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P07451

- CAH3_HUMAN

UniProt

P07451 - CAH3_HUMAN

Protein

Carbonic anhydrase 3

Gene

CA3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 3 (20 Mar 2007)
      Previous versions | rss
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    Functioni

    Reversible hydration of carbon dioxide.

    Catalytic activityi

    H2CO3 = CO2 + H2O.

    Cofactori

    Zinc.

    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)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi94 – 941Zinc; catalytic
    Metal bindingi96 – 961Zinc; catalytic
    Metal bindingi119 – 1191Zinc; catalytic
    Active sitei127 – 1271By similarity

    GO - Molecular functioni

    1. carbonate dehydratase activity Source: ProtInc
    2. nickel cation binding Source: Ensembl
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. bicarbonate transport Source: Reactome
    2. one-carbon metabolic process Source: InterPro
    3. response to ethanol Source: Ensembl
    4. response to oxidative stress Source: Ensembl
    5. 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.

    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
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:1374. CA3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi64 – 641K → H: Enhanced proton transfer in catalysis. 1 Publication
    Mutagenesisi67 – 671R → H: Enhanced proton transfer in catalysis. 1 Publication
    Mutagenesisi197 – 1971F → L: Enhanced activity by at least 10-fold. 1 Publication

    Organism-specific databases

    PharmGKBiPA25990.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 260259Carbonic anhydrase 3PRO_0000077426Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei182 – 1821S-glutathionyl cysteineBy similarity
    Modified residuei187 – 1871S-glutathionyl cysteineBy similarity

    Post-translational modificationi

    S-glutathionylated in hepatocytes under oxidative stress.By similarity

    Keywords - PTMi

    Acetylation, Glutathionylation

    Proteomic databases

    PaxDbiP07451.
    PRIDEiP07451.

    2D gel databases

    UCD-2DPAGEP07451.

    PTM databases

    PhosphoSiteiP07451.

    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

    ArrayExpressiP07451.
    BgeeiP07451.
    CleanExiHS_CA3.
    GenevestigatoriP07451.

    Organism-specific databases

    HPAiCAB004967.
    HPA021775.
    HPA026700.

    Interactioni

    Protein-protein interaction databases

    BioGridi107216. 1 interaction.
    STRINGi9606.ENSP00000285381.

    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
    Helixi35 – 373
    Beta strandi47 – 504
    Helixi53 – 553
    Beta strandi56 – 616
    Beta strandi66 – 705
    Beta strandi73 – 753
    Beta strandi77 – 815
    Beta strandi88 – 9710
    Beta strandi106 – 1094
    Beta strandi115 – 1239
    Helixi125 – 1273
    Helixi130 – 1334
    Beta strandi139 – 15113
    Helixi154 – 1607
    Helixi161 – 1655
    Beta strandi172 – 1743
    Helixi180 – 1834
    Beta strandi190 – 1956
    Beta strandi206 – 2138
    Beta strandi215 – 2173
    Helixi219 – 2257
    Beta strandi229 – 2313
    Beta strandi233 – 2364
    Beta strandi256 – 2583

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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. Positions 2-260.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07451.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni64 – 674Involved in proton transfer
    Regioni198 – 1992Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the alpha-carbonic anhydrase family.Curated

    Phylogenomic databases

    eggNOGiCOG3338.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiP07451.
    KOiK01672.
    OMAiEAPFTHF.
    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:SF96. PTHR18952:SF96. 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

    MAKEWGYASH NGPDHWHELF PNAKGENQSP VELHTKDIRH DPSLQPWSVS    50
    YDGGSAKTIL NNGKTCRVVF DDTYDRSMLR GGPLPGPYRL RQFHLHWGSS 100
    DDHGSEHTVD GVKYAAELHL VHWNPKYNTF KEALKQRDGI AVIGIFLKIG 150
    HENGEFQIFL DALDKIKTKG KEAPFTKFDP SCLFPACRDY WTYQGSFTTP 200
    PCEECIVWLL LKEPMTVSSD QMAKLRSLLS SAENEPPVPL VSNWRPPQPI 250
    NNRVVRASFK 260
    Length:260
    Mass (Da):29,557
    Last modified:March 20, 2007 - v3
    Checksum:iA305334167233FCF
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti31 – 311V → I.3 Publications
    Corresponds to variant rs20571 [ dbSNP | Ensembl ].
    VAR_016180

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    UCSCiuc003ydj.3. human.

    Polymorphism databases

    DMDMi134047703.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS6238.1.
    PIRi A26658. CRHU3.
    RefSeqi NP_005172.1. NM_005181.3.
    UniGenei Hs.82129.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Z93 X-ray 2.10 A 1-260 [» ]
    1Z97 X-ray 2.10 A 1-260 [» ]
    2HFW X-ray 2.50 A 1-259 [» ]
    3UYN X-ray 2.60 A 1-260 [» ]
    3UYQ X-ray 1.70 A 1-260 [» ]
    ProteinModelPortali P07451.
    SMRi P07451. Positions 2-260.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107216. 1 interaction.
    STRINGi 9606.ENSP00000285381.

    Chemistry

    BindingDBi P07451.
    ChEMBLi CHEMBL2885.

    PTM databases

    PhosphoSitei P07451.

    Polymorphism databases

    DMDMi 134047703.

    2D gel databases

    UCD-2DPAGE P07451.

    Proteomic databases

    PaxDbi P07451.
    PRIDEi P07451.

    Protocols and materials databases

    DNASUi 761.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000285381 ; ENSP00000285381 ; ENSG00000164879 .
    GeneIDi 761.
    KEGGi hsa:761.
    UCSCi uc003ydj.3. human.

    Organism-specific databases

    CTDi 761.
    GeneCardsi GC08P086285.
    H-InvDB HIX0078885.
    HGNCi HGNC:1374. CA3.
    HPAi CAB004967.
    HPA021775.
    HPA026700.
    MIMi 114750. gene.
    neXtProti NX_P07451.
    PharmGKBi PA25990.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3338.
    HOGENOMi HOG000112637.
    HOVERGENi HBG002837.
    InParanoidi P07451.
    KOi K01672.
    OMAi EAPFTHF.
    PhylomeDBi P07451.
    TreeFami TF316425.

    Enzyme and pathway databases

    BRENDAi 4.2.1.1. 2681.
    Reactomei REACT_121123. Reversible hydration of carbon dioxide.

    Miscellaneous databases

    EvolutionaryTracei P07451.
    GeneWikii Carbonic_anhydrase_III,_muscle_specific.
    GenomeRNAii 761.
    NextBioi 3078.
    PROi P07451.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07451.
    Bgeei P07451.
    CleanExi HS_CA3.
    Genevestigatori P07451.

    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.
    IPR018441. Carbonic_anhydrase_CA3.
    [Graphical view ]
    PANTHERi PTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF96. PTHR18952:SF96. 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. "Nucleotide sequence and derived amino acid sequence of a cDNA encoding human muscle carbonic anhydrase."
      Lloyd J., McMillan S., Hopkinson D., Edwards Y.H.
      Gene 41:233-239(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Nucleotide sequence, tissue-specific expression, and chromosome location of human carbonic anhydrase III: the human CAIII gene is located on the same chromosome as the closely linked CAI and CAII genes."
      Wade R., Gunning P., Eddy R., Shows T., Kedes L.
      Proc. Natl. Acad. Sci. U.S.A. 83:9571-9575(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-31.
      Tissue: Pericardium and Skeletal muscle.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ILE-31.
    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], VARIANT ILE-31.
      Tissue: Muscle.
    6. "Human muscle carbonic anhydrase: gene structure and DNA methylation patterns in fetal and adult tissues."
      Lloyd J., Brownson C., Tweedie S., Charlton J., Edwards Y.H.
      Genes Dev. 1:594-602(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "Sequence comparisons and functional studies of the proximal promoter of the carbonic anhydrase 3 (CA3) gene."
      Sowden J., Smith H., Morrison K., Edwards Y.
      Gene 214:157-165(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11, DEVELOPMENTAL STAGE.
    8. "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.
    9. "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.
    10. "Crystal structure of human carbonic anhydrase XIII and its complex with the inhibitor acetazolamide."
      Di Fiore A., Monti S.M., Hilvo M., Parkkila S., Romano V., Scaloni A., Pedone C., Scozzafava A., Supuran C.T., De Simone G.
      Proteins 74:164-175(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    11. "Human carbonic anhydrase III: structural and kinetic study of catalysis and proton transfer."
      Duda D.M., Tu C., Fisher S.Z., An H., Yoshioka C., Govindasamy L., Laipis P.J., Agbandje-McKenna M., Silverman D.N., McKenna R.
      Biochemistry 44:10046-10053(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-260 IN COMPLEX WITH ZINC ION, MUTAGENESIS OF PHE-197, ACTIVATION BY IMIDAZOLE AND HISTIDYLHISTIDINE.
    12. "Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase III."
      Elder I., Fisher Z., Laipis P.J., Tu C., McKenna R., Silverman D.N.
      Proteins 68:337-343(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-260 IN COMPLEX WITH ZINC ION, MUTAGENESIS OF LYS-64 AND ARG-67.

    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: October 1, 2014
    This is version 156 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

    External Data

    Dasty 3