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P00920

- CAH2_MOUSE

UniProt

P00920 - CAH2_MOUSE

Protein

Carbonic anhydrase 2

Gene

Ca2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 4 (01 May 2007)
      Previous versions | rss
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    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

    Zinc.

    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: Ensembl

    GO - Biological processi

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

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_199094. Erythrocytes take up carbon dioxide and release oxygen.
    REACT_199096. Reversible hydration of carbon dioxide.
    REACT_199098. Erythrocytes take up oxygen and release 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: 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: Ensembl
    2. axon Source: Ensembl
    3. basolateral plasma membrane Source: Ensembl
    4. cytoplasm Source: UniProtKB
    5. cytosol Source: UniProtKB
    6. extracellular space Source: Ensembl
    7. microvillus Source: Ensembl
    8. myelin sheath Source: MGI
    9. plasma membrane Source: UniProtKB

    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

    Keywords - PTMi

    Acetylation

    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. 1 interaction.
    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.
    GeneTreeiENSGT00750000117305.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiP00920.
    KOiK18245.
    OMAiCFNAENE.
    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

    MSHHWGYSKH NGPENWHKDF PIANGDRQSP VDIDTATAQH DPALQPLLIS    50
    YDKAASKSIV NNGHSFNVEF DDSQDNAVLK GGPLSDSYRL IQFHFHWGSS 100
    DGQGSEHTVN KKKYAAELHL VHWNTKYGDF GKAVQQPDGL AVLGIFLKIG 150
    PASQGLQKVL EALHSIKTKG KRAAFANFDP CSLLPGNLDY WTYPGSLTTP 200
    PLLECVTWIV LREPITVSSE QMSHFRTLNF NEEGDAEEAM VDNWRPAQPL 250
    KNRKIKASFK 260
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS17251.1.
    PIRi A23900. CRMS2.
    RefSeqi NP_033931.4. NM_009801.4.
    XP_006530113.1. XM_006530050.1.
    UniGenei Mm.1186.

    3D structure databases

    ProteinModelPortali P00920.
    SMRi P00920. Positions 2-260.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198483. 1 interaction.
    IntActi P00920. 6 interactions.
    MINTi MINT-1869480.

    Chemistry

    ChEMBLi CHEMBL3689.

    PTM databases

    PhosphoSitei P00920.

    Proteomic databases

    MaxQBi P00920.
    PaxDbi P00920.
    PRIDEi P00920.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029078 ; ENSMUSP00000029078 ; ENSMUSG00000027562 .
    GeneIDi 12349.
    KEGGi mmu:12349.
    UCSCi uc008oqt.2. mouse.

    Organism-specific databases

    CTDi 12349.
    MGIi MGI:88269. Car2.

    Phylogenomic databases

    eggNOGi COG3338.
    GeneTreei ENSGT00750000117305.
    HOGENOMi HOG000112637.
    HOVERGENi HBG002837.
    InParanoidi P00920.
    KOi K18245.
    OMAi CFNAENE.
    OrthoDBi EOG7WMCK7.
    PhylomeDBi P00920.
    TreeFami TF316425.

    Enzyme and pathway databases

    Reactomei REACT_199094. Erythrocytes take up carbon dioxide and release oxygen.
    REACT_199096. Reversible hydration of carbon dioxide.
    REACT_199098. Erythrocytes take up oxygen and release carbon dioxide.

    Miscellaneous databases

    ChiTaRSi CA2. mouse.
    NextBioi 280996.
    PROi P00920.
    SOURCEi Search...

    Gene expression databases

    Bgeei P00920.
    CleanExi MM_CAR2.
    Genevestigatori P00920.

    Family and domain databases

    Gene3Di 3.10.200.10. 1 hit.
    InterProi IPR018443. CA2.
    IPR001148. Carbonic_anhydrase_a.
    IPR023561. Carbonic_anhydrase_a-class.
    IPR018338. Carbonic_anhydrase_a-class_CS.
    [Graphical view ]
    PANTHERi PTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF90. PTHR18952:SF90. 1 hit.
    Pfami PF00194. Carb_anhydrase. 1 hit.
    [Graphical view ]
    SMARTi SM01057. Carb_anhydrase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51069. SSF51069. 1 hit.
    PROSITEi PS00162. ALPHA_CA_1. 1 hit.
    PS51144. ALPHA_CA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.

    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: October 1, 2014
    This is version 135 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