Q06677 · SWA2_YEAST
- ProteinAuxilin-like clathrin uncoating factor SWA2
- GeneSWA2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids668 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Cofactor for the uncoating of clathrin-coated vesicles (CCVs) by Hsp70-type chaperones (SSA1/2/3 and SSB1/2). Coat disassembly is important for fusion of vesicles with target membranes and for recycling components of clathrin coats to the cytoplasm for further rounds of vesicle formation. Binds to assembled clathrin and recruits the ATP-activated chaperone to CCVs. Stimulates the ATPase activity of the clathrin-associated Hsp70-type chaperone SSA1, which then disrupts clathrin-clathrin interactions, leading to release of the clathrin coat. In addition, prevents unproductive clathrin assembly in the cell. Also required for cortical endoplasmic reticulum inheritance.
Miscellaneous
Present with 768 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 | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | vesicle | |
Molecular Function | clathrin binding | |
Molecular Function | ubiquitin binding | |
Biological Process | clathrin coat disassembly | |
Biological Process | clathrin-dependent endocytosis | |
Biological Process | endoplasmic reticulum inheritance |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAuxilin-like clathrin uncoating factor SWA2
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionQ06677
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Peripheral membrane protein
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 388 | In SWA2-1/SWA2-TPR; partial loss of clathrin disassembly function. In SWA2-TPR-J; complete loss of clathrin disassembly function; when associated with 631-AAA-633. | ||||
Sequence: G → R | ||||||
Mutagenesis | 631-633 | In SWA2-J; abolishes ATPase stimulation activity. In SWA2-TPR-J; complete loss of clathrin disassembly function; when associated with R-388. | ||||
Sequence: HPD → AAA |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 25 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000270621 | 1-668 | Auxilin-like clathrin uncoating factor SWA2 | |||
Sequence: MSDPFAHLLTSLKNKDSASASKETTPQSSNSPSITGSAVADVARTDKSPNDSLHSISAPPLIPSPKVDFSAPPLVPTNSTTKSNTANNTPPSALANTDDDFNQLFGMGTVTTTDTIQKPDEDYYGSKEDHLYNGDDALVDEVKDMEIARLMSLGLSIEEATEFYENDVTYERYLEILKSKQKERNDLAIRKKESGIKMEKSGLSNIVGTDSNNLFSMATDFFNKGKKLVDQWTSFPPEANDRLNNYSKTHDKVEDYDLPQVNDSPNRILFEDNEVVENLPPADNPDQDLLTDFETKIDITKRTAPDVSHSSSPTSGILIEENSRRNEPLIEDSLLDFSEGNLTNSKSNEDSTLFNENSNTDSTIPISDIELSGYNEFKAKGTSLFKNGDYINSLQEYEKSLNTLPLNHPLRIIALSNIIASQLKIGEYSKSIENSSMALELFPSSKAKWKNKISNSDPERSFNDIWPKIMIRRAESFEHLESFKKALETYQELIKKNFFDDKIMQGKRRCQDFINPPPVKKSMPVKKKTTTTSPATKKQNLTASSSNSPISVDSTSEIKKRELENAKLALYDKVFEKISSWKDGKDDDIRHLLANLSSLLTWCNWKDVSMQDLVMPKRVKITYMKAVAKTHPDKIPESLSLENKMIAENIFSTLSIAWDKFKLQNDIN | ||||||
Modified residue | 52 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 64 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 264 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 308 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 312 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with the clathrin light and heavy chains CLC1 and CHC1, respectively. Binds to clathrin with its N-terminal domain containing 3 clathrin-binding (CB) motifs. Association with clathrin is transient. Binds to polyubiquitin and ubiquitinated proteins.
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-95 | Disordered | ||||
Sequence: MSDPFAHLLTSLKNKDSASASKETTPQSSNSPSITGSAVADVARTDKSPNDSLHSISAPPLIPSPKVDFSAPPLVPTNSTTKSNTANNTPPSALA | ||||||
Region | 1-100 | CB1 | ||||
Sequence: MSDPFAHLLTSLKNKDSASASKETTPQSSNSPSITGSAVADVARTDKSPNDSLHSISAPPLIPSPKVDFSAPPLVPTNSTTKSNTANNTPPSALANTDDD | ||||||
Compositional bias | 12-38 | Polar residues | ||||
Sequence: LKNKDSASASKETTPQSSNSPSITGSA | ||||||
Compositional bias | 73-95 | Polar residues | ||||
Sequence: PLVPTNSTTKSNTANNTPPSALA | ||||||
Domain | 140-180 | UBA | ||||
Sequence: DEVKDMEIARLMSLGLSIEEATEFYENDVTYERYLEILKSK | ||||||
Region | 238-302 | CB2 | ||||
Sequence: EANDRLNNYSKTHDKVEDYDLPQVNDSPNRILFEDNEVVENLPPADNPDQDLLTDFETKIDITKR | ||||||
Region | 302-323 | Disordered | ||||
Sequence: RTAPDVSHSSSPTSGILIEENS | ||||||
Region | 303-362 | CB3 | ||||
Sequence: TAPDVSHSSSPTSGILIEENSRRNEPLIEDSLLDFSEGNLTNSKSNEDSTLFNENSNTDS | ||||||
Compositional bias | 304-321 | Polar residues | ||||
Sequence: APDVSHSSSPTSGILIEE | ||||||
Region | 339-359 | Disordered | ||||
Sequence: EGNLTNSKSNEDSTLFNENSN | ||||||
Repeat | 374-407 | TPR 1 | ||||
Sequence: YNEFKAKGTSLFKNGDYINSLQEYEKSLNTLPLN | ||||||
Repeat | 412-445 | TPR 2 | ||||
Sequence: IIALSNIIASQLKIGEYSKSIENSSMALELFPSS | ||||||
Repeat | 467-500 | TPR 3 | ||||
Sequence: PKIMIRRAESFEHLESFKKALETYQELIKKNFFD | ||||||
Region | 511-556 | Disordered | ||||
Sequence: QDFINPPPVKKSMPVKKKTTTTSPATKKQNLTASSSNSPISVDSTS | ||||||
Compositional bias | 525-554 | Polar residues | ||||
Sequence: VKKKTTTTSPATKKQNLTASSSNSPISVDS | ||||||
Domain | 603-668 | J | ||||
Sequence: CNWKDVSMQDLVMPKRVKITYMKAVAKTHPDKIPESLSLENKMIAENIFSTLSIAWDKFKLQNDIN |
Domain
The TPR repeats and the J domain are required for interaction with Hsp70-type chaperones. The J domain is responsible for stimulating the ATPase activity of the chaperone.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length668
- Mass (Da)75,020
- Last updated1996-11-01 v1
- ChecksumCCDF1F78315E3D44
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 12-38 | Polar residues | ||||
Sequence: LKNKDSASASKETTPQSSNSPSITGSA | ||||||
Compositional bias | 73-95 | Polar residues | ||||
Sequence: PLVPTNSTTKSNTANNTPPSALA | ||||||
Compositional bias | 304-321 | Polar residues | ||||
Sequence: APDVSHSSSPTSGILIEE | ||||||
Compositional bias | 525-554 | Polar residues | ||||
Sequence: VKKKTTTTSPATKKQNLTASSSNSPISVDS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U32517 EMBL· GenBank· DDBJ | AAB64756.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006938 EMBL· GenBank· DDBJ | DAA12161.1 EMBL· GenBank· DDBJ | Genomic DNA |