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Protein

Carbonic anhydrase 1

Gene

CA1

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

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Reversible hydration of carbon dioxide. Can hydrates cyanamide to urea.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+10 Publications

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

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

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei65Proton acceptorPROSITE-ProRule annotation1
    <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>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
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei200Substrate1 Publication1
    Metal bindingi201Zinc 2; in variant Michigan-11 Publication1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>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

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionLyase
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:HS05785-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    4.2.1.1 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-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-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P00915

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:CA1
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 8

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000133742.13

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:1368 CA1

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    114800 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P00915

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    759

    Open Targets

    More...
    OpenTargetsi
    ENSG00000133742

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA25984

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL261

    Drug and drug target database

    More...
    DrugBanki
    DB08156 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

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...
    GuidetoPHARMACOLOGYi
    2597

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    CA1

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    115449

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000774092 – 261Carbonic anhydrase 1Add BLAST260

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanine2 Publications1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P00915

    PeptideAtlas

    More...
    PeptideAtlasi
    P00915

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P00915

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    12614
    51291

    Consortium for Top Down Proteomics

    More...
    TopDownProteomicsi
    P00915

    2D gel databases

    DOSAC-COBS 2D-PAGE database

    More...
    DOSAC-COBS-2DPAGEi
    P00915

    REPRODUCTION-2DPAGE

    More...
    REPRODUCTION-2DPAGEi
    IPI00215983
    P00915

    University College Dublin 2-DE Proteome Database

    More...
    UCD-2DPAGEi
    P00915

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P00915

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    P00915

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000133742 Expressed in 126 organ(s), highest expression level in mucosa of transverse colon

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_CA1

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P00915 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P00915 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    CAB025790
    HPA006558

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    107214, 4 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    P00915, 4 interactors

    Molecular INTeraction database

    More...
    MINTi
    P00915

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000256119

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P00915

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1261
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P00915

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P00915

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P00915

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini4 – 261Alpha-carbonic anhydrasePROSITE-ProRule annotationAdd BLAST258

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni200 – 201Substrate bindingBy similarity2

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the alpha-carbonic anhydrase family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG0382 Eukaryota
    COG3338 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000161270

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000112637

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG002837

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P00915

    KEGG Orthology (KO)

    More...
    KOi
    K01672

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    DYGSEHT

    Database of Orthologous Groups

    More...
    OrthoDBi
    EOG091G0XFM

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P00915

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF316425

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.10.200.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View 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

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR18952 PTHR18952, 1 hit
    PTHR18952:SF82 PTHR18952:SF82, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00194 Carb_anhydrase, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM01057 Carb_anhydrase, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51069 SSF51069, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00162 ALPHA_CA_1, 1 hit
    PS51144 ALPHA_CA_2, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry has 1 described isoform and 13 potential isoforms that are computationally mapped.Show allAlign All

    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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4959E5FA25E374F8
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 13 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    E5RHP7E5RHP7_HUMAN
    Carbonic anhydrase 1
    CA1
    251Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    E5RFL2E5RFL2_HUMAN
    Carbonic anhydrase 1
    CA1
    118Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    E5RIF9E5RIF9_HUMAN
    Carbonic anhydrase 1
    CA1
    148Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    E5RGU8E5RGU8_HUMAN
    Carbonic anhydrase 1
    CA1
    99Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    E5RII2E5RII2_HUMAN
    Carbonic anhydrase 1
    CA1
    81Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    E5RH81E5RH81_HUMAN
    Carbonic anhydrase 1
    CA1
    175Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    E5RG43E5RG43_HUMAN
    Carbonic anhydrase 1
    CA1
    149Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    E5RFE7E5RFE7_HUMAN
    Carbonic anhydrase 1
    CA1
    194Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    E5RJI8E5RJI8_HUMAN
    Carbonic anhydrase 1
    CA1
    137Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    E5RJF6E5RJF6_HUMAN
    Carbonic anhydrase 1
    CA1
    87Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    There are more potential isoformsShow all

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>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:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    X05014 mRNA Translation: CAA28663.1
    M33987 mRNA Translation: AAA51910.1
    BC027890 mRNA Translation: AAH27890.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS6237.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    JQ0786 CRHU1

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_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

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.23118

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000431316; ENSP00000392338; ENSG00000133742
    ENST00000523022; ENSP00000429798; ENSG00000133742
    ENST00000523953; ENSP00000430656; ENSG00000133742
    ENST00000542576; ENSP00000443517; ENSG00000133742

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    759

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:759

    Keywords - Coding sequence diversityi

    Polymorphism

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    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

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    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[»]
    6EVRX-ray1.50A/B1-261[»]
    6EX1X-ray1.60A/B1-261[»]
    6F3BX-ray1.40A/B1-261[»]
    6FAFX-ray1.99A/B1-261[»]
    6FAGX-ray1.79A/B1-261[»]
    ProteinModelPortaliP00915
    SMRiP00915
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi107214, 4 interactors
    IntActiP00915, 4 interactors
    MINTiP00915
    STRINGi9606.ENSP00000256119

    Chemistry databases

    BindingDBiP00915
    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

    PTM databases

    iPTMnetiP00915
    PhosphoSitePlusiP00915

    Polymorphism and mutation databases

    BioMutaiCA1
    DMDMi115449

    2D gel databases

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

    Proteomic databases

    PaxDbiP00915
    PeptideAtlasiP00915
    PRIDEiP00915
    ProteomicsDBi12614
    51291
    TopDownProteomicsiP00915

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    759
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    759
    DisGeNETi759
    EuPathDBiHostDB:ENSG00000133742.13

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    CA1
    HGNCiHGNC:1368 CA1
    HPAiCAB025790
    HPA006558
    MIMi114800 gene
    neXtProtiNX_P00915
    OpenTargetsiENSG00000133742
    PharmGKBiPA25984

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG0382 Eukaryota
    COG3338 LUCA
    GeneTreeiENSGT00940000161270
    HOGENOMiHOG000112637
    HOVERGENiHBG002837
    InParanoidiP00915
    KOiK01672
    OMAiDYGSEHT
    OrthoDBiEOG091G0XFM
    PhylomeDBiP00915
    TreeFamiTF316425

    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

    Miscellaneous databases

    EvolutionaryTraceiP00915

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    CA1_(gene)

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...
    GenomeRNAii
    759

    Protein Ontology

    More...
    PROi
    PR:P00915

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000133742 Expressed in 126 organ(s), highest expression level in mucosa of transverse colon
    CleanExiHS_CA1
    ExpressionAtlasiP00915 baseline and differential
    GenevisibleiP00915 HS

    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

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCAH1_HUMAN
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P00915
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: December 5, 2018
    This is version 196 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    6. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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