P32798 · COT1_YEAST

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).

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

GO annotations

AspectTerm
Cellular Componentfungal-type vacuole
Cellular Componentfungal-type vacuole membrane
Cellular Componentmembrane raft
Cellular Componentmitochondrion
Molecular Functioncobalt ion transmembrane transporter activity
Molecular Functionzinc ion transmembrane transporter activity
Biological Processcobalt ion transport
Biological Processintracellular zinc ion homeostasis
Biological Processzinc ion transmembrane transport
Biological Processzinc ion transport

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Vacuolar zinc transporter COT1
  • Alternative names
    • Cobalt toxicity protein 1

Gene names

    • Name
      COT1
    • ORF names
      O6131
    • Ordered locus names
      YOR316C

Organism names

Accessions

  • Primary accession
    P32798
  • Secondary accessions
    • D6W314

Proteomes

Organism-specific databases

Subcellular Location

Vacuole membrane
; Multi-pass membrane protein
Note: Targeted to vacuole membrane via the AP-3 pathway.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-9Cytoplasmic
Transmembrane10-30Helical
Topological domain31-33Vacuolar
Transmembrane34-54Helical
Topological domain55-76Cytoplasmic
Transmembrane77-97Helical
Topological domain98-113Vacuolar
Transmembrane114-134Helical
Topological domain135-244Cytoplasmic
Transmembrane245-265Helical
Topological domain266-274Vacuolar
Transmembrane275-295Helical
Topological domain296-439Cytoplasmic

Keywords

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.

TypeIDPosition(s)Description
Mutagenesis45Increases ability to transport iron and decreases ability to transport cobalt.

Variants

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The viewer provides 15 variants from UniProt as well as other sources including ClinVar and dbSNP.

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PTM/Processing

Features

Showing features for chain, modified residue, cross-link.

TypeIDPosition(s)Description
ChainPRO_00002061021-439Vacuolar zinc transporter COT1
Modified residue225Phosphoserine
Cross-link301Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Keywords

Proteomic databases

PTM databases

Expression

Induction

Expression is increased in response to DNA replication stress.

Interaction

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P32798FTH1 P383103EBI-5006, EBI-20959

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for motif, compositional bias, region.

TypeIDPosition(s)Description
Motif140-144Histidine repeat 1
Motif165-169Histidine repeat 2
Compositional bias207-229Polar residues
Region207-231Disordered
Motif219-223Histidine repeat 3
Compositional bias388-403Polar residues
Region388-408Disordered

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    439
  • Mass (Da)
    48,155
  • Last updated
    1996-10-01 v2
  • Checksum
    AC88AAA5F2EE4AED
MKLGSKQVKIISLLLLDTVFFGIEITTGYLSHSLALIADSFHMLNDIISLVVALWAVNVAKNRNPDSTYTYGWKRAEILGALINAVFLIALCVSILIEALQRIIAPPVIENPKFVLYVGVAGLISNTVGLFLFHDNDQEHGHGHGHSHGGIFADHEMHMPSSHTHTHAHVDGIENTTPMDSTDNISEIMPNAIVDSFMNENTRLLTPENASKTPSYSTSSHTIASGGNYTEHNKRKRSLNMHGVFLHVLGDALGNIGVMLSAFFIWKTDYSWKYYTDPLVSLIITGIIFSSALPLSCKASKILLQATPSTLSGDQVEGDLLKIPGIIAIHDFHIWNLTESIFIASLHIQLDISPEQFTDLAKIVRSKLHRYGIHSATLQPEFITREVTSTERAGDSQGDHLQNDPLSLRPKTYGTGISGSTCLIDDAANCNTADCLEDH

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias207-229Polar residues
Sequence conflict227in Ref. 1; AAA74884
Sequence conflict333-334in Ref. 1; AAA74884
Compositional bias388-403Polar residues
Sequence conflict424in Ref. 1; AAA74884

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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