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Protein

Carbonic anhydrase 3

Gene

CA3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Reversible hydration of carbon dioxide.

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zn2+2 Publications

Enzyme regulationi

Activated by proton donors such as imidazole and the dipeptide histidylhistidine. Inhibited by coumarins and sulfonamide derivatives such as acetazolamide.3 Publications

Kineticsi

  1. KM=52.0 mM for CO21 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi94Zinc; catalytic2 Publications1
    Metal bindingi96Zinc; catalytic2 Publications1
    Metal bindingi119Zinc; catalytic2 Publications1
    Active sitei127By similarity1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciZFISH:HS09151-MONOMER.
    BRENDAi4.2.1.1. 2681.
    ReactomeiR-HSA-1475029. Reversible hydration of carbon dioxide.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbonic anhydrase 3 (EC:4.2.1.1)
    Alternative name(s):
    Carbonate dehydratase III
    Carbonic anhydrase III
    Short name:
    CA-III
    Gene namesi
    Name:CA3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:1374. CA3.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi64K → H: Enhanced proton transfer in catalysis. 1 Publication1
    Mutagenesisi67R → H: Enhanced proton transfer in catalysis. 1 Publication1
    Mutagenesisi197F → L: Enhanced activity by at least 10-fold. 1 Publication1

    Organism-specific databases

    DisGeNETi761.
    OpenTargetsiENSG00000164879.
    PharmGKBiPA25990.

    Chemistry databases

    ChEMBLiCHEMBL2885.
    DrugBankiDB00819. Acetazolamide.
    DB00909. Zonisamide.

    Polymorphism and mutation databases

    BioMutaiCA3.
    DMDMi134047703.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedBy similarity
    ChainiPRO_00000774262 – 260Carbonic anhydrase 3Add BLAST259

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylalanineBy similarity1
    Modified residuei29PhosphoserineBy similarity1
    Modified residuei43PhosphoserineBy similarity1
    Modified residuei48PhosphoserineBy similarity1
    Modified residuei50PhosphoserineBy similarity1
    Modified residuei55PhosphoserineBy similarity1
    Modified residuei73PhosphothreonineBy similarity1
    Modified residuei127PhosphotyrosineBy similarity1
    Modified residuei129PhosphothreonineBy similarity1
    Modified residuei176PhosphothreonineBy similarity1
    Modified residuei182S-glutathionyl cysteineBy similarity1
    Modified residuei187S-glutathionyl cysteineBy similarity1
    Modified residuei216PhosphothreonineBy similarity1
    Modified residuei219PhosphoserineBy similarity1

    Post-translational modificationi

    S-glutathionylated in hepatocytes under oxidative stress.By similarity

    Keywords - PTMi

    Acetylation, Glutathionylation, Phosphoprotein

    Proteomic databases

    EPDiP07451.
    PaxDbiP07451.
    PeptideAtlasiP07451.
    PRIDEiP07451.

    2D gel databases

    UCD-2DPAGEP07451.

    PTM databases

    iPTMnetiP07451.
    PhosphoSitePlusiP07451.

    Expressioni

    Tissue specificityi

    Muscle specific.

    Developmental stagei

    At 6 weeks gestation, transcripts accumulate at low levels in the somites and at high levels throughout the notochord. As gestation continues, CA3 becomes abundant in all developing muscle masses and continues at high to moderate levels in the notochord.1 Publication

    Gene expression databases

    BgeeiENSG00000164879.
    CleanExiHS_CA3.
    ExpressionAtlasiP07451. baseline and differential.
    GenevisibleiP07451. HS.

    Organism-specific databases

    HPAiCAB004967.
    HPA021775.
    HPA026700.

    Interactioni

    Protein-protein interaction databases

    BioGridi107216. 2 interactors.
    IntActiP07451. 1 interactor.
    STRINGi9606.ENSP00000285381.

    Chemistry databases

    BindingDBiP07451.

    Structurei

    Secondary structure

    1260
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Turni9 – 11Combined sources3
    Turni13 – 15Combined sources3
    Helixi16 – 18Combined sources3
    Helixi21 – 24Combined sources4
    Beta strandi25 – 27Combined sources3
    Helixi35 – 37Combined sources3
    Beta strandi47 – 50Combined sources4
    Helixi53 – 55Combined sources3
    Beta strandi56 – 61Combined sources6
    Beta strandi66 – 70Combined sources5
    Beta strandi73 – 75Combined sources3
    Beta strandi77 – 81Combined sources5
    Beta strandi88 – 97Combined sources10
    Beta strandi106 – 109Combined sources4
    Beta strandi115 – 123Combined sources9
    Helixi125 – 127Combined sources3
    Helixi130 – 133Combined sources4
    Beta strandi139 – 151Combined sources13
    Helixi154 – 160Combined sources7
    Helixi161 – 165Combined sources5
    Beta strandi172 – 174Combined sources3
    Helixi180 – 183Combined sources4
    Beta strandi190 – 195Combined sources6
    Beta strandi206 – 213Combined sources8
    Beta strandi215 – 217Combined sources3
    Helixi219 – 225Combined sources7
    Beta strandi229 – 231Combined sources3
    Beta strandi233 – 236Combined sources4
    Beta strandi256 – 258Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1Z93X-ray2.10A1-260[»]
    1Z97X-ray2.10A1-260[»]
    2HFWX-ray2.50A1-259[»]
    3UYNX-ray2.60A1-260[»]
    3UYQX-ray1.70A1-260[»]
    ProteinModelPortaliP07451.
    SMRiP07451.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07451.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini3 – 259Alpha-carbonic anhydrasePROSITE-ProRule annotationAdd BLAST257

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni64 – 67Involved in proton transfer4
    Regioni198 – 199Substrate bindingBy similarity2

    Sequence similaritiesi

    Belongs to the alpha-carbonic anhydrase family.Curated
    Contains 1 alpha-carbonic anhydrase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiKOG0382. Eukaryota.
    COG3338. LUCA.
    GeneTreeiENSGT00760000118915.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiP07451.
    KOiK01672.
    OMAiKQRDGIA.
    OrthoDBiEOG091G0XFM.
    PhylomeDBiP07451.
    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.
    IPR018441. Carbonic_anhydrase_CA3.
    [Graphical view]
    PANTHERiPTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF127. PTHR18952:SF127. 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.

    P07451-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAKEWGYASH NGPDHWHELF PNAKGENQSP VELHTKDIRH DPSLQPWSVS
    60 70 80 90 100
    YDGGSAKTIL NNGKTCRVVF DDTYDRSMLR GGPLPGPYRL RQFHLHWGSS
    110 120 130 140 150
    DDHGSEHTVD GVKYAAELHL VHWNPKYNTF KEALKQRDGI AVIGIFLKIG
    160 170 180 190 200
    HENGEFQIFL DALDKIKTKG KEAPFTKFDP SCLFPACRDY WTYQGSFTTP
    210 220 230 240 250
    PCEECIVWLL LKEPMTVSSD QMAKLRSLLS SAENEPPVPL VSNWRPPQPI
    260
    NNRVVRASFK
    Length:260
    Mass (Da):29,557
    Last modified:March 20, 2007 - v3
    Checksum:iA305334167233FCF
    GO

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_01618031V → I.3 PublicationsCorresponds to variant rs20571dbSNPEnsembl.1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M29458 Genomic DNA. Translation: AAA52293.1.
    M29452 Genomic DNA. No translation available.
    AK096880 mRNA. Translation: BAG53390.1.
    AK313254 mRNA. Translation: BAG36064.1.
    CH471068 Genomic DNA. Translation: EAW87133.1.
    BC004897 mRNA. Translation: AAH04897.1.
    AJ006473 Genomic DNA. Translation: CAA07056.1.
    CCDSiCCDS6238.1.
    PIRiA26658. CRHU3.
    RefSeqiNP_005172.1. NM_005181.3.
    UniGeneiHs.82129.

    Genome annotation databases

    EnsembliENST00000285381; ENSP00000285381; ENSG00000164879.
    GeneIDi761.
    KEGGihsa:761.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M29458 Genomic DNA. Translation: AAA52293.1.
    M29452 Genomic DNA. No translation available.
    AK096880 mRNA. Translation: BAG53390.1.
    AK313254 mRNA. Translation: BAG36064.1.
    CH471068 Genomic DNA. Translation: EAW87133.1.
    BC004897 mRNA. Translation: AAH04897.1.
    AJ006473 Genomic DNA. Translation: CAA07056.1.
    CCDSiCCDS6238.1.
    PIRiA26658. CRHU3.
    RefSeqiNP_005172.1. NM_005181.3.
    UniGeneiHs.82129.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1Z93X-ray2.10A1-260[»]
    1Z97X-ray2.10A1-260[»]
    2HFWX-ray2.50A1-259[»]
    3UYNX-ray2.60A1-260[»]
    3UYQX-ray1.70A1-260[»]
    ProteinModelPortaliP07451.
    SMRiP07451.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi107216. 2 interactors.
    IntActiP07451. 1 interactor.
    STRINGi9606.ENSP00000285381.

    Chemistry databases

    BindingDBiP07451.
    ChEMBLiCHEMBL2885.
    DrugBankiDB00819. Acetazolamide.
    DB00909. Zonisamide.

    PTM databases

    iPTMnetiP07451.
    PhosphoSitePlusiP07451.

    Polymorphism and mutation databases

    BioMutaiCA3.
    DMDMi134047703.

    2D gel databases

    UCD-2DPAGEP07451.

    Proteomic databases

    EPDiP07451.
    PaxDbiP07451.
    PeptideAtlasiP07451.
    PRIDEiP07451.

    Protocols and materials databases

    DNASUi761.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000285381; ENSP00000285381; ENSG00000164879.
    GeneIDi761.
    KEGGihsa:761.

    Organism-specific databases

    CTDi761.
    DisGeNETi761.
    GeneCardsiCA3.
    H-InvDBHIX0078885.
    HGNCiHGNC:1374. CA3.
    HPAiCAB004967.
    HPA021775.
    HPA026700.
    MIMi114750. gene.
    neXtProtiNX_P07451.
    OpenTargetsiENSG00000164879.
    PharmGKBiPA25990.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG0382. Eukaryota.
    COG3338. LUCA.
    GeneTreeiENSGT00760000118915.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiP07451.
    KOiK01672.
    OMAiKQRDGIA.
    OrthoDBiEOG091G0XFM.
    PhylomeDBiP07451.
    TreeFamiTF316425.

    Enzyme and pathway databases

    BioCyciZFISH:HS09151-MONOMER.
    BRENDAi4.2.1.1. 2681.
    ReactomeiR-HSA-1475029. Reversible hydration of carbon dioxide.

    Miscellaneous databases

    EvolutionaryTraceiP07451.
    GeneWikiiCarbonic_anhydrase_III,_muscle_specific.
    GenomeRNAii761.
    PROiP07451.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000164879.
    CleanExiHS_CA3.
    ExpressionAtlasiP07451. baseline and differential.
    GenevisibleiP07451. HS.

    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.
    IPR018441. Carbonic_anhydrase_CA3.
    [Graphical view]
    PANTHERiPTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF127. PTHR18952:SF127. 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...

    Entry informationi

    Entry nameiCAH3_HUMAN
    AccessioniPrimary (citable) accession number: P07451
    Secondary accession number(s): B2R867, B3KUC8, O60842
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: March 20, 2007
    Last modified: November 30, 2016
    This is version 176 of the entry and version 3 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 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    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 one 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.