P23900 · FPS1_YEAST
- ProteinGlycerol uptake/efflux facilitator protein
- GeneFPS1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids669 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Channel protein for glycerol. Has a role in both glycerol influx and efflux. Plays a role in osmoregulation: under osmotic stress the channel is apparently closed to allow accumulation of glycerol in the cell under hyperosmotic conditions.
Miscellaneous
Present with 907 molecules/cell in log phase SD medium.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cell periphery | |
Cellular Component | cytoplasm | |
Cellular Component | fungal-type vacuole | |
Cellular Component | plasma membrane | |
Molecular Function | glycerol channel activity | |
Molecular Function | glycerol transmembrane transporter activity | |
Molecular Function | water channel activity | |
Biological Process | acetate transport | |
Biological Process | arsenite transport | |
Biological Process | conjugation with cellular fusion | |
Biological Process | glycerol metabolic process | |
Biological Process | glycerol transmembrane transport | |
Biological Process | polyol transmembrane transport | |
Biological Process | water transport |
Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGlycerol uptake/efflux facilitator protein
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP23900
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-254 | Extracellular | ||||
Sequence: MSNPQKALNDFLSSESVHTHDSSRKQSNKQSSDEGRSSSQPSHHHSGGTNNNNNNNNNNNNSNNNNNGNDGGNDDDYDYEMQDYRPSPQSARPTPTYVPQYSVESGTAFPIQEVIPSAYINTQDINHKDNGPPSASSNRAFRPRGQTTVSANVLNIEDFYKNADDAHTIPESHLSRRRSRSRATSNAGHSANTGATNGRTTGAQTNMESNESPRNVPIMVKPKTLYQNPQTPTVLPSTYHPINKWSSVKNTYLK | ||||||
Transmembrane | 255-275 | Helical | ||||
Sequence: EFLAEFMGTMVMIIFGSAVVC | ||||||
Topological domain | 276-325 | Cytoplasmic | ||||
Sequence: QVNVAGKIQQDNFNVALDNLNVTGSSAETIDAMKSLTSLVSSVAGGTFDD | ||||||
Transmembrane | 326-346 | Helical | ||||
Sequence: VALGWAAAVVMGYFCAGGSAI | ||||||
Topological domain | 347-369 | Extracellular | ||||
Sequence: SGAHLNPSITLANLVYRGFPLKK | ||||||
Transmembrane | 370-390 | Helical | ||||
Sequence: VPYYFAGQLIGAFTGALILFI | ||||||
Topological domain | 391-446 | Cytoplasmic | ||||
Sequence: WYKRVLQEAYSDWWMNESVAGMFCVFPKPYLSSGRQFFSEFLCGAMLQAGTFALTD | ||||||
Transmembrane | 447-467 | Helical | ||||
Sequence: PYTCLSSDVFPLMMFILIFII | ||||||
Topological domain | 468-506 | Extracellular | ||||
Sequence: NASMAYQTGTAMNLARDLGPRLALYAVGFDHKMLWVHHH | ||||||
Transmembrane | 507-527 | Helical | ||||
Sequence: HFFWVPMVGPFIGALMGGLVY | ||||||
Topological domain | 528-669 | Cytoplasmic | ||||
Sequence: DVCIYQGHESPVNWSLPVYKEMIMRAWFRRPGWKKRNRARRTSDLSDFSYNNDDDEEFGERMALQKTKTKSSISDNENEAGEKKVQFKSVQRGKRTFGGIPTILEEEDSIETASLGATTTDSIGLSDTSSEDSHYGNAKKVT |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000064098 | 1-669 | Glycerol uptake/efflux facilitator protein | |||
Sequence: MSNPQKALNDFLSSESVHTHDSSRKQSNKQSSDEGRSSSQPSHHHSGGTNNNNNNNNNNNNSNNNNNGNDGGNDDDYDYEMQDYRPSPQSARPTPTYVPQYSVESGTAFPIQEVIPSAYINTQDINHKDNGPPSASSNRAFRPRGQTTVSANVLNIEDFYKNADDAHTIPESHLSRRRSRSRATSNAGHSANTGATNGRTTGAQTNMESNESPRNVPIMVKPKTLYQNPQTPTVLPSTYHPINKWSSVKNTYLKEFLAEFMGTMVMIIFGSAVVCQVNVAGKIQQDNFNVALDNLNVTGSSAETIDAMKSLTSLVSSVAGGTFDDVALGWAAAVVMGYFCAGGSAISGAHLNPSITLANLVYRGFPLKKVPYYFAGQLIGAFTGALILFIWYKRVLQEAYSDWWMNESVAGMFCVFPKPYLSSGRQFFSEFLCGAMLQAGTFALTDPYTCLSSDVFPLMMFILIFIINASMAYQTGTAMNLARDLGPRLALYAVGFDHKMLWVHHHHFFWVPMVGPFIGALMGGLVYDVCIYQGHESPVNWSLPVYKEMIMRAWFRRPGWKKRNRARRTSDLSDFSYNNDDDEEFGERMALQKTKTKSSISDNENEAGEKKVQFKSVQRGKRTFGGIPTILEEEDSIETASLGATTTDSIGLSDTSSEDSHYGNAKKVT | ||||||
Modified residue | 150 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 168 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 209 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 212 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-16 | Polar residues | ||||
Sequence: MSNPQKALNDFLSSES | ||||||
Region | 1-99 | Disordered | ||||
Sequence: MSNPQKALNDFLSSESVHTHDSSRKQSNKQSSDEGRSSSQPSHHHSGGTNNNNNNNNNNNNSNNNNNGNDGGNDDDYDYEMQDYRPSPQSARPTPTYVP | ||||||
Compositional bias | 17-31 | Basic and acidic residues | ||||
Sequence: VHTHDSSRKQSNKQS | ||||||
Compositional bias | 32-72 | Polar residues | ||||
Sequence: SDEGRSSSQPSHHHSGGTNNNNNNNNNNNNSNNNNNGNDGG | ||||||
Region | 123-147 | Disordered | ||||
Sequence: QDINHKDNGPPSASSNRAFRPRGQT | ||||||
Region | 167-215 | Disordered | ||||
Sequence: HTIPESHLSRRRSRSRATSNAGHSANTGATNGRTTGAQTNMESNESPRN | ||||||
Compositional bias | 184-213 | Polar residues | ||||
Sequence: TSNAGHSANTGATNGRTTGAQTNMESNESP | ||||||
Motif | 352-354 | NPA 1 | ||||
Sequence: NPS | ||||||
Motif | 480-482 | NPA 2 | ||||
Sequence: NLA | ||||||
Region | 591-615 | Disordered | ||||
Sequence: LQKTKTKSSISDNENEAGEKKVQFK | ||||||
Compositional bias | 599-615 | Basic and acidic residues | ||||
Sequence: SISDNENEAGEKKVQFK | ||||||
Region | 635-669 | Disordered | ||||
Sequence: DSIETASLGATTTDSIGLSDTSSEDSHYGNAKKVT | ||||||
Compositional bias | 639-659 | Polar residues | ||||
Sequence: TASLGATTTDSIGLSDTSSED |
Domain
Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro/Leu-Ala/Ser (NPA).
Sequence similarities
Belongs to the MIP/aquaporin (TC 1.A.8) family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length669
- Mass (Da)73,877
- Last updated1996-10-01 v2
- ChecksumBA9C78056A1251B9
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-16 | Polar residues | ||||
Sequence: MSNPQKALNDFLSSES | ||||||
Compositional bias | 17-31 | Basic and acidic residues | ||||
Sequence: VHTHDSSRKQSNKQS | ||||||
Compositional bias | 32-72 | Polar residues | ||||
Sequence: SDEGRSSSQPSHHHSGGTNNNNNNNNNNNNSNNNNNGNDGG | ||||||
Compositional bias | 184-213 | Polar residues | ||||
Sequence: TSNAGHSANTGATNGRTTGAQTNMESNESP | ||||||
Compositional bias | 599-615 | Basic and acidic residues | ||||
Sequence: SISDNENEAGEKKVQFK | ||||||
Compositional bias | 639-659 | Polar residues | ||||
Sequence: TASLGATTTDSIGLSDTSSED | ||||||
Sequence conflict | 640 | in Ref. 1; CAA38096 | ||||
Sequence: A → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X54157 EMBL· GenBank· DDBJ | CAA38096.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z73148 EMBL· GenBank· DDBJ | CAA97494.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006945 EMBL· GenBank· DDBJ | DAA09279.1 EMBL· GenBank· DDBJ | Genomic DNA |