P25618 · CWH43_YEAST
- ProteinProtein CWH43
- GeneCWH43
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids953 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the maintenance of cell wall integrity. Required for the replacement of the diacylglycerol moiety by ceramides during GPI-anchor maturation.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 802 | |||||
Sequence: H |
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 | cellular bud neck | |
Cellular Component | cellular bud tip | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | plasma membrane | |
Biological Process | cell wall organization | |
Biological Process | fungal-type cell wall organization | |
Biological Process | GPI anchor biosynthetic process | |
Biological Process | GPI anchor metabolic process |
Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameProtein CWH43
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP25618
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Note: Concentrates to the bud tip of small budded cells and to the neck of dividing cells.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-7 | Cytoplasmic | ||||
Sequence: MLIINGK | ||||||
Topological domain | 29-64 | Extracellular | ||||
Sequence: YSLHFHKIVTNAHYTYPDEWFPSVSATIGDRYPERS | ||||||
Transmembrane | 65-85 | Helical | ||||
Sequence: IFQILIALTAFPRFLLLLGHY | ||||||
Topological domain | 86-91 | Cytoplasmic | ||||
Sequence: YLNQSK | ||||||
Transmembrane | 92-112 | Helical | ||||
Sequence: VCFLVGVLRTVSCGGWVYITS | ||||||
Topological domain | 113-117 | Extracellular | ||||
Sequence: TDDHD | ||||||
Transmembrane | 118-138 | Helical | ||||
Sequence: IHDIFMITYIVLTLPWDIMIT | ||||||
Topological domain | 139-149 | Cytoplasmic | ||||
Sequence: RYSSPLTSKNK | ||||||
Transmembrane | 150-170 | Helical | ||||
Sequence: GLTATIFFGTLFPMIYWYIQH | ||||||
Topological domain | 171-175 | Extracellular | ||||
Sequence: SVQQR | ||||||
Transmembrane | 176-196 | Helical | ||||
Sequence: AGAYSIYAYFEWSLILLDIAF | ||||||
Topological domain | 197-278 | Cytoplasmic | ||||
Sequence: DAFAYADFKKIDIVLAFNEKPGNTSFFQIRDSSPINYGEEKSSELQKSGEKKVEKEKPVARSATGSYFRFDSFFYLLTNIFN | ||||||
Transmembrane | 279-299 | Helical | ||||
Sequence: GFLFWSNVTSLLCSIWHFPLW | ||||||
Topological domain | 300-307 | Extracellular | ||||
Sequence: YMGISGYE | ||||||
Transmembrane | 308-328 | Helical | ||||
Sequence: AAILGYLGPIFLYLPFVSEAF | ||||||
Topological domain | 329-330 | Cytoplasmic | ||||
Sequence: TQ | ||||||
Transmembrane | 331-351 | Helical | ||||
Sequence: YGVLLGGIIAIGAYIVQMPEL | ||||||
Topological domain | 352 | Extracellular | ||||
Sequence: R | ||||||
Transmembrane | 353-368 | Helical | ||||
Sequence: LISVAVGTSITVATFV | ||||||
Topological domain | 369-380 | Cytoplasmic | ||||
Sequence: QNLRYITNAETS | ||||||
Transmembrane | 381-401 | Helical | ||||
Sequence: FSFALTWLLGLVASVILKMGF | ||||||
Topological domain | 402-420 | Extracellular | ||||
Sequence: YTNNPTWVILDERNGGYNK | ||||||
Transmembrane | 421-441 | Helical | ||||
Sequence: TALVLTVLFGMLSPYVNSINF | ||||||
Topological domain | 442-450 | Cytoplasmic | ||||
Sequence: EGKRNAQAK | ||||||
Transmembrane | 451-471 | Helical | ||||
Sequence: SASLIGKLFLAVGFGSLLFGI | ||||||
Topological domain | 472-495 | Extracellular | ||||
Sequence: HQLLTDSSTTIYWAWEGYNESHGP | ||||||
Transmembrane | 496-516 | Helical | ||||
Sequence: LPWPWGALTCTVMLFASLSSV | ||||||
Topological domain | 517 | Cytoplasmic | ||||
Sequence: K | ||||||
Transmembrane | 518-538 | Helical | ||||
Sequence: FMGKPLVPCLLLLISTAVLSA | ||||||
Topological domain | 539-547 | Extracellular | ||||
Sequence: RSITQWPKY | ||||||
Transmembrane | 548-568 | Helical | ||||
Sequence: IFGGLLYAIAMLWLVPSYFSA | ||||||
Topological domain | 569-585 | Cytoplasmic | ||||
Sequence: LGQVQNIWVYVLSFSVY | ||||||
Transmembrane | 586-606 | Helical | ||||
Sequence: IIFVLAHVWVVAYAFVPMGWV | ||||||
Topological domain | 607-613 | Extracellular | ||||
Sequence: LREKIET | ||||||
Transmembrane | 614-634 | Helical | ||||
Sequence: VLAFSSTFIIIGALTCKNLNI | ||||||
Topological domain | 635-642 | Cytoplasmic | ||||
Sequence: QLVTMGKK | ||||||
Transmembrane | 643-663 | Helical | ||||
Sequence: FFIYVFFFAVALLSLTARFVY | ||||||
Topological domain | 664-953 | Extracellular | ||||
Sequence: DIRPTGIPQPYHPDSQLITAGIWTIHFGLDNDMWASEDRMINLIKDMELDVVGLLETDTQRITMGNRDLTSKLAHDLNMYADFGPGPNKHTWGCVLLSKFPIVNSTHHLLPSPVGELAPAIHATLQTYNDTLVDVFVFHSGQEEDEEDRRLQSNYMAKLMGNTTRPAILLSYLVVDPGEGNYNTYVSETSGMHDIDPSDDDRWCEYILYRGLRRTGYARVARGTITDTELQVGKFQVLSEQALVEHSDSMYEYGHMSEPEYEDMKFPDKFLGEGERGHFYHVFDEPRYYL |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 57 | Causes destabilization of the protein and induces the release of cell wall proteins in the culture medium. | ||||
Sequence: G → R | ||||||
Mutagenesis | 472 | No effect on introduction of ceramides into the GPI anchor. | ||||
Sequence: H → A | ||||||
Mutagenesis | 693 | No effect on introduction of ceramides into the GPI anchor. | ||||
Sequence: D → A | ||||||
Mutagenesis | 713 | Impairs the introduction of ceramides into the GPI anchor. | ||||
Sequence: D → A | ||||||
Mutagenesis | 770 | No effect on introduction of ceramides into the GPI anchor. | ||||
Sequence: H → A | ||||||
Mutagenesis | 771 | No effect on introduction of ceramides into the GPI anchor. | ||||
Sequence: H → A | ||||||
Mutagenesis | 802 | Abrogates the introduction of ceramides into the GPI anchor. | ||||
Sequence: H → A | ||||||
Mutagenesis | 807 | No effect on introduction of ceramides into the GPI anchor. | ||||
Sequence: E → A | ||||||
Mutagenesis | 862 | Impairs the introduction of ceramides into the GPI anchor. | ||||
Sequence: D → A | ||||||
Mutagenesis | 882 | Abrogates the introduction of ceramides into the GPI anchor. | ||||
Sequence: R → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 16 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000021052 | 1-953 | Protein CWH43 | |||
Sequence: MLIINGKIIPIAHTICAFSAFFAALVTGYSLHFHKIVTNAHYTYPDEWFPSVSATIGDRYPERSIFQILIALTAFPRFLLLLGHYYLNQSKVCFLVGVLRTVSCGGWVYITSTDDHDIHDIFMITYIVLTLPWDIMITRYSSPLTSKNKGLTATIFFGTLFPMIYWYIQHSVQQRAGAYSIYAYFEWSLILLDIAFDAFAYADFKKIDIVLAFNEKPGNTSFFQIRDSSPINYGEEKSSELQKSGEKKVEKEKPVARSATGSYFRFDSFFYLLTNIFNGFLFWSNVTSLLCSIWHFPLWYMGISGYEAAILGYLGPIFLYLPFVSEAFTQYGVLLGGIIAIGAYIVQMPELRLISVAVGTSITVATFVQNLRYITNAETSFSFALTWLLGLVASVILKMGFYTNNPTWVILDERNGGYNKTALVLTVLFGMLSPYVNSINFEGKRNAQAKSASLIGKLFLAVGFGSLLFGIHQLLTDSSTTIYWAWEGYNESHGPLPWPWGALTCTVMLFASLSSVKFMGKPLVPCLLLLISTAVLSARSITQWPKYIFGGLLYAIAMLWLVPSYFSALGQVQNIWVYVLSFSVYIIFVLAHVWVVAYAFVPMGWVLREKIETVLAFSSTFIIIGALTCKNLNIQLVTMGKKFFIYVFFFAVALLSLTARFVYDIRPTGIPQPYHPDSQLITAGIWTIHFGLDNDMWASEDRMINLIKDMELDVVGLLETDTQRITMGNRDLTSKLAHDLNMYADFGPGPNKHTWGCVLLSKFPIVNSTHHLLPSPVGELAPAIHATLQTYNDTLVDVFVFHSGQEEDEEDRRLQSNYMAKLMGNTTRPAILLSYLVVDPGEGNYNTYVSETSGMHDIDPSDDDRWCEYILYRGLRRTGYARVARGTITDTELQVGKFQVLSEQALVEHSDSMYEYGHMSEPEYEDMKFPDKFLGEGERGHFYHVFDEPRYYL | ||||||
Glycosylation | 419 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 490 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 767 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 792 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 825 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-229 | PGAP2-like | ||||
Sequence: MLIINGKIIPIAHTICAFSAFFAALVTGYSLHFHKIVTNAHYTYPDEWFPSVSATIGDRYPERSIFQILIALTAFPRFLLLLGHYYLNQSKVCFLVGVLRTVSCGGWVYITSTDDHDIHDIFMITYIVLTLPWDIMITRYSSPLTSKNKGLTATIFFGTLFPMIYWYIQHSVQQRAGAYSIYAYFEWSLILLDIAFDAFAYADFKKIDIVLAFNEKPGNTSFFQIRDSS | ||||||
Region | 230-953 | PGAP2IP-like | ||||
Sequence: PINYGEEKSSELQKSGEKKVEKEKPVARSATGSYFRFDSFFYLLTNIFNGFLFWSNVTSLLCSIWHFPLWYMGISGYEAAILGYLGPIFLYLPFVSEAFTQYGVLLGGIIAIGAYIVQMPELRLISVAVGTSITVATFVQNLRYITNAETSFSFALTWLLGLVASVILKMGFYTNNPTWVILDERNGGYNKTALVLTVLFGMLSPYVNSINFEGKRNAQAKSASLIGKLFLAVGFGSLLFGIHQLLTDSSTTIYWAWEGYNESHGPLPWPWGALTCTVMLFASLSSVKFMGKPLVPCLLLLISTAVLSARSITQWPKYIFGGLLYAIAMLWLVPSYFSALGQVQNIWVYVLSFSVYIIFVLAHVWVVAYAFVPMGWVLREKIETVLAFSSTFIIIGALTCKNLNIQLVTMGKKFFIYVFFFAVALLSLTARFVYDIRPTGIPQPYHPDSQLITAGIWTIHFGLDNDMWASEDRMINLIKDMELDVVGLLETDTQRITMGNRDLTSKLAHDLNMYADFGPGPNKHTWGCVLLSKFPIVNSTHHLLPSPVGELAPAIHATLQTYNDTLVDVFVFHSGQEEDEEDRRLQSNYMAKLMGNTTRPAILLSYLVVDPGEGNYNTYVSETSGMHDIDPSDDDRWCEYILYRGLRRTGYARVARGTITDTELQVGKFQVLSEQALVEHSDSMYEYGHMSEPEYEDMKFPDKFLGEGERGHFYHVFDEPRYYL | ||||||
Region | 862-882 | Required for function in lipid remodeling | ||||
Sequence: DDDRWCEYILYRGLRRTGYAR |
Domain
The PGAP2-like region interacts with the PGAP2IP-like region.
Sequence similarities
In the N-terminal section; belongs to the PGAP2 family.
In the C-terminal section; belongs to the PGAP2IP family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length953
- Mass (Da)107,883
- Last updated2003-10-24 v2
- Checksum9F56CCD85824E848
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X59720 EMBL· GenBank· DDBJ | CAC42972.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006937 EMBL· GenBank· DDBJ | DAA07494.1 EMBL· GenBank· DDBJ | Genomic DNA |