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P00919 (CAH2_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
OrganismOryctolagus cuniculus (Rabbit) [Complete proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

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.

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandMetal-binding
Zinc
   Molecular functionLyase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processone-carbon metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functioncarbonate dehydratase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 260259Carbonic anhydrase 2
PRO_0000077420

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 variant2041E → Q.

Experimental info

Sequence conflict241N → D AA sequence Ref.1
Sequence conflict361N → D AA sequence Ref.1
Sequence conflict501C → S AA sequence Ref.1
Sequence conflict771T → S AA sequence Ref.1
Sequence conflict1031Q → E AA sequence Ref.1
Sequence conflict1771D → N AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
P00919 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 1601916B7D8A2828

FASTA26029,500
        10         20         30         40         50         60 
MSHHWGYGKH NGPEHWHKDF PIANGERQSP IDIDTNAAKH DPSLKPLRVC YEHPISRRII 

        70         80         90        100        110        120 
NNGHSFNVEF DDSHDKTVLK EGPLEGTYRL IQFHFHWGSS DGQGSEHTVN KKKYAAELHL 

       130        140        150        160        170        180 
VHWNTKYGDF GKAVKHPDGL AVLGIFLKIG SATPGLQKVV DTLSSIKTKG KSVDFTDFDP 

       190        200        210        220        230        240 
RGLLPESLDY WTYPGSLTTP PLLECVTWIV LKEPITVSSE QMLKFRNLNF NKEAEPEEPM 

       250        260 
VDNWRPTQPL KGRQVKASFV

« Hide

References

[1]"Amino acid sequence of rabbit carbonic anhydrase II."
Ferrell R.E., Stroup S.K., Tanis R.J., Tashian R.E.
Biochim. Biophys. Acta 533:1-11(1978) [PubMed: 416851] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-260.
[2]"Carbonic anhydrase II mRNA is induced in rabbit kidney cortex during chronic metabolic acidosis."
Schwartz G.J., Winkler C.A., Zavilowitz B.J., Bargiello T.
Am. J. Physiol. 265:F764-F772(1993) [PubMed: 8285209] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-239.
Strain: New Zealand white.
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M98395 mRNA. Translation: AAA80531.1.
PIRCRRB2. A01142.
RefSeqNP_001182637.1. NM_001195708.1.
UniGeneOcu.268.

3D structure databases

ProteinModelPortalP00919.
SMRP00919. Positions 2-259.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSOCUT00000011742; ENSOCUP00000010096; ENSOCUG00000011742.
GeneID100009156.

Organism-specific databases

CTD760.

Phylogenomic databases

eggNOGmaNOG05017.
GeneTreeENSGT00560000076828.
HOVERGENHBG002837.
OrthoDBEOG4X97HR.

Family and domain databases

InterProIPR001148. a_carbonic_anhydrase.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018440. Carbonic_anhydrase_CA2.
[Graphical view]
Gene3DG3DSA:3.10.200.10. Euk_COanhd. 1 hit.
PANTHERPTHR18952:SF28. Carbonic_anhydrase_CA2. 1 hit.
PTHR18952. Euk_COanhd. 1 hit.
PfamPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMSSF51069. Euk_COanhd. 1 hit.
PROSITEPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCAH2_RABIT
AccessionPrimary (citable) accession number: P00919
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 87 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

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