Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 242 (03 Jul 2019)
Sequence version 2 (23 Jan 2007)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Carbonic anhydrase 2

Gene

CA2

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

Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye. Contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption. Stimulates the chloride-bicarbonate exchange activity of SLC26A6.By similarity3 Publications

Miscellaneous

Target of drugs used in treatments against glaucoma disorder and breast cancer.

<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+22 Publications, Co2+1 PublicationNote: Zinc. Can also use cobalt(II) with lower efficiency, but not copper(II), nickel(II) and manganese(II).1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 X-ray, histamine, L-adrenaline, L- and D-phenylalanine, L- and D-histidine, L-His-OMe and beta-Ala-His (carnosine). Competitively inhibited by saccharin, thioxolone, coumarins, 667-coumate, celecoxib (Celebrex), valdecoxib (Bextra), SC-125, SC-560, diclofenac, acetate, azide, bromide, sulfonamide derivatives such as acetazolamide (AZA), methazolamide (MZA), ethoxzolamide (EZA), dichlorophenamide (DCP), brinzolamide, dansylamide, thiabendazole-5-sulfonamide, trifluoromethane sulfonamide and N-hydroxysulfamide, fructose-based sugar sulfamate RWJ-37497, and Foscarnet (phosphonoformate trisodium salt). Repressed strongly by hydrogen sulfide(HS) and weakly by nitrate (NO3). Esterase activity weakly reduced by cyanamide. N-hydroxyurea interfers with zinc binding and inhibit activity.27 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>Absorptioni

Abs(max)=550 nm10 PublicationsAt pH 7.0. Shows a second maximum at 618 nm.

Kineticsi

  1. KM=10 mM for CO210 Publications
  2. KM=82 mM for H2CO310 Publications
  3. KM=3 mM for 4-nitrophenyl acetate10 Publications

    pH dependencei

    Optimum pH is 6-8.10 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei62Activator3 Publications1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei64Proton acceptor3 Publications1
    Active sitei673 Publications1
    Binding sitei67Activator3 Publications1
    Binding sitei92Activator3 Publications1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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; catalytic23 Publications1
    Metal bindingi96Zinc; catalytic22 Publications1
    Metal bindingi119Zinc; catalytic22 Publications1
    Active sitei1273 Publications1

    <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-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

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P00918

    <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 2 (EC:4.2.1.1)
    Alternative name(s):
    Carbonate dehydratase II
    Carbonic anhydrase C
    Short name:
    CAC
    Carbonic anhydrase II
    Short name:
    CA-II
    <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:CA2
    <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

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:1373 CA2

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    611492 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P00918

    <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 & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    <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

    <p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

    Osteopetrosis, autosomal recessive 3 (OPTB3)5 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. Osteopetrosis occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Recessive osteopetrosis commonly manifests in early infancy with macrocephaly, feeding difficulties, evolving blindness and deafness, bone marrow failure, severe anemia, and hepatosplenomegaly. Deafness and blindness are generally thought to represent effects of pressure on nerves. OPTB3 is associated with renal tubular acidosis, cerebral calcification (marble brain disease) and in some cases with mental retardation.
    Related information in OMIM
    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_00138192Q → P in OPTB3; in Czechoslovakia. 2 PublicationsCorresponds to variant dbSNP:rs1304160279Ensembl.1
    Natural variantiVAR_02100994H → Y in OPTB3; partial loss of activity. 1 Publication1
    Natural variantiVAR_001382107H → Y in OPTB3; frequent mutation. 4 PublicationsCorresponds to variant dbSNP:rs118203933EnsemblClinVar.1
    Natural variantiVAR_021010144G → R in OPTB3; complete loss of activity. 1 Publication1

    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>Mutagenesisi5W → A: Impaired activity, not rescued by 4-methylimidazole (4-MI); when associated with W-64. 1 Publication1
    Mutagenesisi7Y → F: Enhanced activity. 2 Publications1
    Mutagenesisi7Y → H: Reduced proton transfer rate. 2 Publications1
    Mutagenesisi62N → A: Reduced activity. 3 Publications1
    Mutagenesisi62N → D: Strongly reduced activity. 3 Publications1
    Mutagenesisi62N → H: Reduced proton transfer; when associated with A-64. 3 Publications1
    Mutagenesisi62N → L: Reduced activity. 3 Publications1
    Mutagenesisi62N → T: Reduced activity. 3 Publications1
    Mutagenesisi62N → V: Reduced activity. 3 Publications1
    Mutagenesisi64H → A: Reduced CO(2) hydrase activity, rescued by 4-methylimidazole (4-MI). Reduced proton transfer; when associated with H-62. Enhanced proton transfer; when associated with H-67. Enhanced proton transfer capacity; when associated with H-99. 4 Publications1
    Mutagenesisi64H → G: Impaired activity, not rescued by 4-methylimidazole (4-MI). 4 Publications1
    Mutagenesisi64H → W: Impaired activity, rescued by 4-methylimidazole (4-MI). Impaired activity, not rescued by 4-methylimidazole (4-MI); when associated with A-5. 4 Publications1
    Mutagenesisi65A → F: Reduced activity. 1 Publication1
    Mutagenesisi65A → H, L or S: Normal activity. 1 Publication1
    Mutagenesisi67N → H: Enhanced proton transfer; when associated with A-64. 3 Publications1
    Mutagenesisi67N → L: Reduced activity. 3 Publications1
    Mutagenesisi67N → Q: Normal activity. 3 Publications1
    Mutagenesisi94H → C, D, E, N or Q: Strongly reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities, impaired stability of zinc binding. 2 Publications1
    Mutagenesisi106E → A or Q: Strongly reduced CO(2) hydrase activity. 2 Publications1
    Mutagenesisi106E → D: Normal CO(2) hydrase activity. 2 Publications1
    Mutagenesisi117E → Q: Strongly reduced activity and sulfonamide affinity. 1 Publication1
    Mutagenesisi119H → D, N or Q: Reduced activity. 1 Publication1
    Mutagenesisi119H → E: Strongly reduced activity. 1 Publication1
    Mutagenesisi121V → A, G, I, L or S: Reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities. 1 Publication1
    Mutagenesisi121V → K or R: Strongly reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities. 1 Publication1
    Mutagenesisi142V → F or Y: Strongly impaired activity. 1 Publication1
    Mutagenesisi142V → G: Weakly impaired activity. 1 Publication1
    Mutagenesisi142V → H: Impaired activity. 1 Publication1
    Mutagenesisi197L → A: Reduced CO(2) hydrase activity. 1 Publication1
    Mutagenesisi197L → E, H or R: Strongly reduced CO(2) hydrase activity. 1 Publication1
    Mutagenesisi197L → F: Normal activity. 1 Publication1
    Mutagenesisi198T → A, C, H or P: Strongly reduced activity. 5 Publications1
    Mutagenesisi198T → D or E: Strongly reduced activity, but enhanced zinc affinity. 5 Publications1
    Mutagenesisi198T → S or V: Reduced activity. 5 Publications1
    Mutagenesisi199T → H: Higher affinity for bicarbonate. Enhanced proton transfer capacity; when associated with A-64. 3 Publications1
    Mutagenesisi199T → S: Enhanced p-nitrophenyl acetate esterase activity, but normal CO(2) hydrase activity. 3 Publications1
    Mutagenesisi201P → A: Normal CO(2) hydrase activity, but impaired stability. 1 Publication1

    Keywords - Diseasei

    Disease mutation, Osteopetrosis

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    760

    MalaCards human disease database

    More...
    MalaCardsi
    CA2
    MIMi259730 phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000104267

    Orphanet; a database dedicated to information on rare diseases and orphan drugs

    More...
    Orphaneti
    2785 Osteopetrosis with renal tubular acidosis

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA25989

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL205

    Drug and drug target database

    More...
    DrugBanki
    DB03333 (4-sulfamoyl-phenyl)-thiocarbamic acid O-(2-thiophen-3-yl-ethyl) ester
    DB02479 (R)-N-(3-Indol-1-Yl-2-Methyl-Propyl)-4-Sulfamoyl-Benzamide
    DB03950 (S)-N-(3-Indol-1-Yl-2-Methyl-Propyl)-4-Sulfamoyl-Benzamide
    DB08659 2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide
    DB08046 2-chloro-5-[(1S)-1-hydroxy-3-oxo-2H-isoindol-1-yl]benzenesulfonamide
    DB08156 3-[4-(AMINOSULFONYL)PHENYL]PROPANOIC ACID
    DB04203 3-Mercuri-4-Aminobenzenesulfonamide
    DB04394 3-Nitro-4-(2-Oxo-Pyrrolidin-1-Yl)-Benzenesulfonamide
    DB08782 4-(2-AMINOETHYL)BENZENESULFONAMIDE
    DB02429 4-(Aminosulfonyl)-N-[(4-Fluorophenyl)Methyl]-Benzamide
    DB01671 4-(Hydroxymercury)Benzoic Acid
    DB08202 4-({[(4-METHYLPIPERAZIN-1-YL)AMINO]CARBONOTHIOYL}AMINO)BENZENESULFONAMIDE
    DB01784 4-Flourobenzenesulfonamide
    DB03385 4-Methylimidazole
    DB03697 4-Sulfonamide-[1-(4-Aminobutane)]Benzamide
    DB04002 4-Sulfonamide-[4-(Thiomethylaminobutane)]Benzamide
    DB00819 Acetazolamide
    DB03877 AL4623
    DB04089 AL5300
    DB01964 AL5424
    DB03526 AL5927
    DB04371 AL6528
    DB02220 Al7089a
    DB03221 AL7099A
    DB02602 AL7182
    DB02535 Aminodi(Ethyloxy)Ethylaminocarbonylbenzenesulfonamide
    DB00436 Bendroflumethiazide
    DB00562 Benzthiazide
    DB01194 Brinzolamide
    DB00880 Chlorothiazide
    DB02679 Cyanamide
    DB00606 Cyclothiazide
    DB02866 Dansylamide
    DB01119 Diazoxide
    DB01144 Diclofenamide
    DB00869 Dorzolamide
    DB08846 Ellagic Acid
    DB01031 Ethinamate
    DB00311 Ethoxzolamide
    DB08157 ETHYL 3-[4-(AMINOSULFONYL)PHENYL]PROPANOATE
    DB01942 Formic Acid
    DB00695 Furosemide
    DB00999 Hydrochlorothiazide
    DB00774 Hydroflumethiazide
    DB08165 indane-5-sulfonamide
    DB03975 Mercuribenzoic Acid
    DB00703 Methazolamide
    DB00232 Methyclothiazide
    DB02069 N-(2-Flouro-Benzyl)-4-Sulfamoyl-Benzamide
    DB08301 N-({[4-(AMINOSULFONYL)PHENYL]AMINO}CARBONYL)-4-METHYLBENZENESULFONAMIDE
    DB03596 N-[2-(1h-Indol-5-Yl)-Butyl]-4-Sulfamoyl-Benzamide
    DB07476 N-[4-(AMINOSULFONYL)PHENYL]-2-MERCAPTOBENZAMIDE
    DB01748 N-Benzyl-4-Sulfamoyl-Benzamide
    DB08155 N-{2-[4-(AMINOSULFONYL)PHENYL]ETHYL}ACETAMIDE
    DB07710 PHENYLALANYLAMINODI(ETHYLOXY)ETHYL BENZENESULFONAMIDEAMINOCARBONYLBENZENESULFONAMIDE
    DB01325 Quinethazone
    DB09460 Sodium carbonate
    DB08329 SULTHIAME
    DB00273 Topiramate
    DB01021 Trichlormethiazide
    DB03904 Urea
    DB00909 Zonisamide

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    CA2

    <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 methionineiRemoved2 Publications
    <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_00000774182 – 260Carbonic anhydrase 2Add 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-acetylserine2 Publications1
    Modified residuei2PhosphoserineBy similarity1
    Modified residuei165PhosphoserineCombined sources1
    Modified residuei172PhosphoserineCombined sources1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P00918

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P00918

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

    More...
    PaxDbi
    P00918

    PeptideAtlas

    More...
    PeptideAtlasi
    P00918

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P00918

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    12616
    51292

    2D gel databases

    USC-OGP 2-DE database

    More...
    OGPi
    P00918

    REPRODUCTION-2DPAGE

    More...
    REPRODUCTION-2DPAGEi
    IPI00218414
    P00918

    University College Dublin 2-DE Proteome Database

    More...
    UCD-2DPAGEi
    P00918

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P00918

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

    More...
    PhosphoSitePlusi
    P00918

    <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
    ENSG00000104267 Expressed in 213 organ(s), highest expression level in colonic mucosa

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P00918 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P00918 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    CAB010102
    HPA001550

    <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">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Interacts with SLC4A4. Interaction with SLC4A7 regulates SLC4A7 transporter activity.

    Interacts with SLC26A6 isoform 4 (via C-terminus cytoplasmic domain).

    90 Publications

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    107215, 18 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    P00918, 7 interactors

    Molecular INTeraction database

    More...
    MINTi
    P00918

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000285379

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P00918

    <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

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

    More...
    SMRi
    P00918

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P00918

    <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>Regioni198 – 199Substrate binding2 Publications2

    <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
    ENSGT00940000160385

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000112637

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P00918

    KEGG Orthology (KO)

    More...
    KOi
    K18245

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    HKEFPIA

    Database of Orthologous Groups

    More...
    OrthoDBi
    1581168at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P00918

    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

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR18952 PTHR18952, 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>. The information is filed in different subsections. The current subsections and their content are listed below:<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 2 potential isoforms that are computationally mapped.Show allAlign All

    P00918-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSHHWGYGKH NGPEHWHKDF PIAKGERQSP VDIDTHTAKY DPSLKPLSVS
    60 70 80 90 100
    YDQATSLRIL NNGHAFNVEF DDSQDKAVLK GGPLDGTYRL IQFHFHWGSL
    110 120 130 140 150
    DGQGSEHTVD KKKYAAELHL VHWNTKYGDF GKAVQQPDGL AVLGIFLKVG
    160 170 180 190 200
    SAKPGLQKVV DVLDSIKTKG KSADFTNFDP RGLLPESLDY WTYPGSLTTP
    210 220 230 240 250
    PLLECVTWIV LKEPISVSSE QVLKFRKLNF NGEGEPEELM VDNWRPAQPL
    260
    KNRQIKASFK
    Length:260
    Mass (Da):29,246
    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:i2EC2BB7548F10558
    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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    E5RID5E5RID5_HUMAN
    Carbonic anhydrase 2
    CA2
    97Annotation score:

    Annotation score:2 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>
    E5RK37E5RK37_HUMAN
    Carbonic anhydrase 2
    CA2
    101Annotation 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>

    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 conflicti179 – 180DP → AA in AAH11949 (PubMed:15489334).Curated2

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_00138018K → E in Jogjakarta. 1 PublicationCorresponds to variant dbSNP:rs118203931EnsemblClinVar.1
    Natural variantiVAR_00138192Q → P in OPTB3; in Czechoslovakia. 2 PublicationsCorresponds to variant dbSNP:rs1304160279Ensembl.1
    Natural variantiVAR_02100994H → Y in OPTB3; partial loss of activity. 1 Publication1
    Natural variantiVAR_001382107H → Y in OPTB3; frequent mutation. 4 PublicationsCorresponds to variant dbSNP:rs118203933EnsemblClinVar.1
    Natural variantiVAR_021010144G → R in OPTB3; complete loss of activity. 1 Publication1
    Natural variantiVAR_001383236P → H in Melbourne. 1 PublicationCorresponds to variant dbSNP:rs118203932EnsemblClinVar.1
    Natural variantiVAR_001384252N → D. Corresponds to variant dbSNP:rs2228063EnsemblClinVar.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
    M77181
    , M77176, M77177, M77178, M77179, M77180 Genomic DNA Translation: AAA51909.1
    Y00339 mRNA Translation: CAA68426.1
    X03251 Genomic DNA Translation: CAA27012.1
    J03037 mRNA Translation: AAA51908.1
    CR536526 mRNA Translation: CAG38763.1
    CR541875 mRNA Translation: CAG46673.1
    AK312978 mRNA Translation: BAG35815.1
    CH471068 Genomic DNA Translation: EAW87136.1
    BC011949 mRNA Translation: AAH11949.1
    M36532 mRNA Translation: AAA51911.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS6239.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A27175 CRHU2

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_000058.1, NM_000067.2

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000285379; ENSP00000285379; ENSG00000104267

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    760

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:760

    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
    M77181
    , M77176, M77177, M77178, M77179, M77180 Genomic DNA Translation: AAA51909.1
    Y00339 mRNA Translation: CAA68426.1
    X03251 Genomic DNA Translation: CAA27012.1
    J03037 mRNA Translation: AAA51908.1
    CR536526 mRNA Translation: CAG38763.1
    CR541875 mRNA Translation: CAG46673.1
    AK312978 mRNA Translation: BAG35815.1
    CH471068 Genomic DNA Translation: EAW87136.1
    BC011949 mRNA Translation: AAH11949.1
    M36532 mRNA Translation: AAA51911.1
    CCDSiCCDS6239.1
    PIRiA27175 CRHU2
    RefSeqiNP_000058.1, NM_000067.2

    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
    12CAX-ray2.40A1-260[»]
    1A42X-ray2.25A2-260[»]
    1AM6X-ray2.00A2-260[»]
    1AVNX-ray2.00A2-260[»]
    1BCDX-ray1.90A2-260[»]
    1BICX-ray1.90A2-260[»]
    1BN1X-ray2.10A2-260[»]
    1BN3X-ray2.20A2-260[»]
    1BN4X-ray2.10A2-260[»]
    1BNMX-ray2.60A2-260[»]
    1BNNX-ray2.30A2-260[»]
    1BNQX-ray2.40A2-260[»]
    1BNTX-ray2.15A2-260[»]
    1BNUX-ray2.15A2-260[»]
    1BNVX-ray2.40A2-260[»]
    1BNWX-ray2.25A2-260[»]
    1BV3X-ray1.85A2-260[»]
    1CA2X-ray2.00A2-260[»]
    1CA3X-ray2.30A1-260[»]
    1CAHX-ray1.88A2-260[»]
    1CAIX-ray1.80A2-260[»]
    1CAJX-ray1.90A2-260[»]
    1CAKX-ray1.90A2-260[»]
    1CALX-ray2.20A2-260[»]
    1CAMX-ray1.70A2-260[»]
    1CANX-ray1.90A2-260[»]
    1CAOX-ray1.90A2-260[»]
    1CAYX-ray2.10A2-260[»]
    1CAZX-ray1.90A2-260[»]
    1CCSX-ray2.35A2-260[»]
    1CCTX-ray2.20A2-260[»]
    1CCUX-ray2.25A2-260[»]
    1CILX-ray1.60A2-260[»]
    1CIMX-ray2.10A2-260[»]
    1CINX-ray2.10A2-260[»]
    1CNBX-ray2.35A2-260[»]
    1CNCX-ray2.20A2-260[»]
    1CNGX-ray1.90A2-260[»]
    1CNHX-ray2.05A2-260[»]
    1CNIX-ray1.80A2-260[»]
    1CNJX-ray1.80A2-260[»]
    1CNKX-ray2.15A2-260[»]
    1CNWX-ray2.00A1-260[»]
    1CNXX-ray1.90A1-260[»]
    1CNYX-ray2.30A1-260[»]
    1CRAX-ray1.90A2-260[»]
    1CVAX-ray2.25A2-260[»]
    1CVBX-ray2.40A2-260[»]
    1CVCX-ray2.30A2-260[»]
    1CVDX-ray2.20A5-259[»]
    1CVEX-ray2.25A2-260[»]
    1CVFX-ray2.25A2-260[»]
    1CVHX-ray2.30A5-259[»]
    1DCAX-ray2.20A1-260[»]
    1DCBX-ray2.10A1-260[»]
    1EOUX-ray2.10A1-260[»]
    1F2WX-ray1.90A2-260[»]
    1FQLX-ray2.00A1-260[»]
    1FQMX-ray2.00A1-260[»]
    1FQNX-ray2.00A1-260[»]
    1FQRX-ray2.00A1-260[»]
    1FR4X-ray1.60A1-260[»]
    1FR7X-ray1.50A/B1-260[»]
    1FSNX-ray2.00A/B1-260[»]
    1FSQX-ray2.00A/B1-260[»]
    1FSRX-ray2.00A/B1-260[»]
    1G0EX-ray1.60A1-260[»]
    1G0FX-ray1.60A1-260[»]
    1G1DX-ray2.04A2-260[»]
    1G3ZX-ray1.86A2-260[»]
    1G45X-ray1.83A2-260[»]
    1G46X-ray1.84A2-260[»]
    1G48X-ray1.86A2-260[»]
    1G4JX-ray1.84A2-260[»]
    1G4OX-ray1.96A2-260[»]
    1G52X-ray1.80A2-260[»]
    1G53X-ray1.94A2-260[»]
    1G54X-ray1.86A2-260[»]
    1H4NX-ray2.00A2-260[»]
    1H9NX-ray1.85A2-260[»]
    1H9QX-ray2.20A2-260[»]
    1HCAX-ray2.30A1-260[»]
    1HEAX-ray2.00A1-260[»]
    1HEBX-ray2.00A1-260[»]
    1HECX-ray2.00A1-260[»]
    1HEDX-ray2.00A1-260[»]
    1HVAX-ray2.30A1-260[»]
    1I8ZX-ray1.93A2-260[»]
    1I90X-ray2.00A2-260[»]
    1I91X-ray2.00A2-260[»]
    1I9LX-ray1.93A2-260[»]
    1I9MX-ray1.84A2-260[»]
    1I9NX-ray1.86A2-260[»]
    1I9OX-ray1.86A2-260[»]
    1I9PX-ray1.92A2-260[»]
    1I9QX-ray1.80A2-260[»]
    1IF4X-ray1.93A2-260[»]
    1IF5X-ray2.00A2-260[»]
    1IF6X-ray2.09A2-259[»]
    1IF7X-ray1.98A2-260[»]
    1IF8X-ray1.94A2-260[»]
    1IF9</