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Protein

Carbonic anhydrase 1

Gene

CA1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

    BioCyciMetaCyc:HS05785-MONOMER
    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
    MIMi114800 gene
    neXtProtiNX_P00915

    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
    MINTiP00915
    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 CA_dom
    IPR036398 CA_dom_sf
    IPR023561 Carbonic_anhydrase_a-class
    IPR018338 Carbonic_anhydrase_a-class_CS
    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 PublicationsCorresponds to variant dbSNP:rs990757234Ensembl.1
    Natural variantiVAR_048679143A → V. Corresponds to variant dbSNP:rs7821248Ensembl.1
    Natural variantiVAR_001379254G → R in Guam. 1 PublicationCorresponds to variant dbSNP:rs121909577EnsemblClinVar.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: May 23, 2018
    This is version 191 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

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