P48284 · CAH4_RAT
- ProteinCarbonic anhydrase 4
- GeneCa4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids309 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the reversible hydration of carbon dioxide into bicarbonate and protons and thus is essential to maintaining intracellular and extracellular pH. May stimulate the sodium/bicarbonate transporter activity of SLC4A4 that acts in pH homeostasis. It is essential for acid overload removal from the retina and retina epithelium, and acid release in the choriocapillaris in the choroid.
Catalytic activity
- H+ + hydrogencarbonate = CO2 + H2OThis reaction proceeds in the forward and the backward directions.
Cofactor
Activity regulation
Inhibited by acetazolamide.
Features
Showing features for active site, binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | apical plasma membrane | |
Cellular Component | brush border membrane | |
Cellular Component | cell surface | |
Cellular Component | endoplasmic reticulum-Golgi intermediate compartment | |
Cellular Component | external side of plasma membrane | |
Cellular Component | extracellular exosome | |
Cellular Component | Golgi apparatus | |
Cellular Component | membrane | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | plasma membrane | |
Cellular Component | rough endoplasmic reticulum | |
Cellular Component | sarcolemma | |
Cellular Component | sarcoplasmic reticulum | |
Cellular Component | secretory granule membrane | |
Cellular Component | trans-Golgi network | |
Cellular Component | transport vesicle membrane | |
Molecular Function | carbonate dehydratase activity | |
Molecular Function | zinc ion binding | |
Biological Process | bicarbonate transport | |
Biological Process | one-carbon metabolic process | |
Biological Process | response to steroid hormone | |
Biological Process | response to xenobiotic stimulus |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCarbonic anhydrase 4
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP48284
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, lipidation, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-17 | |||||
Sequence: MQLLLALLALAYVAPST | ||||||
Chain | PRO_0000004232 | 18-281 | Carbonic anhydrase 4 | |||
Sequence: EDSHWCYEIQAKEPNSHCSGPEQWTGDCKKNQQSPINIVTSKTKLNPSLTPFTFVGYDQKKKWEVKNNQHSVEMSLGEDIYIFGGDLPTQYKAIQLHLHWSEESNKGSEHSIDGKHFAMEMHVVHKKMTTGDKVQDSDSKDKIAVLAFMVEVGNEVNEGFQPLVEALSRLSKPFTNSTVSESCLQDMLPEKKKLSAYFRYQGSLTTPGCDETVIWTVFEEPIKIHKDQFLEFSKKLYYDQEQKLNMKDNVRPLQPLGNRQVFRS | ||||||
Disulfide bond | 23↔35 | |||||
Sequence: CYEIQAKEPNSHC | ||||||
Disulfide bond | 45↔226 | |||||
Sequence: CKKNQQSPINIVTSKTKLNPSLTPFTFVGYDQKKKWEVKNNQHSVEMSLGEDIYIFGGDLPTQYKAIQLHLHWSEESNKGSEHSIDGKHFAMEMHVVHKKMTTGDKVQDSDSKDKIAVLAFMVEVGNEVNEGFQPLVEALSRLSKPFTNSTVSESCLQDMLPEKKKLSAYFRYQGSLTTPGC | ||||||
Glycosylation | 193 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Lipidation | 281 | GPI-anchor amidated serine | ||||
Sequence: S | ||||||
Propeptide | PRO_0000004233 | 282-309 | Removed in mature form | |||
Sequence: HASGRLLSLPLPTLLVPTLTCLVASFLH |
Post-translational modification
The N-terminus is blocked.
Glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Present in kidney and lung. Also particularly abundant in brain, muscle, heart and liver. Not detected in skin or spleen.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 20-282 | Alpha-carbonic anhydrase | ||||
Sequence: SHWCYEIQAKEPNSHCSGPEQWTGDCKKNQQSPINIVTSKTKLNPSLTPFTFVGYDQKKKWEVKNNQHSVEMSLGEDIYIFGGDLPTQYKAIQLHLHWSEESNKGSEHSIDGKHFAMEMHVVHKKMTTGDKVQDSDSKDKIAVLAFMVEVGNEVNEGFQPLVEALSRLSKPFTNSTVSESCLQDMLPEKKKLSAYFRYQGSLTTPGCDETVIWTVFEEPIKIHKDQFLEFSKKLYYDQEQKLNMKDNVRPLQPLGNRQVFRSH |
Sequence similarities
Belongs to the alpha-carbonic anhydrase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length309
- Mass (Da)35,076
- Last updated1996-02-01 v1
- Checksum9EBD1315348CFC8C
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6A1H6 | A0A8I6A1H6_RAT | Car4 | 308 | ||
A0A0H2UHB3 | A0A0H2UHB3_RAT | Car4 | 314 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
S68245 EMBL· GenBank· DDBJ | AAB29505.1 EMBL· GenBank· DDBJ | mRNA | ||
BC097329 EMBL· GenBank· DDBJ | AAH97329.1 EMBL· GenBank· DDBJ | mRNA |