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Protein

Carbonic anhydrase 14

Gene

CA14

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Reversible hydration of carbon dioxide.

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zn2+1 Publication

Enzyme regulationi

Activated by histamine, L-adrenaline, L- and D-histidine, and L- and D-phenylalanine. Inhibited by coumarins, saccharin, sulfonamide derivatives such as acetazolamide (AZA) and Foscarnet (phosphonoformate trisodium salt).8 Publications

Kineticsi

  1. KM=7.9 mM for CO21 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei84Proton acceptorBy similarity1
    Metal bindingi109Zinc; catalytic1 Publication1
    Metal bindingi111Zinc; catalytic1 Publication1
    Metal bindingi135Zinc; catalytic1 Publication1
    Active sitei144By similarity1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciZFISH:HS04211-MONOMER.
    BRENDAi4.2.1.1. 2681.
    ReactomeiR-HSA-1475029. Reversible hydration of carbon dioxide.
    SABIO-RKQ9ULX7.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbonic anhydrase 14 (EC:4.2.1.1)
    Alternative name(s):
    Carbonate dehydratase XIV
    Carbonic anhydrase XIV
    Short name:
    CA-XIV
    Gene namesi
    Name:CA14
    ORF Names:UNQ690/PRO1335
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1372. CA14.

    Subcellular locationi

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Topological domaini16 – 290ExtracellularSequence analysisAdd BLAST275
    Transmembranei291 – 311HelicalSequence analysisAdd BLAST21
    Topological domaini312 – 337CytoplasmicSequence analysisAdd BLAST26

    GO - Cellular componenti

    • integral component of membrane Source: ProtInc
    • plasma membrane Source: Reactome
    Complete GO annotation...

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    DisGeNETi23632.
    OpenTargetsiENSG00000118298.
    PharmGKBiPA25988.

    Chemistry databases

    ChEMBLiCHEMBL3510.
    DrugBankiDB00819. Acetazolamide.
    DB00909. Zonisamide.
    GuidetoPHARMACOLOGYi2598.

    Polymorphism and mutation databases

    BioMutaiCA14.
    DMDMi8928036.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 15Sequence analysisAdd BLAST15
    ChainiPRO_000000425116 – 337Carbonic anhydrase 14Add BLAST322

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi40 ↔ 2211 Publication
    Glycosylationi213N-linked (GlcNAc...)1 Publication1
    Modified residuei325PhosphoserineCombined sources1

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    EPDiQ9ULX7.
    PaxDbiQ9ULX7.
    PeptideAtlasiQ9ULX7.
    PRIDEiQ9ULX7.

    PTM databases

    iPTMnetiQ9ULX7.
    PhosphoSitePlusiQ9ULX7.

    Expressioni

    Tissue specificityi

    High expression in all parts of the central nervous system and lower expression in adult liver, heart, small intestine, colon, kidney, urinary bladder and skeletal muscle.

    Gene expression databases

    BgeeiENSG00000118298.
    CleanExiHS_CA14.
    ExpressionAtlasiQ9ULX7. baseline and differential.
    GenevisibleiQ9ULX7. HS.

    Organism-specific databases

    HPAiHPA008482.

    Interactioni

    Protein-protein interaction databases

    BioGridi117162. 47 interactors.
    IntActiQ9ULX7. 1 interactor.
    STRINGi9606.ENSP00000358107.

    Chemistry databases

    BindingDBiQ9ULX7.

    Structurei

    Secondary structure

    1337
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi24 – 26Combined sources3
    Helixi30 – 32Combined sources3
    Helixi33 – 36Combined sources4
    Helixi38 – 41Combined sources4
    Beta strandi42 – 44Combined sources3
    Helixi52 – 54Combined sources3
    Beta strandi66 – 68Combined sources3
    Beta strandi77 – 81Combined sources5
    Beta strandi86 – 89Combined sources4
    Beta strandi95 – 101Combined sources7
    Beta strandi103 – 112Combined sources10
    Beta strandi122 – 125Combined sources4
    Beta strandi131 – 140Combined sources10
    Turni141 – 143Combined sources3
    Helixi147 – 150Combined sources4
    Beta strandi157 – 169Combined sources13
    Helixi172 – 178Combined sources7
    Helixi179 – 183Combined sources5
    Beta strandi190 – 193Combined sources4
    Helixi198 – 201Combined sources4
    Beta strandi209 – 214Combined sources6
    Beta strandi225 – 232Combined sources8
    Beta strandi234 – 237Combined sources4
    Helixi238 – 245Combined sources8
    Beta strandi249 – 255Combined sources7
    Beta strandi275 – 277Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4LU3X-ray2.00A16-290[»]
    5CJFX-ray1.83A16-291[»]
    ProteinModelPortaliQ9ULX7.
    SMRiQ9ULX7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini20 – 278Alpha-carbonic anhydrasePROSITE-ProRule annotationAdd BLAST259

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni217 – 218Substrate bindingBy similarity2

    Sequence similaritiesi

    Belongs to the alpha-carbonic anhydrase family.Curated
    Contains 1 alpha-carbonic anhydrase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiKOG0382. Eukaryota.
    COG3338. LUCA.
    GeneTreeiENSGT00760000118915.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiQ9ULX7.
    KOiK01672.
    OMAiSYPECGS.
    OrthoDBiEOG091G0XFM.
    PhylomeDBiQ9ULX7.
    TreeFamiTF316425.

    Family and domain databases

    Gene3Di3.10.200.10. 1 hit.
    InterProiIPR001148. Carbonic_anhydrase_a.
    IPR023561. Carbonic_anhydrase_a-class.
    IPR018431. Carbonic_anhydrase_CA14.
    [Graphical view]
    PANTHERiPTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF84. PTHR18952:SF84. 1 hit.
    PfamiPF00194. Carb_anhydrase. 1 hit.
    [Graphical view]
    SMARTiSM01057. Carb_anhydrase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51069. SSF51069. 1 hit.
    PROSITEiPS51144. ALPHA_CA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9ULX7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLFSALLLEV IWILAADGGQ HWTYEGPHGQ DHWPASYPEC GNNAQSPIDI
    60 70 80 90 100
    QTDSVTFDPD LPALQPHGYD QPGTEPLDLH NNGHTVQLSL PSTLYLGGLP
    110 120 130 140 150
    RKYVAAQLHL HWGQKGSPGG SEHQINSEAT FAELHIVHYD SDSYDSLSEA
    160 170 180 190 200
    AERPQGLAVL GILIEVGETK NIAYEHILSH LHEVRHKDQK TSVPPFNLRE
    210 220 230 240 250
    LLPKQLGQYF RYNGSLTTPP CYQSVLWTVF YRRSQISMEQ LEKLQGTLFS
    260 270 280 290 300
    TEEEPSKLLV QNYRALQPLN QRMVFASFIQ AGSSYTTGEM LSLGVGILVG
    310 320 330
    CLCLLLAVYF IARKIRKKRL ENRKSVVFTS AQATTEA
    Length:337
    Mass (Da):37,668
    Last modified:May 1, 2000 - v1
    Checksum:i6E101C44EA70A700
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti229V → A in BAC11191 (PubMed:14702039).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB025904 mRNA. Translation: BAA85002.1.
    AY358689 mRNA. Translation: AAQ89052.1.
    AK074765 mRNA. Translation: BAC11191.1.
    BT020054 mRNA. Translation: AAV38857.1.
    AL138795 Genomic DNA. Translation: CAI22810.1.
    BC034412 mRNA. Translation: AAH34412.1.
    CCDSiCCDS947.1.
    RefSeqiNP_036245.1. NM_012113.2.
    UniGeneiHs.528988.

    Genome annotation databases

    EnsembliENST00000369111; ENSP00000358107; ENSG00000118298.
    GeneIDi23632.
    KEGGihsa:23632.
    UCSCiuc001etx.5. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB025904 mRNA. Translation: BAA85002.1.
    AY358689 mRNA. Translation: AAQ89052.1.
    AK074765 mRNA. Translation: BAC11191.1.
    BT020054 mRNA. Translation: AAV38857.1.
    AL138795 Genomic DNA. Translation: CAI22810.1.
    BC034412 mRNA. Translation: AAH34412.1.
    CCDSiCCDS947.1.
    RefSeqiNP_036245.1. NM_012113.2.
    UniGeneiHs.528988.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4LU3X-ray2.00A16-290[»]
    5CJFX-ray1.83A16-291[»]
    ProteinModelPortaliQ9ULX7.
    SMRiQ9ULX7.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi117162. 47 interactors.
    IntActiQ9ULX7. 1 interactor.
    STRINGi9606.ENSP00000358107.

    Chemistry databases

    BindingDBiQ9ULX7.
    ChEMBLiCHEMBL3510.
    DrugBankiDB00819. Acetazolamide.
    DB00909. Zonisamide.
    GuidetoPHARMACOLOGYi2598.

    PTM databases

    iPTMnetiQ9ULX7.
    PhosphoSitePlusiQ9ULX7.

    Polymorphism and mutation databases

    BioMutaiCA14.
    DMDMi8928036.

    Proteomic databases

    EPDiQ9ULX7.
    PaxDbiQ9ULX7.
    PeptideAtlasiQ9ULX7.
    PRIDEiQ9ULX7.

    Protocols and materials databases

    DNASUi23632.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000369111; ENSP00000358107; ENSG00000118298.
    GeneIDi23632.
    KEGGihsa:23632.
    UCSCiuc001etx.5. human.

    Organism-specific databases

    CTDi23632.
    DisGeNETi23632.
    GeneCardsiCA14.
    HGNCiHGNC:1372. CA14.
    HPAiHPA008482.
    MIMi604832. gene.
    neXtProtiNX_Q9ULX7.
    OpenTargetsiENSG00000118298.
    PharmGKBiPA25988.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG0382. Eukaryota.
    COG3338. LUCA.
    GeneTreeiENSGT00760000118915.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiQ9ULX7.
    KOiK01672.
    OMAiSYPECGS.
    OrthoDBiEOG091G0XFM.
    PhylomeDBiQ9ULX7.
    TreeFamiTF316425.

    Enzyme and pathway databases

    BioCyciZFISH:HS04211-MONOMER.
    BRENDAi4.2.1.1. 2681.
    ReactomeiR-HSA-1475029. Reversible hydration of carbon dioxide.
    SABIO-RKQ9ULX7.

    Miscellaneous databases

    ChiTaRSiCA14. human.
    GeneWikiiCA14.
    GenomeRNAii23632.
    PROiQ9ULX7.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000118298.
    CleanExiHS_CA14.
    ExpressionAtlasiQ9ULX7. baseline and differential.
    GenevisibleiQ9ULX7. HS.

    Family and domain databases

    Gene3Di3.10.200.10. 1 hit.
    InterProiIPR001148. Carbonic_anhydrase_a.
    IPR023561. Carbonic_anhydrase_a-class.
    IPR018431. Carbonic_anhydrase_CA14.
    [Graphical view]
    PANTHERiPTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF84. PTHR18952:SF84. 1 hit.
    PfamiPF00194. Carb_anhydrase. 1 hit.
    [Graphical view]
    SMARTiSM01057. Carb_anhydrase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51069. SSF51069. 1 hit.
    PROSITEiPS51144. ALPHA_CA_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiCAH14_HUMAN
    AccessioniPrimary (citable) accession number: Q9ULX7
    Secondary accession number(s): Q5TB24, Q8NCF4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 2000
    Last modified: November 2, 2016
    This is version 151 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.