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P00920 (CAH2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. 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·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
Synonyms:Car2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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. 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. Ref.9

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. Interacts with SLC26A6 By similarity.

Subcellular location

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.

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
   LigandMetal-binding
Zinc
   Molecular functionLyase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiotensin-activated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

carbon dioxide transport

Inferred from mutant phenotype PubMed 16217040. Source: MGI

kidney development

Inferred from electronic annotation. Source: Ensembl

morphogenesis of an epithelium

Inferred from mutant phenotype PubMed 16217040. Source: MGI

odontogenesis of dentin-containing tooth

Inferred from electronic annotation. Source: Ensembl

one-carbon metabolic process

Inferred from electronic annotation. Source: InterPro

positive regulation of bone resorption

Inferred from electronic annotation. Source: Ensembl

positive regulation of cellular pH reduction

Inferred from electronic annotation. Source: Ensembl

positive regulation of dipeptide transmembrane transport

Inferred from mutant phenotype Ref.9. Source: UniProtKB

positive regulation of osteoclast differentiation

Inferred from electronic annotation. Source: Ensembl

regulation of anion transport

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of intracellular pH

Inferred from mutant phenotype Ref.9. Source: UniProtKB

response to estrogen

Inferred from electronic annotation. Source: Ensembl

response to pH

Inferred from electronic annotation. Source: Ensembl

response to zinc ion

Inferred from electronic annotation. Source: Ensembl

secretion

Inferred from mutant phenotype PubMed 16217040. Source: MGI

   Cellular_componentapical part of cell

Inferred from electronic annotation. Source: Ensembl

axon

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 15385584. Source: UniProtKB

extracellular space

Inferred from electronic annotation. Source: Ensembl

microvillus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncarbonate dehydratase activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 260259Carbonic anhydrase 2
PRO_0000077419

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 By similarity

Experimental info

Sequence conflict391Q → H in AAA37356. Ref.1
Sequence conflict391Q → H in AAH55291. Ref.4
Sequence conflict1451I → Y in AAA37356. Ref.1
Sequence conflict1451I → Y in AAA37357. Ref.2
Sequence conflict2131E → D in AAA37357. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P00920 [UniParc].

Last modified May 1, 2007. Version 4.
Checksum: 095760368D446AA6

FASTA26029,033
        10         20         30         40         50         60 
MSHHWGYSKH NGPENWHKDF PIANGDRQSP VDIDTATAQH DPALQPLLIS YDKAASKSIV 

        70         80         90        100        110        120 
NNGHSFNVEF DDSQDNAVLK GGPLSDSYRL IQFHFHWGSS DGQGSEHTVN KKKYAAELHL 

       130        140        150        160        170        180 
VHWNTKYGDF GKAVQQPDGL AVLGIFLKIG PASQGLQKVL EALHSIKTKG KRAAFANFDP 

       190        200        210        220        230        240 
CSLLPGNLDY WTYPGSLTTP PLLECVTWIV LREPITVSSE QMSHFRTLNF NEEGDAEEAM 

       250        260 
VDNWRPAQPL KNRKIKASFK 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence and derived amino acid sequence of cDNA coding for mouse carbonic anhydrase II."
Curtis P.J., Withers E., Demuth D., Watt R., Venta P.J., Tashian R.E.
Gene 25:325-332(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Structure and exon to protein domain relationships of the mouse carbonic anhydrase II gene."
Venta P.J., Montgomery J.C., Hewett-Emmett D., Wiebauer K., Tashian R.E.
J. Biol. Chem. 260:12130-12135(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Kidney.
[4]"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].
Strain: FVB/N.
Tissue: Colon.
[5]"Comparison of the 5' regions of human and mouse carbonic anhydrase II genes and identification of possible regulatory elements."
Venta P.J., Montgomery J.C., Hewett-Emmett D., Tashian R.E.
Biochim. Biophys. Acta 826:195-201(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77.
[6]Lubec G., Klug S., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 19-53; 58-80; 90-111; 114-126; 133-167 AND 213-226, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[7]"Cloning of mouse carbonic anhydrase mRNA and its induction in mouse erythroleukemic cells."
Curtis P.J.
J. Biol. Chem. 258:4459-4463(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 155-178 AND 214-240.
[8]"Organization of the mouse and human carbonic anhydrase II genes."
Venta P.J., Montgomery J.C., Wiebauer K., Hewett-Emmett D., Tashian R.E.
Ann. N. Y. Acad. Sci. 429:309-323(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 241-260.
[9]"Putative anion transporter-1 (Pat-1, Slc26a6) contributes to intracellular pH regulation during H+-dipeptide transport in duodenal villous epithelium."
Simpson J.E., Walker N.M., Supuran C.T., Soleimani M., Clarke L.L.
Am. J. Physiol. 298:G683-G691(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K00811 mRNA. Translation: AAA37356.1.
M81022 expand/collapse EMBL AC list , M81016, M81017, M81018, M81019, M81020, M81021 Genomic DNA. Translation: AAA37357.1.
AK002333 mRNA. Translation: BAB22019.1.
AK002498 mRNA. Translation: BAB22146.2.
BC055291 mRNA. Translation: AAH55291.1.
M25944 mRNA. Translation: AAA39505.1.
PIRCRMS2. A23900.
RefSeqNP_033931.4. NM_009801.4.
XP_006530113.1. XM_006530050.1.
UniGeneMm.1186.

3D structure databases

ProteinModelPortalP00920.
SMRP00920. Positions 2-260.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198483. 1 interaction.
IntActP00920. 6 interactions.
MINTMINT-1869480.

Chemistry

ChEMBLCHEMBL3689.

PTM databases

PhosphoSiteP00920.

Proteomic databases

PaxDbP00920.
PRIDEP00920.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029078; ENSMUSP00000029078; ENSMUSG00000027562.
GeneID12349.
KEGGmmu:12349.
UCSCuc008oqt.2. mouse.

Organism-specific databases

CTD12349.
MGIMGI:88269. Car2.

Phylogenomic databases

eggNOGCOG3338.
GeneTreeENSGT00750000117305.
HOGENOMHOG000112637.
HOVERGENHBG002837.
InParanoidP00920.
KOK01672.
OMADEANEAC.
OrthoDBEOG7WMCK7.
PhylomeDBP00920.
TreeFamTF316425.

Gene expression databases

BgeeP00920.
CleanExMM_CAR2.
GenevestigatorP00920.

Family and domain databases

Gene3D3.10.200.10. 1 hit.
InterProIPR018443. CA2/13.
IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF31. PTHR18952:SF31. 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

ChiTaRSCA2. mouse.
NextBio280996.
PROP00920.
SOURCESearch...

Entry information

Entry nameCAH2_MOUSE
AccessionPrimary (citable) accession number: P00920
Secondary accession number(s): Q6LDQ7 expand/collapse secondary AC list , Q7TPE1, Q9DCT3, Q9DCY9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 1, 2007
Last modified: April 16, 2014
This is version 130 of the entry and version 4 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot