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Reviewed, UniProtKB/Swiss-Prot P00919 (CAH2_RABIT)

Last modified September 22, 2009. Version 69. 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

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Names and origin

Protein namesRecommended name:
    Carbonic anhydrase 2
    EC=4.2.1.1
Alternative name(s):
    Carbonic anhydrase II
      Short name=CA-II
    Carbonate dehydratase II
Gene names
Name: CA2
OrganismOryctolagus cuniculus (Rabbit)
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

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Protein attributes

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

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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.

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.

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Ontologies

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

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Sites

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

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Sequences

Sequence LengthMass (Da)Tools
P00919-1 [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

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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.

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Cross-references

Sequence databases

M98395 mRNA. Translation: AAA80531.1.
PIRCRRB2. A01142.
UniGeneOcu.268

3D structure databases

HSSPHSSP built from PDB template 1BV3 based on UniProtKB P00918.
SMRP00919. Positions 3-259.
ModBaseSearch...

Phylogenomic databases

HOVERGENP00919.

Enzyme and pathway databases

BRENDA4.2.1.1. 255.

Family and domain databases

InterProIPR001148. Carbonic_anhydrase_a-class_cat.
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]
ProDomPD000865. Euk_COanhd. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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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: September 22, 2009
This is version 69 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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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