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Protein

Carbonic anhydrase 13

Gene

CA13

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

Inhibited by acetazolamide.1 Publication

Kineticsi

  1. KM=13.8 mM for CO21 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei65Proton acceptorBy similarity1
    Active sitei68By similarity1
    Metal bindingi95Zinc; catalytic1 Publication1
    Metal bindingi97Zinc; catalytic1 Publication1
    Metal bindingi120Zinc; catalytic1 Publication1
    Active sitei129By similarity1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciZFISH:G66-32297-MONOMER.
    ReactomeiR-HSA-1475029. Reversible hydration of carbon dioxide.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbonic anhydrase 13 (EC:4.2.1.1)
    Alternative name(s):
    Carbonate dehydratase XIII
    Carbonic anhydrase XIII
    Short name:
    CA-XIII
    Gene namesi
    Name:CA13
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:14914. CA13.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Pathology & Biotechi

    Organism-specific databases

    DisGeNETi377677.
    OpenTargetsiENSG00000185015.
    PharmGKBiPA134891311.

    Chemistry databases

    ChEMBLiCHEMBL3912.
    DrugBankiDB00909. Zonisamide.

    Polymorphism and mutation databases

    BioMutaiCA13.
    DMDMi30580350.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000774401 – 262Carbonic anhydrase 13Add BLAST262

    Proteomic databases

    EPDiQ8N1Q1.
    MaxQBiQ8N1Q1.
    PaxDbiQ8N1Q1.
    PeptideAtlasiQ8N1Q1.
    PRIDEiQ8N1Q1.

    2D gel databases

    OGPiQ8N1Q1.

    PTM databases

    iPTMnetiQ8N1Q1.
    PhosphoSitePlusiQ8N1Q1.

    Expressioni

    Tissue specificityi

    Expressed in thymus, small intestine, spleen, prostate, ovary, colon and testis.1 Publication

    Gene expression databases

    BgeeiENSG00000185015.
    CleanExiHS_CA13.
    GenevisibleiQ8N1Q1. HS.

    Organism-specific databases

    HPAiCAB025567.
    HPA024689.

    Interactioni

    Protein-protein interaction databases

    IntActiQ8N1Q1. 1 interactor.
    STRINGi9606.ENSP00000318912.

    Chemistry databases

    BindingDBiQ8N1Q1.

    Structurei

    Secondary structure

    1262
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Turni10 – 12Combined sources3
    Helixi14 – 20Combined sources7
    Helixi22 – 25Combined sources4
    Beta strandi26 – 28Combined sources3
    Turni36 – 38Combined sources3
    Beta strandi48 – 51Combined sources4
    Beta strandi56 – 62Combined sources7
    Beta strandi64 – 71Combined sources8
    Beta strandi74 – 82Combined sources9
    Beta strandi89 – 98Combined sources10
    Beta strandi107 – 110Combined sources4
    Beta strandi116 – 125Combined sources10
    Turni126 – 128Combined sources3
    Helixi132 – 135Combined sources4
    Beta strandi141 – 151Combined sources11
    Helixi156 – 162Combined sources7
    Helixi163 – 168Combined sources6
    Beta strandi174 – 176Combined sources3
    Helixi182 – 185Combined sources4
    Beta strandi192 – 197Combined sources6
    Beta strandi208 – 215Combined sources8
    Beta strandi217 – 219Combined sources3
    Helixi221 – 227Combined sources7
    Beta strandi230 – 234Combined sources5
    Beta strandi258 – 260Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3CZVX-ray2.00A/B1-262[»]
    3D0NX-ray1.55A/B1-262[»]
    3DA2X-ray2.05A/B1-261[»]
    4HU1X-ray1.95A/B1-262[»]
    4KNMX-ray1.90A/B1-262[»]
    4KNNX-ray1.40A/B1-262[»]
    4QIZX-ray1.55A/B1-262[»]
    4QJPX-ray1.62A/B1-262[»]
    4QJXX-ray1.95A1-262[»]
    4QSJX-ray1.70A/B1-262[»]
    5E2NX-ray1.53A/B1-262[»]
    ProteinModelPortaliQ8N1Q1.
    SMRiQ8N1Q1.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8N1Q1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini4 – 261Alpha-carbonic anhydrasePROSITE-ProRule annotationAdd BLAST258

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni200 – 201Substrate bindingBy similarity2

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiKOG0382. Eukaryota.
    COG3338. LUCA.
    GeneTreeiENSGT00760000118915.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiQ8N1Q1.
    KOiK01672.
    OMAiLQIGEPN.
    OrthoDBiEOG091G0XFM.
    PhylomeDBiQ8N1Q1.
    TreeFamiTF316425.

    Family and domain databases

    Gene3Di3.10.200.10. 1 hit.
    InterProiIPR001148. Carbonic_anhydrase_a.
    IPR023561. Carbonic_anhydrase_a-class.
    IPR018338. Carbonic_anhydrase_a-class_CS.
    [Graphical view]
    PANTHERiPTHR18952. PTHR18952. 1 hit.
    PfamiPF00194. Carb_anhydrase. 1 hit.
    [Graphical view]
    SMARTiSM01057. Carb_anhydrase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51069. SSF51069. 1 hit.
    PROSITEiPS00162. ALPHA_CA_1. 1 hit.
    PS51144. ALPHA_CA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8N1Q1-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSRLSWGYRE HNGPIHWKEF FPIADGDQQS PIEIKTKEVK YDSSLRPLSI
    60 70 80 90 100
    KYDPSSAKII SNSGHSFNVD FDDTENKSVL RGGPLTGSYR LRQVHLHWGS
    110 120 130 140 150
    ADDHGSEHIV DGVSYAAELH VVHWNSDKYP SFVEAAHEPD GLAVLGVFLQ
    160 170 180 190 200
    IGEPNSQLQK ITDTLDSIKE KGKQTRFTNF DLLSLLPPSW DYWTYPGSLT
    210 220 230 240 250
    VPPLLESVTW IVLKQPINIS SQQLAKFRSL LCTAEGEAAA FLVSNHRPPQ
    260
    PLKGRKVRAS FH
    Length:262
    Mass (Da):29,443
    Last modified:October 1, 2002 - v1
    Checksum:iAE677F028ED729FE
    GO

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_05920768N → S.Corresponds to variant rs4740046dbSNPEnsembl.1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK095314 mRNA. Translation: BAC04528.1.
    BC052602 mRNA. Translation: AAH52602.1.
    CCDSiCCDS6236.1.
    RefSeqiNP_940986.1. NM_198584.2.
    UniGeneiHs.127189.

    Genome annotation databases

    EnsembliENST00000321764; ENSP00000318912; ENSG00000185015.
    GeneIDi377677.
    KEGGihsa:377677.
    UCSCiuc003ydg.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK095314 mRNA. Translation: BAC04528.1.
    BC052602 mRNA. Translation: AAH52602.1.
    CCDSiCCDS6236.1.
    RefSeqiNP_940986.1. NM_198584.2.
    UniGeneiHs.127189.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3CZVX-ray2.00A/B1-262[»]
    3D0NX-ray1.55A/B1-262[»]
    3DA2X-ray2.05A/B1-261[»]
    4HU1X-ray1.95A/B1-262[»]
    4KNMX-ray1.90A/B1-262[»]
    4KNNX-ray1.40A/B1-262[»]
    4QIZX-ray1.55A/B1-262[»]
    4QJPX-ray1.62A/B1-262[»]
    4QJXX-ray1.95A1-262[»]
    4QSJX-ray1.70A/B1-262[»]
    5E2NX-ray1.53A/B1-262[»]
    ProteinModelPortaliQ8N1Q1.
    SMRiQ8N1Q1.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiQ8N1Q1. 1 interactor.
    STRINGi9606.ENSP00000318912.

    Chemistry databases

    BindingDBiQ8N1Q1.
    ChEMBLiCHEMBL3912.
    DrugBankiDB00909. Zonisamide.

    PTM databases

    iPTMnetiQ8N1Q1.
    PhosphoSitePlusiQ8N1Q1.

    Polymorphism and mutation databases

    BioMutaiCA13.
    DMDMi30580350.

    2D gel databases

    OGPiQ8N1Q1.

    Proteomic databases

    EPDiQ8N1Q1.
    MaxQBiQ8N1Q1.
    PaxDbiQ8N1Q1.
    PeptideAtlasiQ8N1Q1.
    PRIDEiQ8N1Q1.

    Protocols and materials databases

    DNASUi377677.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000321764; ENSP00000318912; ENSG00000185015.
    GeneIDi377677.
    KEGGihsa:377677.
    UCSCiuc003ydg.3. human.

    Organism-specific databases

    CTDi377677.
    DisGeNETi377677.
    GeneCardsiCA13.
    HGNCiHGNC:14914. CA13.
    HPAiCAB025567.
    HPA024689.
    MIMi611436. gene.
    neXtProtiNX_Q8N1Q1.
    OpenTargetsiENSG00000185015.
    PharmGKBiPA134891311.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG0382. Eukaryota.
    COG3338. LUCA.
    GeneTreeiENSGT00760000118915.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiQ8N1Q1.
    KOiK01672.
    OMAiLQIGEPN.
    OrthoDBiEOG091G0XFM.
    PhylomeDBiQ8N1Q1.
    TreeFamiTF316425.

    Enzyme and pathway databases

    BioCyciZFISH:G66-32297-MONOMER.
    ReactomeiR-HSA-1475029. Reversible hydration of carbon dioxide.

    Miscellaneous databases

    ChiTaRSiCA13. human.
    EvolutionaryTraceiQ8N1Q1.
    GenomeRNAii377677.
    PROiQ8N1Q1.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000185015.
    CleanExiHS_CA13.
    GenevisibleiQ8N1Q1. HS.

    Family and domain databases

    Gene3Di3.10.200.10. 1 hit.
    InterProiIPR001148. Carbonic_anhydrase_a.
    IPR023561. Carbonic_anhydrase_a-class.
    IPR018338. Carbonic_anhydrase_a-class_CS.
    [Graphical view]
    PANTHERiPTHR18952. PTHR18952. 1 hit.
    PfamiPF00194. Carb_anhydrase. 1 hit.
    [Graphical view]
    SMARTiSM01057. Carb_anhydrase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51069. SSF51069. 1 hit.
    PROSITEiPS00162. ALPHA_CA_1. 1 hit.
    PS51144. ALPHA_CA_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiCAH13_HUMAN
    AccessioniPrimary (citable) accession number: Q8N1Q1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 9, 2003
    Last sequence update: October 1, 2002
    Last modified: November 30, 2016
    This is version 128 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 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    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.