinc ion transport |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameVacuolar zinc transporter COT1
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP32798
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Vacuole membrane ; Multi-pass membrane protein
Note: Targeted to vacuole membrane via the AP-3 pathway.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-9 | Cytoplasmic | ||||
Sequence: MKLGSKQVK | ||||||
Transmembrane | 10-30 | Helical | ||||
Sequence: IISLLLLDTVFFGIEITTGYL | ||||||
Topological domain | 31-33 | Vacuolar | ||||
Sequence: SHS | ||||||
Transmembrane | 34-54 | Helical | ||||
Sequence: LALIADSFHMLNDIISLVVAL | ||||||
Topological domain | 55-76 | Cytoplasmic | ||||
Sequence: WAVNVAKNRNPDSTYTYGWKRA | ||||||
Transmembrane | 77-97 | Helical | ||||
Sequence: EILGALINAVFLIALCVSILI | ||||||
Topological domain | 98-113 | Vacuolar | ||||
Sequence: EALQRIIAPPVIENPK | ||||||
Transmembrane | 114-134 | Helical | ||||
Sequence: FVLYVGVAGLISNTVGLFLFH | ||||||
Topological domain | 135-244 | Cytoplasmic | ||||
Sequence: DNDQEHGHGHGHSHGGIFADHEMHMPSSHTHTHAHVDGIENTTPMDSTDNISEIMPNAIVDSFMNENTRLLTPENASKTPSYSTSSHTIASGGNYTEHNKRKRSLNMHGV | ||||||
Transmembrane | 245-265 | Helical | ||||
Sequence: FLHVLGDALGNIGVMLSAFFI | ||||||
Topological domain | 266-274 | Vacuolar | ||||
Sequence: WKTDYSWKY | ||||||
Transmembrane | 275-295 | Helical | ||||
Sequence: YTDPLVSLIITGIIFSSALPL | ||||||
Topological domain | 296-439 | Cytoplasmic | ||||
Sequence: SCKASKILLQATPSTLSGDQVEGDLLKIPGIIAIHDFHIWNLTESIFIASLHIQLDISPEQFTDLAKIVRSKLHRYGIHSATLQPEFITREVTSTERAGDSQGDHLQNDPLSLRPKTYGTGISGSTCLIDDAANCNTADCLEDH |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Reduces zinc transport into the vacuole and hence limit the over-accumulation of zinc caused by the deletion of ZRT3.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 45 | Increases ability to transport iron and decreases ability to transport cobalt. | ||||
Sequence: N → I |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 15 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000206102 | 1-439 | Vacuolar zinc transporter COT1 | |||
Sequence: MKLGSKQVKIISLLLLDTVFFGIEITTGYLSHSLALIADSFHMLNDIISLVVALWAVNVAKNRNPDSTYTYGWKRAEILGALINAVFLIALCVSILIEALQRIIAPPVIENPKFVLYVGVAGLISNTVGLFLFHDNDQEHGHGHGHSHGGIFADHEMHMPSSHTHTHAHVDGIENTTPMDSTDNISEIMPNAIVDSFMNENTRLLTPENASKTPSYSTSSHTIASGGNYTEHNKRKRSLNMHGVFLHVLGDALGNIGVMLSAFFIWKTDYSWKYYTDPLVSLIITGIIFSSALPLSCKASKILLQATPSTLSGDQVEGDLLKIPGIIAIHDFHIWNLTESIFIASLHIQLDISPEQFTDLAKIVRSKLHRYGIHSATLQPEFITREVTSTERAGDSQGDHLQNDPLSLRPKTYGTGISGSTCLIDDAANCNTADCLEDH | ||||||
Modified residue | 225 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 301 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Expression is increased in response to DNA replication stress.
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P32798 | FTH1 P38310 | 3 | EBI-5006, EBI-20959 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 140-144 | Histidine repeat 1 | ||||
Sequence: HGHGH | ||||||
Motif | 165-169 | Histidine repeat 2 | ||||
Sequence: HTHAH | ||||||
Compositional bias | 207-229 | Polar residues | ||||
Sequence: PENASKTPSYSTSSHTIASGGNY | ||||||
Region | 207-231 | Disordered | ||||
Sequence: PENASKTPSYSTSSHTIASGGNYTE | ||||||
Motif | 219-223 | Histidine repeat 3 | ||||
Sequence: SSHTI | ||||||
Compositional bias | 388-403 | Polar residues | ||||
Sequence: TSTERAGDSQGDHLQN | ||||||
Region | 388-408 | Disordered | ||||
Sequence: TSTERAGDSQGDHLQNDPLSL |
Domain
Contains 3 histidine repeat motifs between the 4th and 5th transmembrane, exposed to the cytoplasm, that may be involved in the binding site of zinc.
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length439
- Mass (Da)48,155
- Last updated1996-10-01 v2
- ChecksumAC88AAA5F2EE4AED
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 207-229 | Polar residues | ||||
Sequence: PENASKTPSYSTSSHTIASGGNY | ||||||
Sequence conflict | 227 | in Ref. 1; AAA74884 | ||||
Sequence: G → E | ||||||
Sequence conflict | 333-334 | in Ref. 1; AAA74884 | ||||
Sequence: HI → RV | ||||||
Compositional bias | 388-403 | Polar residues | ||||
Sequence: TSTERAGDSQGDHLQN | ||||||
Sequence conflict | 424 | in Ref. 1; AAA74884 | ||||
Sequence: I → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M88252 EMBL· GenBank· DDBJ | AAA74884.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X90565 EMBL· GenBank· DDBJ | CAA62171.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z75224 EMBL· GenBank· DDBJ | CAA99636.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006948 EMBL· GenBank· DDBJ | DAA11080.1 EMBL· GenBank· DDBJ | Genomic DNA |