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P43166

- CAH7_HUMAN

UniProt

P43166 - CAH7_HUMAN

Protein

Carbonic anhydrase 7

Gene

CA7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Reversible hydration of carbon dioxide.

    Catalytic activityi

    H2CO3 = CO2 + H2O.

    Cofactori

    Zinc.

    Enzyme regulationi

    Activated by histamine, L-adrenaline, L- and D-histidine, and L- and D-phenylalanine. Inhibited coumarins, sulfonamide derivatives such as acetazolamide (AZA), by saccharin and Foscarnet (phosphonoformate trisodium salt).7 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei66 – 661Proton acceptorBy similarity
    Metal bindingi96 – 961Zinc; catalytic
    Metal bindingi98 – 981Zinc; catalytic
    Metal bindingi121 – 1211Zinc; catalytic
    Active sitei130 – 1301By similarity

    GO - Molecular functioni

    1. carbonate dehydratase activity Source: ProtInc
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. bicarbonate transport Source: Reactome
    2. one-carbon metabolic process Source: InterPro
    3. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi4.2.1.1. 2681.
    ReactomeiREACT_121123. Reversible hydration of carbon dioxide.
    SABIO-RKP43166.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbonic anhydrase 7 (EC:4.2.1.1)
    Alternative name(s):
    Carbonate dehydratase VII
    Carbonic anhydrase VII
    Short name:
    CA-VII
    Gene namesi
    Name:CA7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:1381. CA7.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25996.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 264264Carbonic anhydrase 7PRO_0000077431Add
    BLAST

    Proteomic databases

    PaxDbiP43166.
    PRIDEiP43166.

    PTM databases

    PhosphoSiteiP43166.

    Expressioni

    Gene expression databases

    ArrayExpressiP43166.
    BgeeiP43166.
    CleanExiHS_CA7.
    GenevestigatoriP43166.

    Organism-specific databases

    HPAiHPA047237.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000345659.

    Structurei

    Secondary structure

    1
    264
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni11 – 133
    Helixi15 – 173
    Helixi18 – 214
    Helixi23 – 264
    Beta strandi27 – 293
    Helixi37 – 393
    Beta strandi40 – 423
    Beta strandi46 – 527
    Beta strandi58 – 636
    Beta strandi68 – 725
    Beta strandi75 – 8410
    Beta strandi90 – 9910
    Beta strandi108 – 1114
    Beta strandi117 – 1259
    Turni127 – 1293
    Helixi133 – 1364
    Beta strandi142 – 15413
    Helixi157 – 1648
    Turni165 – 1695
    Beta strandi174 – 1774
    Helixi183 – 1864
    Beta strandi193 – 1986
    Beta strandi209 – 2168
    Beta strandi218 – 2203
    Helixi222 – 2298
    Beta strandi232 – 2343
    Beta strandi259 – 2624

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3MDZX-ray2.32A5-262[»]
    3ML5X-ray2.05A1-264[»]
    ProteinModelPortaliP43166.
    SMRiP43166. Positions 5-262.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni201 – 2022Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the alpha-carbonic anhydrase family.Curated

    Phylogenomic databases

    eggNOGiCOG3338.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiP43166.
    KOiK01672.
    OMAiLVHWNAR.
    OrthoDBiEOG7WMCK7.
    PhylomeDBiP43166.
    TreeFamiTF316425.

    Family and domain databases

    Gene3Di3.10.200.10. 1 hit.
    InterProiIPR001148. Carbonic_anhydrase_a.
    IPR023561. Carbonic_anhydrase_a-class.
    IPR018338. Carbonic_anhydrase_a-class_CS.
    IPR018438. Carbonic_anhydrase_CA7.
    [Graphical view]
    PANTHERiPTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF26. PTHR18952:SF26. 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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P43166-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MTGHHGWGYG QDDGPSHWHK LYPIAQGDRQ SPINIISSQA VYSPSLQPLE    50
    LSYEACMSLS ITNNGHSVQV DFNDSDDRTV VTGGPLEGPY RLKQFHFHWG 100
    KKHDVGSEHT VDGKSFPSEL HLVHWNAKKY STFGEAASAP DGLAVVGVFL 150
    ETGDEHPSMN RLTDALYMVR FKGTKAQFSC FNPKCLLPAS RHYWTYPGSL 200
    TTPPLSESVT WIVLREPICI SERQMGKFRS LLFTSEDDER IHMVNNFRPP 250
    QPLKGRVVKA SFRA 264
    Length:264
    Mass (Da):29,658
    Last modified:November 1, 1995 - v1
    Checksum:i7AD559FC6E07EF96
    GO
    Isoform 2 (identifier: P43166-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-56: Missing.

    Show »
    Length:208
    Mass (Da):23,452
    Checksum:iAF3D016A27182D18
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5656Missing in isoform 2. 1 PublicationVSP_044254Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M76423
    , M76420, M76421, M76422 Genomic DNA. Translation: AAA51923.1.
    AY075019 mRNA. Translation: AAL78167.1.
    AY075020 mRNA. Translation: AAL78168.1.
    AC004638 Genomic DNA. Translation: AAC23785.1.
    AC044802 Genomic DNA. No translation available.
    CH471092 Genomic DNA. Translation: EAW83047.1.
    BC033865 mRNA. Translation: AAH33865.1.
    CCDSiCCDS10821.1. [P43166-1]
    CCDS42173.1. [P43166-2]
    PIRiA55272. CRHU7.
    RefSeqiNP_001014435.1. NM_001014435.1. [P43166-2]
    NP_005173.1. NM_005182.2. [P43166-1]
    XP_005256193.1. XM_005256136.1. [P43166-2]
    UniGeneiHs.37014.

    Genome annotation databases

    EnsembliENST00000338437; ENSP00000345659; ENSG00000168748. [P43166-1]
    ENST00000394069; ENSP00000377632; ENSG00000168748. [P43166-2]
    GeneIDi766.
    KEGGihsa:766.
    UCSCiuc002eqi.3. human. [P43166-1]

    Polymorphism databases

    DMDMi1168744.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M76423
    , M76420 , M76421 , M76422 Genomic DNA. Translation: AAA51923.1 .
    AY075019 mRNA. Translation: AAL78167.1 .
    AY075020 mRNA. Translation: AAL78168.1 .
    AC004638 Genomic DNA. Translation: AAC23785.1 .
    AC044802 Genomic DNA. No translation available.
    CH471092 Genomic DNA. Translation: EAW83047.1 .
    BC033865 mRNA. Translation: AAH33865.1 .
    CCDSi CCDS10821.1. [P43166-1 ]
    CCDS42173.1. [P43166-2 ]
    PIRi A55272. CRHU7.
    RefSeqi NP_001014435.1. NM_001014435.1. [P43166-2 ]
    NP_005173.1. NM_005182.2. [P43166-1 ]
    XP_005256193.1. XM_005256136.1. [P43166-2 ]
    UniGenei Hs.37014.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3MDZ X-ray 2.32 A 5-262 [» ]
    3ML5 X-ray 2.05 A 1-264 [» ]
    ProteinModelPortali P43166.
    SMRi P43166. Positions 5-262.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000345659.

    Chemistry

    BindingDBi P43166.
    ChEMBLi CHEMBL2326.
    GuidetoPHARMACOLOGYi 2749.

    PTM databases

    PhosphoSitei P43166.

    Polymorphism databases

    DMDMi 1168744.

    Proteomic databases

    PaxDbi P43166.
    PRIDEi P43166.

    Protocols and materials databases

    DNASUi 766.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000338437 ; ENSP00000345659 ; ENSG00000168748 . [P43166-1 ]
    ENST00000394069 ; ENSP00000377632 ; ENSG00000168748 . [P43166-2 ]
    GeneIDi 766.
    KEGGi hsa:766.
    UCSCi uc002eqi.3. human. [P43166-1 ]

    Organism-specific databases

    CTDi 766.
    GeneCardsi GC16P066880.
    HGNCi HGNC:1381. CA7.
    HPAi HPA047237.
    MIMi 114770. gene.
    neXtProti NX_P43166.
    PharmGKBi PA25996.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3338.
    HOGENOMi HOG000112637.
    HOVERGENi HBG002837.
    InParanoidi P43166.
    KOi K01672.
    OMAi LVHWNAR.
    OrthoDBi EOG7WMCK7.
    PhylomeDBi P43166.
    TreeFami TF316425.

    Enzyme and pathway databases

    BRENDAi 4.2.1.1. 2681.
    Reactomei REACT_121123. Reversible hydration of carbon dioxide.
    SABIO-RK P43166.

    Miscellaneous databases

    GeneWikii Carbonic_anhydrase_7.
    GenomeRNAii 766.
    NextBioi 3096.
    PROi P43166.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P43166.
    Bgeei P43166.
    CleanExi HS_CA7.
    Genevestigatori P43166.

    Family and domain databases

    Gene3Di 3.10.200.10. 1 hit.
    InterProi IPR001148. Carbonic_anhydrase_a.
    IPR023561. Carbonic_anhydrase_a-class.
    IPR018338. Carbonic_anhydrase_a-class_CS.
    IPR018438. Carbonic_anhydrase_CA7.
    [Graphical view ]
    PANTHERi PTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF26. PTHR18952:SF26. 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. "Characterization of the human gene for a newly discovered carbonic anhydrase, CA VII, and its localization to chromosome 16."
      Montgomery J.C., Venta P.J., Eddy R.L., Fukushima Y.S., Shows T.B., Tashian R.E.
      Genomics 11:835-848(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    2. "Molecular identification of carbonic anhydrases (CA) and CA-related (CAR) genes."
      Chen Y., Huang C.-H.
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1).
      Tissue: Colon, Kidney and Stomach.
    6. "Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and crystallographic analysis of their adducts with isoform II: engineering proton-transfer processes within the active site of an enzyme."
      Temperini C., Scozzafava A., Vullo D., Supuran C.T.
      Chemistry 12:7057-7066(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    7. "Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII, and XIV with L- and D-phenylalanine and crystallographic analysis of their adducts with isozyme II: stereospecific recognition within the active site of an enzyme and its consequences for the drug design."
      Temperini C., Scozzafava A., Vullo D., Supuran C.T.
      J. Med. Chem. 49:3019-3027(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    8. "Saccharin inhibits carbonic anhydrases: possible explanation for its unpleasant metallic aftertaste."
      Koehler K., Hillebrecht A., Schulze Wischeler J., Innocenti A., Heine A., Supuran C.T., Klebe G.
      Angew. Chem. Int. Ed. Engl. 46:7697-7699(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    9. "Carbonic anhydrase activators: L-Adrenaline plugs the active site entrance of isozyme II, activating better isoforms I, IV, VA, VII, and XIV."
      Temperini C., Innocenti A., Scozzafava A., Mastrolorenzo A., Supuran C.T.
      Bioorg. Med. Chem. Lett. 17:628-635(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    10. "Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-ray crystal structure of the antiviral drug foscarnet complexed to human carbonic anhydrase I."
      Temperini C., Innocenti A., Guerri A., Scozzafava A., Rusconi S., Supuran C.T.
      Bioorg. Med. Chem. Lett. 17:2210-2215(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    11. "A thiabendazole sulfonamide shows potent inhibitory activity against mammalian and nematode alpha-carbonic anhydrases."
      Crocetti L., Maresca A., Temperini C., Hall R.A., Scozzafava A., Muehlschlegel F.A., Supuran C.T.
      Bioorg. Med. Chem. Lett. 19:1371-1375(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    12. "Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new class of suicide inhibitors."
      Maresca A., Temperini C., Vu H., Pham N.B., Poulsen S.-A., Scozzafava A., Quinn R.J., Supuran C.T.
      J. Am. Chem. Soc. 131:3057-3062(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    13. "Crystal structure of human carbonic anhydrase VII [isoform 1], CA7."
      Structural genomics consortium (SGC)
      Submitted (JUN-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 5-262 IN COMPLEX WITH ZINC IONS.

    Entry informationi

    Entry nameiCAH7_HUMAN
    AccessioniPrimary (citable) accession number: P43166
    Secondary accession number(s): Q541F0, Q86YU0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 127 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3