Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Carbonic anhydrase 2

Gene

Ca2

Organism
Mus musculus (Mouse)
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

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; catalytic
Metal bindingi96 – 961Zinc; catalytic
Metal bindingi119 – 1191Zinc; catalytic
Active sitei127 – 1271By similarity

GO - Molecular functioni

  1. carbonate dehydratase activity Source: MGI
  2. zinc ion binding Source: MGI

GO - Biological processi

  1. angiotensin-activated signaling pathway Source: UniProtKB
  2. carbon dioxide transport Source: MGI
  3. cellular response to fluid shear stress Source: Ensembl
  4. kidney development Source: Ensembl
  5. morphogenesis of an epithelium Source: MGI
  6. odontogenesis of dentin-containing tooth Source: Ensembl
  7. one-carbon metabolic process Source: InterPro
  8. positive regulation of bone resorption Source: Ensembl
  9. positive regulation of cellular pH reduction Source: MGI
  10. positive regulation of dipeptide transmembrane transport Source: UniProtKB
  11. positive regulation of osteoclast differentiation Source: Ensembl
  12. positive regulation of synaptic transmission, GABAergic Source: MGI
  13. regulation of anion transport Source: UniProtKB
  14. regulation of chloride transport Source: MGI
  15. regulation of intracellular pH Source: UniProtKB
  16. regulation of pH Source: MGI
  17. response to estrogen Source: Ensembl
  18. response to pH Source: Ensembl
  19. response to zinc ion Source: Ensembl
  20. secretion Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_309678. Erythrocytes take up oxygen and release carbon dioxide.
REACT_318918. Erythrocytes take up carbon dioxide and release oxygen.
REACT_327358. 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
Synonyms:Car2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:88269. Car2.

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

  1. apical part of cell Source: MGI
  2. axon Source: Ensembl
  3. basolateral plasma membrane Source: Ensembl
  4. cytoplasm Source: UniProtKB
  5. cytosol Source: UniProtKB
  6. extracellular space Source: Ensembl
  7. extracellular vesicular exosome Source: MGI
  8. microvillus Source: Ensembl
  9. myelin sheath Source: UniProtKB
  10. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 260259Carbonic anhydrase 2PRO_0000077419Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei165 – 1651PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP00920.
PaxDbiP00920.
PRIDEiP00920.

PTM databases

PhosphoSiteiP00920.

Expressioni

Gene expression databases

BgeeiP00920.
CleanExiMM_CAR2.
GenevestigatoriP00920.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi198483. 2 interactions.
IntActiP00920. 6 interactions.
MINTiMINT-1869480.

Structurei

3D structure databases

ProteinModelPortaliP00920.
SMRiP00920. 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

eggNOGiCOG3338.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP00920.
KOiK18245.
OMAiMAHHWGY.
OrthoDBiEOG7WMCK7.
PhylomeDBiP00920.
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:SF90. PTHR18952:SF90. 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.

P00920-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHHWGYSKH NGPENWHKDF PIANGDRQSP VDIDTATAQH DPALQPLLIS
60 70 80 90 100
YDKAASKSIV NNGHSFNVEF DDSQDNAVLK GGPLSDSYRL IQFHFHWGSS
110 120 130 140 150
DGQGSEHTVN KKKYAAELHL VHWNTKYGDF GKAVQQPDGL AVLGIFLKIG
160 170 180 190 200
PASQGLQKVL EALHSIKTKG KRAAFANFDP CSLLPGNLDY WTYPGSLTTP
210 220 230 240 250
PLLECVTWIV LREPITVSSE QMSHFRTLNF NEEGDAEEAM VDNWRPAQPL
260
KNRKIKASFK
Length:260
Mass (Da):29,033
Last modified:May 1, 2007 - v4
Checksum:i095760368D446AA6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 391Q → H in AAA37356 (PubMed:6420240).Curated
Sequence conflicti39 – 391Q → H in AAH55291 (PubMed:15489334).Curated
Sequence conflicti145 – 1451I → Y in AAA37356 (PubMed:6420240).Curated
Sequence conflicti145 – 1451I → Y in AAA37357 (PubMed:2995362).Curated
Sequence conflicti213 – 2131E → D in AAA37357 (PubMed:2995362).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00811 mRNA. Translation: AAA37356.1.
M81022
, 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.
CCDSiCCDS17251.1.
PIRiA23900. CRMS2.
RefSeqiNP_033931.4. NM_009801.4.
XP_006530113.1. XM_006530050.1.
UniGeneiMm.1186.

Genome annotation databases

EnsembliENSMUST00000029078; ENSMUSP00000029078; ENSMUSG00000027562.
GeneIDi12349.
KEGGimmu:12349.
UCSCiuc008oqt.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00811 mRNA. Translation: AAA37356.1.
M81022
, 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.
CCDSiCCDS17251.1.
PIRiA23900. CRMS2.
RefSeqiNP_033931.4. NM_009801.4.
XP_006530113.1. XM_006530050.1.
UniGeneiMm.1186.

3D structure databases

ProteinModelPortaliP00920.
SMRiP00920. Positions 2-260.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198483. 2 interactions.
IntActiP00920. 6 interactions.
MINTiMINT-1869480.

Chemistry

ChEMBLiCHEMBL3689.

PTM databases

PhosphoSiteiP00920.

Proteomic databases

MaxQBiP00920.
PaxDbiP00920.
PRIDEiP00920.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029078; ENSMUSP00000029078; ENSMUSG00000027562.
GeneIDi12349.
KEGGimmu:12349.
UCSCiuc008oqt.2. mouse.

Organism-specific databases

CTDi12349.
MGIiMGI:88269. Car2.

Phylogenomic databases

eggNOGiCOG3338.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP00920.
KOiK18245.
OMAiMAHHWGY.
OrthoDBiEOG7WMCK7.
PhylomeDBiP00920.
TreeFamiTF316425.

Enzyme and pathway databases

ReactomeiREACT_309678. Erythrocytes take up oxygen and release carbon dioxide.
REACT_318918. Erythrocytes take up carbon dioxide and release oxygen.
REACT_327358. Reversible hydration of carbon dioxide.

Miscellaneous databases

NextBioi280996.
PROiP00920.
SOURCEiSearch...

Gene expression databases

BgeeiP00920.
CleanExiMM_CAR2.
GenevestigatoriP00920.

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:SF90. PTHR18952:SF90. 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. "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(1982) [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(1984) [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.
    , 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(2004) [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(2003) [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(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77.
  6. Lubec G., Klug S., Kang S.U.
    Submitted (MAR-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(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 155-178 AND 214-240.
  8. 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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiCAH2_MOUSE
AccessioniPrimary (citable) accession number: P00920
Secondary accession number(s): Q6LDQ7
, Q7TPE1, Q9DCT3, Q9DCY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 1, 2007
Last modified: April 1, 2015
This is version 141 of the entry and version 4 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.