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P00921 (CAH2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carbonic anhydrase 2

EC=4.2.1.1
Alternative name(s):
Carbonate dehydratase II
Carbonic anhydrase II
Short name=CA-II
Gene names
Name:CA2
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length260 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential for bone resorption and osteoclast differentiation By similarity. Reversible hydration of carbon dioxide.

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Zinc.

Enzyme regulation

Inhibited by acetazolamide By similarity.

Subunit structure

Interacts with SLC4A4. Interaction with SLC4A7 regulates SLC4A7 transporter activity By similarity.

Subcellular location

Cytoplasm.

Miscellaneous

One minor and two major forms were isolated chromatographically.

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3 Ref.4
Chain2 – 260259Carbonic anhydrase 2
PRO_0000077417

Regions

Region198 – 1992Substrate binding By similarity

Sites

Active site641Proton acceptor By similarity
Active site671 By similarity
Active site1271 By similarity
Metal binding941Zinc; catalytic
Metal binding961Zinc; catalytic
Metal binding1191Zinc; catalytic

Amino acid modifications

Modified residue21N-acetylserine

Natural variations

Natural variant571R → Q in one of the major forms.

Secondary structure

........................................................ 260
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00921 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A89412C23FFD19A7

FASTA26029,114
        10         20         30         40         50         60 
MSHHWGYGKH NGPEHWHKDF PIANGERQSP VDIDTKAVVQ DPALKPLALV YGEATSRRMV 

        70         80         90        100        110        120 
NNGHSFNVEY DDSQDKAVLK DGPLTGTYRL VQFHFHWGSS DDQGSEHTVD RKKYAAELHL 

       130        140        150        160        170        180 
VHWNTKYGDF GTAAQQPDGL AVVGVFLKVG DANPALQKVL DALDSIKTKG KSTDFPNFDP 

       190        200        210        220        230        240 
GSLLPNVLDY WTYPGSLTTP PLLESVTWIV LKEPISVSSQ QMLKFRTLNF NAEGEPELLM 

       250        260 
LANWRPAQPL KNRQVRGFPK 

« Hide

References

« Hide 'large scale' references
[1]"Full length cDNA of bovine carbonic anhydrase II."
Daigle R., Castro I., Desrochers M., Charest P.-M.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Bone marrow.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Hypothalamus.
[3]"Primary structure of bovine erythrocyte carbonic carbonic anhydrase CI. II. Complete sequence."
Sciaky M., Limozin N., Filippi-Foveau D., Gulian J.M., Laurent-Tabusse G.
Biochimie 58:1071-1082(1976) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-260.
Tissue: Erythrocyte.
[4]"Genetic independence of two forms of carbonic anhydrase from bovine erythrocytes."
Gulian J.M., Limozin N., Mallet B., di Costanzo J., Charrel M.
Biochimie 59:293-302(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[5]"Structure of bovine carbonic anhydrase II at 1.95 A resolution."
Saito R., Sato T., Ikai A., Tanaka N.
Acta Crystallogr. D 60:792-795(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION.
[6]"Antigen specificity and high affinity binding provided by one single loop of a camel single-domain antibody."
Desmyter A., Decanniere K., Muyldermans S., Wyns L.
J. Biol. Chem. 276:26285-26290(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 1-254 IN COMPLEX WITH ANTIBODY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY240020 mRNA. Translation: AAO85140.1.
BC103260 mRNA. Translation: AAI03261.1.
PIRCRBO2. A01144.
RefSeqNP_848667.1. NM_178572.2.
UniGeneBt.49731.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G6VX-ray3.50A1-254[»]
1V9EX-ray1.95A/B2-260[»]
1V9IX-ray2.95C2-260[»]
ProteinModelPortalP00921.
SMRP00921. Positions 2-260.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP00921. 1 interaction.

Chemistry

BindingDBP00921.
ChEMBLCHEMBL2096971.

Proteomic databases

PaxDbP00921.
PRIDEP00921.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID280740.
KEGGbta:280740.

Organism-specific databases

CTD760.

Phylogenomic databases

eggNOGCOG3338.
HOGENOMHOG000112637.
HOVERGENHBG002837.
InParanoidP00921.
KOK18245.

Family and domain databases

Gene3D3.10.200.10. 1 hit.
InterProIPR018443. CA2.
IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF90. PTHR18952:SF90. 1 hit.
PfamPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMSSF51069. SSF51069. 1 hit.
PROSITEPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00921.
NextBio20804911.

Entry information

Entry nameCAH2_BOVIN
AccessionPrimary (citable) accession number: P00921
Secondary accession number(s): Q3ZBJ5, Q865Y7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references