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Protein

Carbonic anhydrase 2

Gene

Ca2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential for bone resorption and osteoclast differentiation. Reversible hydration of carbon dioxide. Contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption. Stimulates the chloride-bicarbonate exchange activity of SLC26A6.1 Publication

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zn2+By similarity

Enzyme regulationi

Inhibited by acetazolamide.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei64 – 641Proton acceptorBy similarity
Active sitei67 – 671By similarity
Metal bindingi94 – 941Zinc; catalyticBy similarity
Metal bindingi96 – 961Zinc; catalyticBy similarity
Metal bindingi119 – 1191Zinc; catalyticBy similarity
Active sitei127 – 1271By similarity

GO - Molecular functioni

  • arylesterase activity Source: Ensembl
  • carbonate dehydratase activity Source: RGD
  • zinc ion binding Source: Ensembl

GO - Biological processi

  • angiotensin-activated signaling pathway Source: UniProtKB
  • carbon dioxide transport Source: Ensembl
  • cellular response to fluid shear stress Source: RGD
  • kidney development Source: RGD
  • morphogenesis of an epithelium Source: Ensembl
  • odontogenesis of dentin-containing tooth Source: RGD
  • one-carbon metabolic process Source: InterPro
  • osteoclast differentiation Source: RGD
  • positive regulation of bone resorption Source: RGD
  • positive regulation of cellular pH reduction Source: RGD
  • positive regulation of dipeptide transmembrane transport Source: UniProtKB
  • positive regulation of osteoclast differentiation Source: RGD
  • positive regulation of synaptic transmission, GABAergic Source: Ensembl
  • regulation of anion transport Source: UniProtKB
  • regulation of bone resorption Source: RGD
  • regulation of cellular pH Source: RGD
  • regulation of chloride transport Source: Ensembl
  • regulation of intracellular pH Source: UniProtKB
  • response to estrogen Source: RGD
  • response to organic substance Source: RGD
  • response to pH Source: RGD
  • response to steroid hormone Source: RGD
  • response to zinc ion Source: RGD
  • secretion Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-RNO-1237044. Erythrocytes take up carbon dioxide and release oxygen.
R-RNO-1247673. Erythrocytes take up oxygen and release carbon dioxide.
R-RNO-1475029. Reversible hydration of carbon dioxide.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase 2 (EC:4.2.1.1)
Alternative name(s):
Carbonate dehydratase II
Carbonic anhydrase II
Short name:
CA-II
Gene namesi
Name:Ca2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi2240. Ca2.

Subcellular locationi

  • Cytoplasm
  • Cell membrane By similarity

  • Note: Colocalized with SLC26A6 at the surface of the cell membrane in order to form a bicarbonate transport metabolon. Displaced from the cytosolic surface of the cell membrane by PKC in phorbol myristate acetate (PMA)-induced cells (By similarity).By similarity

GO - Cellular componenti

  • apical part of cell Source: RGD
  • axon Source: RGD
  • basolateral plasma membrane Source: RGD
  • cytoplasm Source: UniProtKB
  • cytosol Source: Ensembl
  • extracellular exosome Source: Ensembl
  • extracellular space Source: RGD
  • microvillus Source: RGD
  • myelin sheath Source: Ensembl
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL4706.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 260259Carbonic anhydrase 2PRO_0000077421Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21PhosphoserineCombined sources
Modified residuei87 – 871PhosphoserineBy similarity
Modified residuei165 – 1651PhosphoserineBy similarity
Modified residuei232 – 2321PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP27139.
PRIDEiP27139.

2D gel databases

World-2DPAGE0004:P27139.

PTM databases

iPTMnetiP27139.
PhosphoSiteiP27139.

Expressioni

Gene expression databases

GenevisibleiP27139. RN.

Interactioni

Subunit structurei

Interacts with SLC4A4 and SLC26A6. Interaction with SLC4A7 regulates SLC4A7 transporter activity (By similarity).By similarity

Protein-protein interaction databases

IntActiP27139. 2 interactions.
STRINGi10116.ENSRNOP00000013354.

Chemistry

BindingDBiP27139.

Structurei

3D structure databases

ProteinModelPortaliP27139.
SMRiP27139. Positions 2-260.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni198 – 1992Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP27139.
KOiK18245.
OMAiFHECVIW.
OrthoDBiEOG7WMCK7.
PhylomeDBiP27139.
TreeFamiTF316425.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR018443. CA2.
IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF120. PTHR18952:SF120. 1 hit.
PfamiPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTiSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMiSSF51069. SSF51069. 1 hit.
PROSITEiPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P27139-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHHWGYSKS NGPENWHKEF PIANGDRQSP VDIDTGTAQH DPSLQPLLIC
60 70 80 90 100
YDKVASKSIV NNGHSFNVEF DDSQDFAVLK EGPLSGSYRL IQFHFHWGSS
110 120 130 140 150
DGQGSEHTVN KKKYAAELHL VHWNTKYGDF GKAVQHPDGL AVLGIFLKIG
160 170 180 190 200
PASQGLQKIT EALHSIKTKG KRAAFANFDP CSLLPGNLDY WTYPGSLTTP
210 220 230 240 250
PLLECVTWIV LKEPITVSSE QMSHFRKLNF NSEGEAEELM VDNWRPAQPL
260
KNRKIKASFK
Length:260
Mass (Da):29,114
Last modified:January 23, 2007 - v2
Checksum:i8263A3C0B9B5753D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58294 mRNA. Translation: CAA41227.1.
AH006769 Genomic DNA. Translation: AAC53104.1.
BC065577 mRNA. Translation: AAH65577.1.
PIRiJH0527.
RefSeqiNP_062164.1. NM_019291.1.
UniGeneiRn.26083.

Genome annotation databases

EnsembliENSRNOT00000013354; ENSRNOP00000013354; ENSRNOG00000009629.
GeneIDi54231.
KEGGirno:54231.
UCSCiRGD:2240. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58294 mRNA. Translation: CAA41227.1.
AH006769 Genomic DNA. Translation: AAC53104.1.
BC065577 mRNA. Translation: AAH65577.1.
PIRiJH0527.
RefSeqiNP_062164.1. NM_019291.1.
UniGeneiRn.26083.

3D structure databases

ProteinModelPortaliP27139.
SMRiP27139. Positions 2-260.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP27139. 2 interactions.
STRINGi10116.ENSRNOP00000013354.

Chemistry

BindingDBiP27139.
ChEMBLiCHEMBL4706.

PTM databases

iPTMnetiP27139.
PhosphoSiteiP27139.

2D gel databases

World-2DPAGE0004:P27139.

Proteomic databases

PaxDbiP27139.
PRIDEiP27139.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000013354; ENSRNOP00000013354; ENSRNOG00000009629.
GeneIDi54231.
KEGGirno:54231.
UCSCiRGD:2240. rat.

Organism-specific databases

CTDi12349.
RGDi2240. Ca2.

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP27139.
KOiK18245.
OMAiFHECVIW.
OrthoDBiEOG7WMCK7.
PhylomeDBiP27139.
TreeFamiTF316425.

Enzyme and pathway databases

ReactomeiR-RNO-1237044. Erythrocytes take up carbon dioxide and release oxygen.
R-RNO-1247673. Erythrocytes take up oxygen and release carbon dioxide.
R-RNO-1475029. Reversible hydration of carbon dioxide.

Miscellaneous databases

NextBioi610662.
PROiP27139.

Gene expression databases

GenevisibleiP27139. RN.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR018443. CA2.
IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF120. PTHR18952:SF120. 1 hit.
PfamiPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTiSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMiSSF51069. SSF51069. 1 hit.
PROSITEiPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of a cDNA encoding rat brain carbonic anhydrase II and its deduced amino acid sequence."
    Stolle C.A., McGowan M.H., Heim R.A., Varia M., Neubauer J.A.
    Gene 109:265-267(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. "Characterization of the rat carbonic anhydrase II gene structure: sequence analysis of the 5' flanking region and 3' UTR."
    McGowan M.H., Neubauer J.A., Stolle C.A.
    Gene 186:181-188(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  4. Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 58-80; 81-110; 114-126; 133-158 AND 213-226, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain, Hippocampus and Spinal cord.
  5. "Carbonic anhydrase II plays a major role in osteoclast differentiation and bone resorption by effecting the steady state intracellular pH and Ca2+."
    Lehenkari P., Hentunen T.A., Laitala-Leinonen T., Tuukkanen J., Vaeaenaenen H.K.
    Exp. Cell Res. 242:128-137(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCAH2_RAT
AccessioniPrimary (citable) accession number: P27139
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.