Reviewed,
UniProtKB/Swiss-Prot P24258 (CAH2_CHLRE)
Last modified
January 19, 2010.
Version 79.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Carbonic anhydrase 2 EC=4.2.1.1 Alternative name(s): Carbonate dehydratase 2 Short name=CA2 Cleaved into the following 2 chains: 1- Recommended name: Carbonic anhydrase 2 large chain 2- Recommended name: Carbonic anhydrase 2 small chain | ||
| Gene names |
| ||
| Organism | Chlamydomonas reinhardtii | ||
| Taxonomic identifier | 3055 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Chlorophyta › Chlorophyceae › Chlamydomonadales › Chlamydomonadaceae › Chlamydomonas |
Protein attributes
| Sequence length | 380 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Reversible hydration of carbon dioxide. |
| Catalytic activity | H2CO3 = CO2 + H2O. |
| Cofactor | Zinc. |
| Subunit structure | Tetramer of two large and two small subunits linked by two disulfide bonds. |
| Subcellular location | |
| Induction | Expressed under high-CO2 condition. Ref.2 |
| Sequence similarities | Belongs to the alpha-carbonic anhydrase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Periplasm |
| Domain | Signal |
| Ligand | Metal-binding Zinc |
| Molecular function | Lyase |
| PTM | Disulfide bond Glycoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | one-carbon metabolic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | periplasmic space 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: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 20 | 20 | Ref.3 Ref.4 | ||||||||
| Chain | 21 – 380 | 360 | Carbonic anhydrase 2 | PRO_0000004260 | |||||||
| Chain | 21 – ?343 | 323 | Carbonic anhydrase 2 large chain | PRO_0000004261 | |||||||
| Chain | 344 – 380 | 37 | Carbonic anhydrase 2 small chain | PRO_0000004262 | |||||||
Regions | |||||||||||
| Compositional bias | 310 – 324 | 15 | His-rich | ||||||||
Sites | |||||||||||
| Metal binding | 163 | 1 | Zinc; catalytic By similarity | ||||||||
| Metal binding | 165 | 1 | Zinc; catalytic By similarity | ||||||||
| Metal binding | 182 | 1 | Zinc; catalytic By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 101 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 135 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 297 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 21 | Interchain By similarity | |||||||||
| Disulfide bond | 61 ↔ 264 | By similarity | |||||||||
| Disulfide bond | 194 ↔ 198 | By similarity | |||||||||
| Disulfide bond | 296 ↔ 354 | Interchain (between large and small chains) By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 220 – 225 | 6 | Missing in CAA38360. Ref.1 | ||||||||
Sequences
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References
| [1] | "Nucleotide sequences of two genes CAH1 and CAH2 which encode carbonic anhydrase polypeptides in Chlamydomonas reinhardtii." Fukuzawa H., Fujiwara S., Tachiki A., Miyachi S. Nucleic Acids Res. 18:6441-6442(1990) [PubMed: 2243800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: IAM C-9. |
| [2] | "Structure and differential expression of two genes encoding carbonic anhydrase in Chlamydomonas reinhardtii." Fujiwara S., Fukuzawa H., Tachiki A., Miyachi S. Proc. Natl. Acad. Sci. U.S.A. 87:9779-9783(1990) [PubMed: 2124702] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION. |
| [3] | "Partial characterization of a new isoenzyme of carbonic anhydrase isolated from Chlamydomonas reinhardtii." Rawat M., Moroney J.V. J. Biol. Chem. 266:9719-9723(1991) [PubMed: 1903396] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-41 AND 344-363. |
| [4] | "Characterization of carbonic anhydrase isozyme CA2, which is the CAH2 gene product, in Chlamydomonas reinhardtii." Tachiki A., Fukuzawa H., Miyachi S. Biosci. Biotechnol. Biochem. 56:794-798(1992) [PubMed: 1368343] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-41 AND 344-364, CHARACTERIZATION. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X54488 Genomic DNA. Translation: CAA38360.1. |
| PIR | S14188. |
| RefSeq | XP_001692290.1. |
| UniGene | Cre.16115 |
3D structure databases | |
| SMR | P24258. Positions 38-293. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P24258. |
Genome annotation databases | |
| GeneID | 5717780. |
| KEGG | cre:CHLREDRAFT_128726. |
Enzyme and pathway databases | |
| BRENDA | 4.2.1.1. 144. |
Family and domain databases | |
| InterPro | IPR001148. Carbonic_anhydrase_a-class_cat. IPR018338. Carbonic_anhydrase_a-class_CS. IPR018340. Carbonic_anhydrase_CAH1-like. [Graphical view] |
| Gene3D | G3DSA:3.10.200.10. Euk_COanhd. 1 hit. |
| PANTHER | PTHR18952:SF2. Carbonic_anhydrase_CAH1-like. 1 hit. PTHR18952. Euk_COanhd. 1 hit. |
| Pfam | PF00194. Carb_anhydrase. 1 hit. [Graphical view] |
| PROSITE | PS00162. ALPHA_CA_1. 1 hit. PS51144. ALPHA_CA_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CAH2_CHLRE | ||||||||
| Accession | Primary (citable) accession number: P24258 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||

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