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Protein

Carbonic anhydrase 1

Gene

CA1

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. Can hydrates cyanamide to urea.1 Publication

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zn2+10 Publications

Enzyme regulationi

Activated by histamine, imidazole, L-adrenaline, L- and D-histidine, and L- and D-phenylalanine. Inhibited by coumarins, sulfonamide derivatives such as acetazolamide, benzenesulfonamide and derivatives (4-carboxyethylbenzene-sulfonamide, 4-carboxyethylbenzene-sulfonamide ethyl ester, 4-(acetyl-2-aminoethyl)benzene-sulfonamide, 4-aminoethylbenzene-sulfonamide), and 'prong inhibitors' BR15, BR17, BR22 and BR30. Activated by a short exposition to Foscarnet (phosphonoformate trisodium salt), but inhibited by a long one. Esterase activity weakly reduced by cyanamide.9 Publications

Kineticsi

  1. KM=4.0 mM for CO22 Publications
  2. KM=15 mM for 4-nitrophenyl acetate2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei65Proton acceptorPROSITE-ProRule annotation1
    Metal bindingi65Zinc 2; in variant Michigan-11 Publication1
    Metal bindingi68Zinc 2; in variant Michigan-11 Publication1
    Metal bindingi95Zinc 1; catalytic10 Publications1
    Metal bindingi97Zinc 1; catalytic10 Publications1
    Metal bindingi120Zinc 1; catalytic10 Publications1
    Active sitei129By similarity1
    Binding sitei200Substrate1 Publication1
    Metal bindingi201Zinc 2; in variant Michigan-11 Publication1

    GO - Molecular functioni

    • arylesterase activity Source: CACAO
    • carbonate dehydratase activity Source: CACAO
    • hydro-lyase activity Source: CACAO
    • zinc ion binding Source: InterPro

    GO - Biological processi

    Keywordsi

    Molecular functionLyase
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi4.2.1.1. 2681.
    ReactomeiR-HSA-1237044. Erythrocytes take up carbon dioxide and release oxygen.
    R-HSA-1247673. Erythrocytes take up oxygen and release carbon dioxide.
    R-HSA-1475029. Reversible hydration of carbon dioxide.
    R-HSA-8950505. Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
    SABIO-RKiP00915.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbonic anhydrase 1 (EC:4.2.1.1)
    Alternative name(s):
    Carbonate dehydratase I
    Carbonic anhydrase B
    Short name:
    CAB
    Carbonic anhydrase I
    Short name:
    CA-I
    Gene namesi
    Name:CA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 8

    Organism-specific databases

    EuPathDBiHostDB:ENSG00000133742.13.
    HGNCiHGNC:1368. CA1.

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    DisGeNETi759.
    OpenTargetsiENSG00000133742.
    PharmGKBiPA25984.

    Chemistry databases

    ChEMBLiCHEMBL261.
    DrugBankiDB08156. 3-[4-(AMINOSULFONYL)PHENYL]PROPANOIC ACID.
    DB00819. Acetazolamide.
    DB00381. Amlodipine.
    DB00436. Bendroflumethiazide.
    DB00562. Benzthiazide.
    DB01194. Brinzolamide.
    DB00880. Chlorothiazide.
    DB00606. Cyclothiazide.
    DB01119. Diazoxide.
    DB01144. Diclofenamide.
    DB00869. Dorzolamide.
    DB08846. Ellagic Acid.
    DB01031. Ethinamate.
    DB00311. Ethoxzolamide.
    DB08157. ETHYL 3-[4-(AMINOSULFONYL)PHENYL]PROPANOATE.
    DB00999. Hydrochlorothiazide.
    DB00774. Hydroflumethiazide.
    DB00703. Methazolamide.
    DB00423. Methocarbamol.
    DB00232. Methyclothiazide.
    DB08155. N-{2-[4-(AMINOSULFONYL)PHENYL]ETHYL}ACETAMIDE.
    DB01325. Quinethazone.
    DB09460. Sodium carbonate.
    DB01021. Trichlormethiazide.
    DB00909. Zonisamide.
    GuidetoPHARMACOLOGYi2597.

    Polymorphism and mutation databases

    BioMutaiCA1.
    DMDMi115449.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00000774092 – 261Carbonic anhydrase 1Add BLAST260

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylalanine2 Publications1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP00915.
    PeptideAtlasiP00915.
    PRIDEiP00915.
    TopDownProteomicsiP00915.

    2D gel databases

    DOSAC-COBS-2DPAGEiP00915.
    REPRODUCTION-2DPAGEiIPI00215983.
    P00915.
    UCD-2DPAGEiP00915.

    PTM databases

    iPTMnetiP00915.
    PhosphoSitePlusiP00915.

    Expressioni

    Gene expression databases

    BgeeiENSG00000133742.
    CleanExiHS_CA1.
    ExpressionAtlasiP00915. baseline and differential.
    GenevisibleiP00915. HS.

    Organism-specific databases

    HPAiCAB025790.
    HPA006558.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TFCP2Q128006EBI-3912102,EBI-717422

    Protein-protein interaction databases

    BioGridi107214. 4 interactors.
    IntActiP00915. 4 interactors.
    STRINGi9606.ENSP00000256119.

    Chemistry databases

    BindingDBiP00915.

    Structurei

    Secondary structure

    1261
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Turni10 – 12Combined sources3
    Helixi14 – 19Combined sources6
    Helixi22 – 25Combined sources4
    Beta strandi26 – 28Combined sources3
    Beta strandi32 – 34Combined sources3
    Helixi36 – 38Combined sources3
    Beta strandi48 – 51Combined sources4
    Helixi54 – 56Combined sources3
    Beta strandi57 – 62Combined sources6
    Beta strandi67 – 71Combined sources5
    Beta strandi74 – 82Combined sources9
    Beta strandi89 – 98Combined sources10
    Beta strandi100 – 104Combined sources5
    Beta strandi107 – 110Combined sources4
    Beta strandi116 – 125Combined sources10
    Turni126 – 128Combined sources3
    Helixi132 – 135Combined sources4
    Beta strandi141 – 153Combined sources13
    Helixi156 – 158Combined sources3
    Helixi159 – 164Combined sources6
    Helixi165 – 167Combined sources3
    Beta strandi174 – 176Combined sources3
    Helixi182 – 185Combined sources4
    Beta strandi192 – 197Combined sources6
    Beta strandi208 – 215Combined sources8
    Beta strandi217 – 219Combined sources3
    Helixi221 – 228Combined sources8
    Beta strandi230 – 233Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1AZMX-ray2.00A2-261[»]
    1BZMX-ray2.00A2-261[»]
    1CRMX-ray2.00A2-261[»]
    1CZMX-ray2.00A2-261[»]
    1HCBX-ray1.60A2-261[»]
    1HUGX-ray2.00A2-261[»]
    1HUHX-ray2.20A2-261[»]
    1J9WX-ray2.60A/B2-261[»]
    1JV0X-ray2.00A/B2-261[»]
    2CABX-ray2.00A2-261[»]
    2FOYX-ray1.55A/B2-261[»]
    2FW4X-ray2.00A/B2-261[»]
    2IT4X-ray2.00A/B6-261[»]
    2NMXX-ray1.55A/B2-261[»]
    2NN1X-ray1.65A/B2-261[»]
    2NN7X-ray1.85A/B2-261[»]
    3LXEX-ray1.90A/B2-261[»]
    3W6HX-ray2.96A/B2-261[»]
    3W6IX-ray2.69A/E2-261[»]
    4WR7X-ray1.50A/B3-261[»]
    4WUPX-ray1.75A/B3-261[»]
    4WUQX-ray1.75A/B3-261[»]
    5E2MX-ray1.41A/B3-261[»]
    5GMMX-ray2.00A/B1-261[»]
    ProteinModelPortaliP00915.
    SMRiP00915.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00915.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini4 – 261Alpha-carbonic anhydrasePROSITE-ProRule annotationAdd BLAST258

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni200 – 201Substrate bindingBy similarity2

    Sequence similaritiesi

    Belongs to the alpha-carbonic anhydrase family.Curated

    Phylogenomic databases

    eggNOGiKOG0382. Eukaryota.
    COG3338. LUCA.
    GeneTreeiENSGT00760000118915.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiP00915.
    KOiK01672.
    OMAiVTWIICK.
    OrthoDBiEOG091G0XFM.
    PhylomeDBiP00915.
    TreeFamiTF316425.

    Family and domain databases

    Gene3Di3.10.200.10. 1 hit.
    InterProiView protein in InterPro
    IPR001148. Carbonic_anhydrase_a.
    IPR023561. Carbonic_anhydrase_a-class.
    IPR018338. Carbonic_anhydrase_a-class_CS.
    IPR036398. Carbonic_anhydrase_a_sf.
    IPR018442. Carbonic_anhydrase_CA1.
    PANTHERiPTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF82. PTHR18952:SF82. 1 hit.
    PfamiView protein in Pfam
    PF00194. Carb_anhydrase. 1 hit.
    SMARTiView protein in SMART
    SM01057. Carb_anhydrase. 1 hit.
    SUPFAMiSSF51069. SSF51069. 1 hit.
    PROSITEiView protein in PROSITE
    PS00162. ALPHA_CA_1. 1 hit.
    PS51144. ALPHA_CA_2. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00915-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MASPDWGYDD KNGPEQWSKL YPIANGNNQS PVDIKTSETK HDTSLKPISV
    60 70 80 90 100
    SYNPATAKEI INVGHSFHVN FEDNDNRSVL KGGPFSDSYR LFQFHFHWGS
    110 120 130 140 150
    TNEHGSEHTV DGVKYSAELH VAHWNSAKYS SLAEAASKAD GLAVIGVLMK
    160 170 180 190 200
    VGEANPKLQK VLDALQAIKT KGKRAPFTNF DPSTLLPSSL DFWTYPGSLT
    210 220 230 240 250
    HPPLYESVTW IICKESISVS SEQLAQFRSL LSNVEGDNAV PMQHNNRPTQ
    260
    PLKGRTVRAS F
    Length:261
    Mass (Da):28,870
    Last modified:January 23, 2007 - v2
    Checksum:i4959E5FA25E374F8
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti75 – 76DN → ND AA sequence (PubMed:4217196).Curated2
    Sequence conflicti75 – 76DN → ND AA sequence (PubMed:4625868).Curated2

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_00137868H → R in variant Michigan-1; confers enhanced esterase activity and an additional zinc binding site. 2 Publications1
    Natural variantiVAR_048679143A → V. Corresponds to variant dbSNP:rs7821248Ensembl.1
    Natural variantiVAR_001379254G → R in Guam. 1 PublicationCorresponds to variant dbSNP:rs121909577Ensembl.1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X05014 mRNA. Translation: CAA28663.1.
    M33987 mRNA. Translation: AAA51910.1.
    BC027890 mRNA. Translation: AAH27890.1.
    CCDSiCCDS6237.1.
    PIRiJQ0786. CRHU1.
    RefSeqiNP_001122301.1. NM_001128829.3.
    NP_001122302.1. NM_001128830.3.
    NP_001122303.1. NM_001128831.3.
    NP_001158302.1. NM_001164830.1.
    NP_001729.1. NM_001738.4.
    UniGeneiHs.23118.

    Genome annotation databases

    EnsembliENST00000431316; ENSP00000392338; ENSG00000133742.
    ENST00000523022; ENSP00000429798; ENSG00000133742.
    ENST00000523953; ENSP00000430656; ENSG00000133742.
    ENST00000542576; ENSP00000443517; ENSG00000133742.
    GeneIDi759.
    KEGGihsa:759.

    Keywords - Coding sequence diversityi

    Polymorphism

    Similar proteinsi

    Entry informationi

    Entry nameiCAH1_HUMAN
    AccessioniPrimary (citable) accession number: P00915
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 25, 2017
    This is version 188 of the entry and version 2 of the sequence. See 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, Direct protein sequencing, 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