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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+By similarity

Enzyme regulationi

Inhibited by acetazolamide.1 Publication

Kineticsi

  1. KM=13.8 mM for CO21 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei65 – 651Proton acceptorBy similarity
    Active sitei68 – 681By similarity
    Metal bindingi95 – 951Zinc; catalytic
    Metal bindingi97 – 971Zinc; catalytic
    Metal bindingi120 – 1201Zinc; catalytic
    Active sitei129 – 1291By similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_121123. 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
    ProteomesiUP000005640 Componenti: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:14914. CA13.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134891311.

    Chemistry

    DrugBankiDB00909. Zonisamide.

    Polymorphism and mutation databases

    BioMutaiCA13.
    DMDMi30580350.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 262262Carbonic anhydrase 13PRO_0000077440Add
    BLAST

    Proteomic databases

    MaxQBiQ8N1Q1.
    PaxDbiQ8N1Q1.
    PeptideAtlasiQ8N1Q1.
    PRIDEiQ8N1Q1.

    2D gel databases

    OGPiQ8N1Q1.

    PTM databases

    PhosphoSiteiQ8N1Q1.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    BgeeiQ8N1Q1.
    CleanExiHS_CA13.
    GenevestigatoriQ8N1Q1.

    Organism-specific databases

    HPAiCAB025567.
    HPA024689.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000318912.

    Structurei

    Secondary structure

    1
    262
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni10 – 123Combined sources
    Helixi14 – 207Combined sources
    Helixi22 – 254Combined sources
    Beta strandi26 – 283Combined sources
    Turni36 – 383Combined sources
    Beta strandi48 – 514Combined sources
    Beta strandi56 – 627Combined sources
    Beta strandi64 – 718Combined sources
    Beta strandi74 – 829Combined sources
    Beta strandi89 – 9810Combined sources
    Beta strandi107 – 1104Combined sources
    Beta strandi116 – 12510Combined sources
    Turni126 – 1283Combined sources
    Helixi132 – 1354Combined sources
    Beta strandi141 – 15111Combined sources
    Helixi156 – 1627Combined sources
    Helixi163 – 1686Combined sources
    Beta strandi174 – 1763Combined sources
    Helixi182 – 1854Combined sources
    Beta strandi192 – 1976Combined sources
    Beta strandi208 – 2158Combined sources
    Beta strandi217 – 2193Combined sources
    Helixi221 – 2277Combined sources
    Beta strandi230 – 2345Combined sources
    Beta strandi258 – 2603Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    4QSJX-ray1.70A/B1-262[»]
    ProteinModelPortaliQ8N1Q1.
    SMRiQ8N1Q1. Positions 5-262.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8N1Q1.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni200 – 2012Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the alpha-carbonic anhydrase family.Curated

    Phylogenomic databases

    eggNOGiCOG3338.
    GeneTreeiENSGT00760000118915.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiQ8N1Q1.
    KOiK01672.
    OMAiQIGEPNS.
    OrthoDBiEOG7WMCK7.
    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)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti68 – 681N → S.
    Corresponds to variant rs4740046 [ dbSNP | Ensembl ].
    VAR_059207

    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.2. 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
    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[»]
    4QSJX-ray1.70A/B1-262[»]
    ProteinModelPortaliQ8N1Q1.
    SMRiQ8N1Q1. Positions 5-262.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi9606.ENSP00000318912.

    Chemistry

    BindingDBiQ8N1Q1.
    ChEMBLiCHEMBL2095180.
    DrugBankiDB00909. Zonisamide.

    PTM databases

    PhosphoSiteiQ8N1Q1.

    Polymorphism and mutation databases

    BioMutaiCA13.
    DMDMi30580350.

    2D gel databases

    OGPiQ8N1Q1.

    Proteomic databases

    MaxQBiQ8N1Q1.
    PaxDbiQ8N1Q1.
    PeptideAtlasiQ8N1Q1.
    PRIDEiQ8N1Q1.

    Protocols and materials databases

    DNASUi377677.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000321764; ENSP00000318912; ENSG00000185015.
    GeneIDi377677.
    KEGGihsa:377677.
    UCSCiuc003ydg.2. human.

    Organism-specific databases

    CTDi377677.
    GeneCardsiGC08P086232.
    HGNCiHGNC:14914. CA13.
    HPAiCAB025567.
    HPA024689.
    MIMi611436. gene.
    neXtProtiNX_Q8N1Q1.
    PharmGKBiPA134891311.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG3338.
    GeneTreeiENSGT00760000118915.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiQ8N1Q1.
    KOiK01672.
    OMAiQIGEPNS.
    OrthoDBiEOG7WMCK7.
    PhylomeDBiQ8N1Q1.
    TreeFamiTF316425.

    Enzyme and pathway databases

    ReactomeiREACT_121123. Reversible hydration of carbon dioxide.

    Miscellaneous databases

    ChiTaRSiCA13. human.
    EvolutionaryTraceiQ8N1Q1.
    GenomeRNAii377677.
    NextBioi100682.
    PROiQ8N1Q1.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ8N1Q1.
    CleanExiHS_CA13.
    GenevestigatoriQ8N1Q1.

    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...

    Publicationsi

    « Hide 'large scale' publications
    1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Tongue.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Pancreas.
    3. Cited for: CHARACTERIZATION, TISSUE SPECIFICITY.
    4. "Crystal structure of human carbonic anhydrase XIII and its complex with the inhibitor acetazolamide."
      Di Fiore A., Monti S.M., Hilvo M., Parkkila S., Romano V., Scaloni A., Pedone C., Scozzafava A., Supuran C.T., De Simone G.
      Proteins 74:164-175(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR ACETAZOLAMIDE, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    5. "X-ray structure of human carbonic anhydrase 13 in complex with inhibitor."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1-261 IN COMPLEX WITH INHIBITOR.

    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: April 29, 2015
    This is version 116 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

    External Data

    Dasty 3

    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 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.