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Reviewed, UniProtKB/Swiss-Prot P24258 (CAH2_CHLRE)

Last modified January 19, 2010. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
Name: CAH2
OrganismChlamydomonas reinhardtii
Taxonomic identifier3055 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

Protein attributes

Sequence length380 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Periplasm.

Induction

Expressed under high-CO2 condition. Ref.2

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionLyase
   PTMDisulfide bond
Glycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processone-carbon metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncarbonate dehydratase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.3 Ref.4
Chain21 – 380360Carbonic anhydrase 2
PRO_0000004260
Chain21 – ?343323Carbonic anhydrase 2 large chain
PRO_0000004261
Chain344 – 38037Carbonic anhydrase 2 small chain
PRO_0000004262

Regions

Compositional bias310 – 32415His-rich

Sites

Metal binding1631Zinc; catalytic By similarity
Metal binding1651Zinc; catalytic By similarity
Metal binding1821Zinc; catalytic By similarity

Amino acid modifications

Glycosylation1011N-linked (GlcNAc...) Potential
Glycosylation1351N-linked (GlcNAc...) Potential
Glycosylation2971N-linked (GlcNAc...) Potential
Disulfide bond21Interchain By similarity
Disulfide bond61 ↔ 264 By similarity
Disulfide bond194 ↔ 198 By similarity
Disulfide bond296 ↔ 354Interchain (between large and small chains) By similarity

Experimental info

Sequence conflict220 – 2256Missing in CAA38360. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P24258-1 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: 5ABC3823A1DD7862

FASTA38042,172
        10         20         30         40         50         60 
MARTGALLLA ALALAGCAQA CIYKFGTSPD SKATHTGDHW DHSLNGENWE GKDGAGNPWV 

        70         80         90        100        110        120 
CKTGRKQSPI NVPQYHVLDG KGSKIATGLQ TQWSYPDLMS NGSSVQVINN GHTIQVQWTY 

       130        140        150        160        170        180 
DYAGHATIAI PAMRNQSNRI VDVLEMRPND ASDRVTAVPT QFHFHSTSEH LLAGKIFPLE 

       190        200        210        220        230        240 
LHIVHKVTDK LEACKGGCFS VTGILFQLDN GPDNELLEPI FANMPTREGT FTNLPAGTTI 

       250        260        270        280        290        300 
KLGELLPSDR DYVTYEGSLT TPPCSEGLLW HVMTQPQRIS FGQWNRYRLA VGEKECNSTE 

       310        320        330        340        350        360 
TDAAHADAGH HHHHHRRLLH NHAHLEEVPA ATSEPKHYFR RVMEETENPD AYTCTTVAFG 

       370        380 
QNFRNAQYAN GRTIKLARYE 

« Hide

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.
PIRS14188.
RefSeqXP_001692290.1.
UniGeneCre.16115

3D structure databases

SMRP24258. Positions 38-293.
ModBaseSearch...

Proteomic databases

PRIDEP24258.

Genome annotation databases

GeneID5717780.
KEGGcre:CHLREDRAFT_128726.

Enzyme and pathway databases

BRENDA4.2.1.1. 144.

Family and domain databases

InterProIPR001148. Carbonic_anhydrase_a-class_cat.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018340. Carbonic_anhydrase_CAH1-like.
[Graphical view]
Gene3DG3DSA:3.10.200.10. Euk_COanhd. 1 hit.
PANTHERPTHR18952:SF2. Carbonic_anhydrase_CAH1-like. 1 hit.
PTHR18952. Euk_COanhd. 1 hit.
PfamPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
PROSITEPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCAH2_CHLRE
AccessionPrimary (citable) accession number: P24258
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: January 19, 2010
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents