Q5S1S4 (CAH3_PIG) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 49.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Carbonic anhydrase 3 EC=4.2.1.1 Alternative name(s): Carbonate dehydratase III Carbonic anhydrase III Short name=CA-III | ||
| Gene names |
| ||
| Organism | Sus scrofa (Pig) [Complete proteome] | ||
| Taxonomic identifier | 9823 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus |
Protein attributes
| Sequence length | 260 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Reversible hydration of carbon dioxide. |
| Catalytic activity | H2CO3 = CO2 + H2O. |
| Cofactor | Zinc By similarity. |
| Enzyme regulation | Inhibited by acetazolamide By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Post-translational modification | S-glutathionylated in hepatocytes under oxidative stress By similarity. |
| Sequence similarities | Belongs to the alpha-carbonic anhydrase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Metal-binding Zinc |
| Molecular function | Lyase |
| PTM | Glutathionylation |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | one-carbon metabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | carbonate dehydratase activity Inferred from electronic annotation. Source: EC zinc ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 260 | 259 | Carbonic anhydrase 3 | PRO_0000077428 | |||||
Regions | |||||||||
| Region | 64 – 67 | 4 | Involved in proton transfer By similarity | ||||||
| Region | 198 – 199 | 2 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 127 | 1 | By similarity | ||||||
| Metal binding | 94 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 96 | 1 | Zinc; catalytic By similarity | ||||||
| Metal binding | 119 | 1 | Zinc; catalytic By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 182 | 1 | S-glutathionyl cysteine By similarity | ||||||
| Modified residue | 187 | 1 | S-glutathionyl cysteine By similarity | ||||||
Sequences
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References
| [1] | "Molecular characterization and association analysis of porcine CA3." Wang H.L., Zhu Z.M., Wang H., Yang S.L., Zhao S.H., Li K. Cytogenet. Genome Res. 115:129-133(2006) [PubMed: 17065793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Isolation, prediction of one novel swine gene that is differentially expressed in the longissimus dorsi muscle tissues from landrace large white cross combination." Liu G.Y., Xiong Z.Y. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [3] | "Characterization of the porcine carbonic anhydrase III (CA3) mRNA." Wu J., Deng C.Y., Xiong Y.Z. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Skeletal muscle. |
| [4] | "Characterization of the porcine carbonic anhydrase III (CA3) gene." Wu J., Deng C.Y., Xiong Y.Z., Zhou D.H. Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | DQ157048 Genomic DNA. Translation: ABA41599.1. AY789645 mRNA. Translation: AAV65838.1. AY789514 mRNA. Translation: AAV83540.1. DQ675018 Genomic DNA. Translation: ABG49150.1. |
| RefSeq | NP_001008688.1. NM_001008688.1. |
| UniGene | Ssc.10960. |
3D structure databases | |
| ProteinModelPortal | Q5S1S4. |
| SMR | Q5S1S4. Positions 2-260. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSSSCT00000006734; ENSSSCP00000006551; ENSSSCG00000006141. |
| GeneID | 494016. |
| KEGG | ssc:494016. |
Organism-specific databases | |
| CTD | 761. |
Phylogenomic databases | |
| GeneTree | ENSGT00560000076828. |
| HOVERGEN | HBG002837. |
| OMA | LQPWSVS. |
| OrthoDB | EOG4001JV. |
Family and domain databases | |
| InterPro | IPR001148. a_carbonic_anhydrase. IPR023561. Carbonic_anhydrase_a-class. IPR018338. Carbonic_anhydrase_a-class_CS. IPR018441. Carbonic_anhydrase_CA3. [Graphical view] |
| Gene3D | G3DSA:3.10.200.10. Euk_COanhd. 1 hit. |
| KO | K01672. |
| PANTHER | PTHR18952:SF29. Carbonic_anhydrase_CA3. 1 hit. PTHR18952. Euk_COanhd. 1 hit. |
| Pfam | PF00194. Carb_anhydrase. 1 hit. [Graphical view] |
| SMART | SM01057. Carb_anhydrase. 1 hit. [Graphical view] |
| SUPFAM | SSF51069. Euk_COanhd. 1 hit. |
| PROSITE | PS00162. ALPHA_CA_1. 1 hit. PS51144. ALPHA_CA_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CAH3_PIG | ||||||||
| Accession | Primary (citable) accession number: Q5S1S4 Secondary accession number(s): Q0Z809 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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