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P07630

- CAH2_CHICK

UniProt

P07630 - CAH2_CHICK

Protein

Carbonic anhydrase 2

Gene

CA2

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript 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: Ensembl

    GO - Biological processi

    1. angiotensin-activated signaling pathway Source: Ensembl
    2. carbon dioxide transport Source: Ensembl
    3. morphogenesis of an epithelium Source: Ensembl
    4. one-carbon metabolic process Source: InterPro
    5. positive regulation of dipeptide transmembrane transport Source: Ensembl
    6. regulation of anion transport Source: Ensembl
    7. regulation of intracellular pH Source: Ensembl
    8. secretion Source: Ensembl

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_197145. Erythrocytes take up carbon dioxide and release oxygen.
    REACT_197148. Reversible hydration of carbon dioxide.
    REACT_197150. 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
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Chromosome 2

    Subcellular locationi

    Cytoplasm. Cell membrane By similarity

    GO - Cellular componenti

    1. apical part of cell Source: Ensembl
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: Ensembl
    4. 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_0000077423Add
    BLAST

    Proteomic databases

    PaxDbiP07630.
    PRIDEiP07630.

    Interactioni

    Protein-protein interaction databases

    STRINGi9031.ENSGALP00000025525.

    Structurei

    Secondary structure

    1
    260
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni8 – 103
    Turni12 – 143
    Helixi15 – 184
    Helixi20 – 234
    Turni34 – 363
    Beta strandi37 – 393
    Beta strandi46 – 494
    Beta strandi55 – 606
    Beta strandi65 – 695
    Beta strandi72 – 809
    Beta strandi87 – 9610
    Beta strandi105 – 1084
    Beta strandi114 – 12310
    Helixi124 – 1263
    Helixi129 – 1324
    Beta strandi138 – 15013
    Helixi153 – 1553
    Helixi156 – 1616
    Turni162 – 1654
    Beta strandi171 – 1733
    Helixi179 – 1824
    Beta strandi189 – 1946
    Beta strandi205 – 2128
    Beta strandi214 – 2163
    Helixi218 – 2247
    Beta strandi228 – 2303
    Beta strandi255 – 2573

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Q4Imodel-A1-260[»]
    ProteinModelPortaliP07630.
    SMRiP07630. 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.
    InParanoidiP07630.
    KOiK18245.
    OMAiNDENESH.
    OrthoDBiEOG7WMCK7.
    PhylomeDBiP07630.
    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.

    P07630-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSHHWGYDSH NGPAHWHEHF PIANGERQSP IAISTKAARY DPALKPLSFS    50
    YDAGTAKAIV NNGHSFNVEF DDSSDKSVLQ GGALDGVYRL VQFHIHWGSC 100
    EGQGSEHTVD GVKYDAELHI VHWNVKYGKF AEALKHPDGL AVVGIFMKVG 150
    NAKPEIQKVV DALNSIQTKG KQASFTNFDP TGLLPPCRDY WTYPGSLTTP 200
    PLHECVIWHV LKEPITVSSE QMCKLRGLCF SAENEPVCRM VDNWRPCQPL 250
    KSREVRASFQ 260
    Length:260
    Mass (Da):29,008
    Last modified:January 23, 2007 - v3
    Checksum:i6723309BC77A4950
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51W → L in CAA28501. (PubMed:3102231)Curated
    Sequence conflicti8 – 81D → G in AAA48646. (PubMed:6331256)Curated
    Sequence conflicti87 – 871V → S in AAA48646. (PubMed:6331256)Curated
    Sequence conflicti250 – 2501L → V in CAA31175. (PubMed:3029691)Curated
    Sequence conflicti250 – 2501L → V in CAA29417. (PubMed:3029691)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z14957 mRNA. Translation: CAA78681.1.
    X12639 mRNA. Translation: CAA31175.1.
    X06000
    , X06001, X06002, X06003, X06004, X06005 Genomic DNA. Translation: CAA29417.1.
    X04810 mRNA. Translation: CAA28501.1.
    X17378 mRNA. Translation: CAA35250.1.
    M25943 mRNA. Translation: AAA48646.1.
    PIRiJC2580.
    RefSeqiNP_990648.1. NM_205317.1.
    UniGeneiGga.3986.

    Genome annotation databases

    EnsembliENSGALT00000025572; ENSGALP00000025525; ENSGALG00000015862.
    GeneIDi396257.
    KEGGigga:396257.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z14957 mRNA. Translation: CAA78681.1 .
    X12639 mRNA. Translation: CAA31175.1 .
    X06000
    , X06001 , X06002 , X06003 , X06004 , X06005 Genomic DNA. Translation: CAA29417.1 .
    X04810 mRNA. Translation: CAA28501.1 .
    X17378 mRNA. Translation: CAA35250.1 .
    M25943 mRNA. Translation: AAA48646.1 .
    PIRi JC2580.
    RefSeqi NP_990648.1. NM_205317.1.
    UniGenei Gga.3986.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Q4I model - A 1-260 [» ]
    ProteinModelPortali P07630.
    SMRi P07630. Positions 2-260.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9031.ENSGALP00000025525.

    Proteomic databases

    PaxDbi P07630.
    PRIDEi P07630.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSGALT00000025572 ; ENSGALP00000025525 ; ENSGALG00000015862 .
    GeneIDi 396257.
    KEGGi gga:396257.

    Organism-specific databases

    CTDi 760.

    Phylogenomic databases

    eggNOGi COG3338.
    GeneTreei ENSGT00750000117305.
    HOGENOMi HOG000112637.
    HOVERGENi HBG002837.
    InParanoidi P07630.
    KOi K18245.
    OMAi NDENESH.
    OrthoDBi EOG7WMCK7.
    PhylomeDBi P07630.
    TreeFami TF316425.

    Enzyme and pathway databases

    Reactomei REACT_197145. Erythrocytes take up carbon dioxide and release oxygen.
    REACT_197148. Reversible hydration of carbon dioxide.
    REACT_197150. Erythrocytes take up oxygen and release carbon dioxide.

    Miscellaneous databases

    NextBioi 20816309.
    PROi P07630.

    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. "A novel carbonic anhydrase II mRNA isolated from mature chicken testis displays a TATA box and other promoter sequences in a leader 5' untranslated region not present in somatic tissues."
      Mezquita J., Pau M., Mezquita C.
      Gene 147:231-235(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Hubbard White Mountain.
      Tissue: Testis.
    2. "The chicken carbonic anhydrase II gene: evidence for a recent shift in intron position."
      Yoshihara C.M., Lee J.-D., Dodgson J.B.
      Nucleic Acids Res. 15:753-770(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Strain: White leghorn.
    3. "Sequence of carbonic anhydrase II cDNA from chick retina."
      Rogers J.H.
      Eur. J. Biochem. 162:119-122(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-260.
      Strain: White leghorn.
      Tissue: Retina.
    4. "Utilization of the second polyadenylation signal at the 3' end of the chicken carbonic anhydrase II gene."
      Godbout R., Andison R., Upton C., Day R.
      Nucleic Acids Res. 18:1049-1049(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 222-260.
      Tissue: Retina.
    5. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-87.

    Entry informationi

    Entry nameiCAH2_CHICK
    AccessioniPrimary (citable) accession number: P07630
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    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

    Keywords - Technical termi

    3D-structure, Complete proteome, 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