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P00921

- CAH2_BOVIN

UniProt

P00921 - CAH2_BOVIN

Protein

Carbonic anhydrase 2

Gene

CA2

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Essential for bone resorption and osteoclast differentiation By similarity. Reversible hydration of carbon dioxide.By similarity

    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: UniProtKB-EC
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. angiotensin-activated signaling pathway Source: UniProtKB
    2. one-carbon metabolic process Source: InterPro
    3. positive regulation of dipeptide transmembrane transport Source: UniProtKB
    4. regulation of anion transport Source: UniProtKB
    5. regulation of intracellular pH Source: UniProtKB

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Metal-binding, Zinc

    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
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 260259Carbonic anhydrase 2PRO_0000077417Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP00921.
    PRIDEiP00921.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    IntActiP00921. 1 interaction.

    Structurei

    Secondary structure

    1
    260
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni9 – 113
    Turni13 – 153
    Helixi16 – 183
    Helixi21 – 244
    Beta strandi25 – 273
    Beta strandi31 – 333
    Helixi35 – 373
    Beta strandi47 – 504
    Beta strandi56 – 616
    Beta strandi63 – 708
    Beta strandi73 – 819
    Beta strandi88 – 9710
    Beta strandi99 – 1024
    Beta strandi106 – 1094
    Beta strandi115 – 12410
    Helixi125 – 1273
    Helixi130 – 1334
    Beta strandi139 – 15113
    Helixi154 – 1563
    Helixi157 – 1626
    Helixi163 – 1653
    Beta strandi167 – 1693
    Beta strandi172 – 1743
    Helixi180 – 1834
    Beta strandi190 – 1956
    Beta strandi206 – 2138
    Beta strandi215 – 2173
    Helixi219 – 2257
    Beta strandi228 – 2314
    Beta strandi256 – 2583

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G6VX-ray3.50A1-254[»]
    1V9EX-ray1.95A/B2-260[»]
    1V9IX-ray2.95C2-260[»]
    ProteinModelPortaliP00921.
    SMRiP00921. Positions 2-260.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00921.

    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.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiP00921.
    KOiK18245.

    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.

    P00921-1 [UniParc]FASTAAdd to Basket

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    MSHHWGYGKH NGPEHWHKDF PIANGERQSP VDIDTKAVVQ DPALKPLALV    50
    YGEATSRRMV NNGHSFNVEY DDSQDKAVLK DGPLTGTYRL VQFHFHWGSS 100
    DDQGSEHTVD RKKYAAELHL VHWNTKYGDF GTAAQQPDGL AVVGVFLKVG 150
    DANPALQKVL DALDSIKTKG KSTDFPNFDP GSLLPNVLDY WTYPGSLTTP 200
    PLLESVTWIV LKEPISVSSQ QMLKFRTLNF NAEGEPELLM LANWRPAQPL 250
    KNRQVRGFPK 260
    Length:260
    Mass (Da):29,114
    Last modified:January 23, 2007 - v3
    Checksum:iA89412C23FFD19A7
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti57 – 571R → Q in one of the major forms.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY240020 mRNA. Translation: AAO85140.1.
    BC103260 mRNA. Translation: AAI03261.1.
    PIRiA01144. CRBO2.
    RefSeqiNP_848667.1. NM_178572.2.
    UniGeneiBt.49731.

    Genome annotation databases

    GeneIDi280740.
    KEGGibta:280740.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Worthington enzyme manual

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY240020 mRNA. Translation: AAO85140.1 .
    BC103260 mRNA. Translation: AAI03261.1 .
    PIRi A01144. CRBO2.
    RefSeqi NP_848667.1. NM_178572.2.
    UniGenei Bt.49731.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G6V X-ray 3.50 A 1-254 [» ]
    1V9E X-ray 1.95 A/B 2-260 [» ]
    1V9I X-ray 2.95 C 2-260 [» ]
    ProteinModelPortali P00921.
    SMRi P00921. Positions 2-260.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P00921. 1 interaction.

    Chemistry

    BindingDBi P00921.
    ChEMBLi CHEMBL2096971.

    Proteomic databases

    PaxDbi P00921.
    PRIDEi P00921.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 280740.
    KEGGi bta:280740.

    Organism-specific databases

    CTDi 760.

    Phylogenomic databases

    eggNOGi COG3338.
    HOGENOMi HOG000112637.
    HOVERGENi HBG002837.
    InParanoidi P00921.
    KOi K18245.

    Miscellaneous databases

    EvolutionaryTracei P00921.
    NextBioi 20804911.

    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. "Full length cDNA of bovine carbonic anhydrase II."
      Daigle R., Castro I., Desrochers M., Charest P.-M.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Bone marrow.
    2. NIH - Mammalian Gene Collection (MGC) project
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Hypothalamus.
    3. "Primary structure of bovine erythrocyte carbonic carbonic anhydrase CI. II. Complete sequence."
      Sciaky M., Limozin N., Filippi-Foveau D., Gulian J.M., Laurent-Tabusse G.
      Biochimie 58:1071-1082(1976) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-260.
      Tissue: Erythrocyte.
    4. "Genetic independence of two forms of carbonic anhydrase from bovine erythrocytes."
      Gulian J.M., Limozin N., Mallet B., di Costanzo J., Charrel M.
      Biochimie 59:293-302(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    5. "Structure of bovine carbonic anhydrase II at 1.95 A resolution."
      Saito R., Sato T., Ikai A., Tanaka N.
      Acta Crystallogr. D 60:792-795(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION.
    6. "Antigen specificity and high affinity binding provided by one single loop of a camel single-domain antibody."
      Desmyter A., Decanniere K., Muyldermans S., Wyns L.
      J. Biol. Chem. 276:26285-26290(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 1-254 IN COMPLEX WITH ANTIBODY.

    Entry informationi

    Entry nameiCAH2_BOVIN
    AccessioniPrimary (citable) accession number: P00921
    Secondary accession number(s): Q3ZBJ5, Q865Y7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 128 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    One minor and two major forms were isolated chromatographically.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3