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Protein

Carbonic anhydrase 3

Gene

CA3

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.

<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+2 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 proton donors such as imidazole and the dipeptide histidylhistidine. Inhibited by coumarins and sulfonamide derivatives such as acetazolamide.3 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=52.0 mM for CO21 Publication

    Sites

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

    <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

    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

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    4.2.1.1 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-1475029 Reversible hydration of carbon dioxide

    <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 3 (EC:4.2.1.1)
    Alternative name(s):
    Carbonate dehydratase III
    Carbonic anhydrase III
    Short name:
    CA-III
    <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:CA3
    <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:ENSG00000164879.6

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:1374 CA3

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    114750 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P07451

    <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

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

    DisGeNET

    More...
    DisGeNETi
    761

    Open Targets

    More...
    OpenTargetsi
    ENSG00000164879

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA25990

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL2885

    Drug and drug target database

    More...
    DrugBanki
    DB00819 Acetazolamide
    DB08846 Ellagic Acid
    DB00909 Zonisamide

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    CA3

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    134047703

    <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 methionineiRemovedBy similarity
    <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_00000774262 – 260Carbonic anhydrase 3Add BLAST259

    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-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

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    S-glutathionylated in hepatocytes under oxidative stress.By similarity

    Keywords - PTMi

    Acetylation, Glutathionylation, Phosphoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P07451

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

    More...
    PaxDbi
    P07451

    PeptideAtlas

    More...
    PeptideAtlasi
    P07451

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P07451

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    52004

    2D gel databases

    University College Dublin 2-DE Proteome Database

    More...
    UCD-2DPAGEi
    P07451

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P07451

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

    More...
    PhosphoSitePlusi
    P07451

    <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

    <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Muscle specific.

    <p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>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

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000164879 Expressed in 158 organ(s), highest expression level in vastus lateralis

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_CA3

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P07451 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P07451 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    CAB004967
    HPA021775
    HPA026700

    <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

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    107216, 4 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    P07451, 2 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000285381

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P07451

    <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

    1260
    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
    P07451

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

    More...
    SMRi
    P07451

    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
    P07451

    <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>Domaini3 – 259Alpha-carbonic anhydrasePROSITE-ProRule annotationAdd BLAST257

    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>Regioni64 – 67Involved in proton transfer4
    Regioni198 – 199Substrate 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
    ENSGT00940000159435

    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
    P07451

    KEGG Orthology (KO)

    More...
    KOi
    K01672

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    YDRSMLR

    Database of Orthologous Groups

    More...
    OrthoDBi
    EOG091G0XFM

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P07451

    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
    IPR018441 Carbonic_anhydrase_CA3

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR18952 PTHR18952, 1 hit
    PTHR18952:SF127 PTHR18952:SF127, 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 1 potential isoform that is computationally mapped.Show allAlign All

    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
    <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:iA305334167233FCF
    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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    E5RHI4E5RHI4_HUMAN
    Carbonic anhydrase 3
    CA3
    19Annotation 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>

    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_01618031V → I3 PublicationsCorresponds to variant dbSNP:rs20571Ensembl.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
    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

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS6238.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A26658 CRHU3

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_005172.1, NM_005181.3

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.82129

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000285381; ENSP00000285381; ENSG00000164879

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    761

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:761

    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
    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:

    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
    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, 4 interactors
    IntActiP07451, 2 interactors
    STRINGi9606.ENSP00000285381

    Chemistry databases

    BindingDBiP07451
    ChEMBLiCHEMBL2885
    DrugBankiDB00819 Acetazolamide
    DB08846 Ellagic Acid
    DB00909 Zonisamide

    PTM databases

    iPTMnetiP07451
    PhosphoSitePlusiP07451

    Polymorphism and mutation databases

    BioMutaiCA3
    DMDMi134047703

    2D gel databases

    UCD-2DPAGEiP07451

    Proteomic databases

    EPDiP07451
    PaxDbiP07451
    PeptideAtlasiP07451
    PRIDEiP07451
    ProteomicsDBi52004

    Protocols and materials databases

    The DNASU plasmid repository

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    DNASUi
    761
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000285381; ENSP00000285381; ENSG00000164879
    GeneIDi761
    KEGGihsa:761

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    761
    DisGeNETi761
    EuPathDBiHostDB:ENSG00000164879.6

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    CA3

    H-Invitational Database, human transcriptome db

    More...
    H-InvDBi
    HIX0078885
    HGNCiHGNC:1374 CA3
    HPAiCAB004967
    HPA021775
    HPA026700
    MIMi114750 gene
    neXtProtiNX_P07451
    OpenTargetsiENSG00000164879
    PharmGKBiPA25990

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG0382 Eukaryota
    COG3338 LUCA
    GeneTreeiENSGT00940000159435
    HOGENOMiHOG000112637
    HOVERGENiHBG002837
    InParanoidiP07451
    KOiK01672
    OMAiYDRSMLR
    OrthoDBiEOG091G0XFM
    PhylomeDBiP07451
    TreeFamiTF316425

    Enzyme and pathway databases

    BRENDAi4.2.1.1 2681
    ReactomeiR-HSA-1475029 Reversible hydration of carbon dioxide

    Miscellaneous databases

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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    ChiTaRSi
    CA3 human
    EvolutionaryTraceiP07451

    The Gene Wiki collection of pages on human genes and proteins

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    GeneWikii
    Carbonic_anhydrase_III,_muscle_specific

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

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    GenomeRNAii
    761

    Protein Ontology

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    PROi
    PR:P07451

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000164879 Expressed in 158 organ(s), highest expression level in vastus lateralis
    CleanExiHS_CA3
    ExpressionAtlasiP07451 baseline and differential
    GenevisibleiP07451 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
    IPR018441 Carbonic_anhydrase_CA3
    PANTHERiPTHR18952 PTHR18952, 1 hit
    PTHR18952:SF127 PTHR18952:SF127, 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

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    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 nameiCAH3_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: P07451
    Secondary accession number(s): B2R867, B3KUC8, O60842
    <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: April 1, 1988
    Last sequence update: March 20, 2007
    Last modified: December 5, 2018
    This is version 189 of the entry and version 3 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, 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
    UniProt is an ELIXIR core data resource
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