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Reviewed, UniProtKB/Swiss-Prot P00922 (CAH2_SHEEP)

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

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
OrganismOvis aries (Sheep)
Taxonomic identifier9940 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis

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.

Subunit structure

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

Subcellular location

Cytoplasm.

Miscellaneous

One minor and three major forms were isolated chromatographically.

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 260259Carbonic anhydrase 2
PRO_0000077422

Sites

Metal binding941Zinc; catalytic
Metal binding961Zinc; catalytic
Metal binding1191Zinc; catalytic

Amino acid modifications

Modified residue21N-acetylserine Ref.1 Ref.2

Natural variations

Natural variant361K → T in one of the major forms. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P00922-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 5881DD762616363D

FASTA26029,211
        10         20         30         40         50         60 
MSHHWGYGEH NGPEHWHKDF PIADGERQSP VDIDTKAVVP DPALKPLALL YEQAASRRMV 

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

       130        140        150        160        170        180 
VHWNTKYGDF GTAAQQPDGL AVVGVFLKVG DANPALQKVL DVLDSIKTKG KSADFPNFDP 

       190        200        210        220        230        240 
SSLLKRALNY WTYPGSLTNP PLLESVTWVV LKEPTSVSSQ QMLKFRSLNF NAEGEPELLM 

       250        260 
LANWRPAQPL KNRQVRVFPK 

« Hide

References

[1]"Amino acid sequence of sheep carbonic anhydrase C."
Tanis R.J., Ferrell R.E., Tashian R.E.
Biochim. Biophys. Acta 371:534-548(1974) [PubMed: 4215456] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-260, ACETYLATION AT SER-2.
[2]"Multiple molecular forms of erythrocyte carbonic anhydrase of sheep."
Mallet B., Gulian J.M., Sciaky M., Laurent G., Charrel M.
Biochim. Biophys. Acta 576:290-304(1979) [PubMed: 106895] [Abstract]
Cited for: VARIANT THR-36.

Cross-references

Sequence databases

PIRCRSH2. A01145.

3D structure databases

HSSPHSSP built from PDB template 1CIM based on UniProtKB P00918.
SMRP00922. Positions 2-260.
ModBaseSearch...

Phylogenomic databases

HOVERGENP00922.

Enzyme and pathway databases

BRENDA4.2.1.1. 271.

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...

Entry information

Entry nameCAH2_SHEEP
AccessionPrimary (citable) accession number: P00922
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 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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