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Q8N1Q1

- CAH13_HUMAN

UniProt

Q8N1Q1 - CAH13_HUMAN

Protein

Carbonic anhydrase 13

Gene

CA13

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
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    Functioni

    Reversible hydration of carbon dioxide.

    Catalytic activityi

    H2CO3 = CO2 + H2O.

    Cofactori

    Zinc.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

    1. carbonate dehydratase activity Source: UniProtKB-EC
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. bicarbonate transport Source: Reactome
    2. one-carbon metabolic process Source: InterPro
    3. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi4.2.1.1. 3474.
    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: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:14914. CA13.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134891311.

    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 – 123
    Helixi14 – 207
    Helixi22 – 254
    Beta strandi26 – 283
    Turni36 – 383
    Beta strandi48 – 514
    Beta strandi56 – 627
    Beta strandi64 – 718
    Beta strandi74 – 829
    Beta strandi89 – 9810
    Beta strandi107 – 1104
    Beta strandi116 – 12510
    Turni126 – 1283
    Helixi132 – 1354
    Beta strandi141 – 15111
    Helixi156 – 1627
    Helixi163 – 1686
    Beta strandi174 – 1763
    Helixi182 – 1854
    Beta strandi192 – 1976
    Beta strandi208 – 2158
    Beta strandi217 – 2193
    Helixi221 – 2277
    Beta strandi230 – 2345
    Beta strandi258 – 2603

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    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.
    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

    MSRLSWGYRE HNGPIHWKEF FPIADGDQQS PIEIKTKEVK YDSSLRPLSI    50
    KYDPSSAKII SNSGHSFNVD FDDTENKSVL RGGPLTGSYR LRQVHLHWGS 100
    ADDHGSEHIV DGVSYAAELH VVHWNSDKYP SFVEAAHEPD GLAVLGVFLQ 150
    IGEPNSQLQK ITDTLDSIKE KGKQTRFTNF DLLSLLPPSW DYWTYPGSLT 200
    VPPLLESVTW IVLKQPINIS SQQLAKFRSL LCTAEGEAAA FLVSNHRPPQ 250
    PLKGRKVRAS FH 262
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi30580350.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK095314 mRNA. Translation: BAC04528.1 .
    BC052602 mRNA. Translation: AAH52602.1 .
    CCDSi CCDS6236.1.
    RefSeqi NP_940986.1. NM_198584.2.
    UniGenei Hs.127189.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3CZV X-ray 2.00 A/B 1-262 [» ]
    3D0N X-ray 1.55 A/B 1-262 [» ]
    3DA2 X-ray 2.05 A/B 1-261 [» ]
    4HU1 X-ray 1.95 A/B 1-262 [» ]
    4KNM X-ray 1.90 A/B 1-262 [» ]
    4KNN X-ray 1.40 A/B 1-262 [» ]
    ProteinModelPortali Q8N1Q1.
    SMRi Q8N1Q1. Positions 5-262.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000318912.

    Chemistry

    BindingDBi Q8N1Q1.
    ChEMBLi CHEMBL2095180.

    PTM databases

    PhosphoSitei Q8N1Q1.

    Polymorphism databases

    DMDMi 30580350.

    2D gel databases

    OGPi Q8N1Q1.

    Proteomic databases

    MaxQBi Q8N1Q1.
    PaxDbi Q8N1Q1.
    PeptideAtlasi Q8N1Q1.
    PRIDEi Q8N1Q1.

    Protocols and materials databases

    DNASUi 377677.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000321764 ; ENSP00000318912 ; ENSG00000185015 .
    GeneIDi 377677.
    KEGGi hsa:377677.
    UCSCi uc003ydg.2. human.

    Organism-specific databases

    CTDi 377677.
    GeneCardsi GC08P086232.
    HGNCi HGNC:14914. CA13.
    HPAi CAB025567.
    HPA024689.
    MIMi 611436. gene.
    neXtProti NX_Q8N1Q1.
    PharmGKBi PA134891311.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3338.
    HOGENOMi HOG000112637.
    HOVERGENi HBG002837.
    InParanoidi Q8N1Q1.
    KOi K01672.
    OMAi QIGEPNS.
    OrthoDBi EOG7WMCK7.
    PhylomeDBi Q8N1Q1.
    TreeFami TF316425.

    Enzyme and pathway databases

    BRENDAi 4.2.1.1. 3474.
    Reactomei REACT_121123. Reversible hydration of carbon dioxide.

    Miscellaneous databases

    ChiTaRSi CA13. human.
    EvolutionaryTracei Q8N1Q1.
    GenomeRNAii 377677.
    NextBioi 100682.
    PROi Q8N1Q1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8N1Q1.
    CleanExi HS_CA13.
    Genevestigatori Q8N1Q1.

    Family and domain databases

    Gene3Di 3.10.200.10. 1 hit.
    InterProi IPR001148. Carbonic_anhydrase_a.
    IPR023561. Carbonic_anhydrase_a-class.
    IPR018338. Carbonic_anhydrase_a-class_CS.
    [Graphical view ]
    PANTHERi PTHR18952. PTHR18952. 1 hit.
    Pfami PF00194. Carb_anhydrase. 1 hit.
    [Graphical view ]
    SMARTi SM01057. Carb_anhydrase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51069. SSF51069. 1 hit.
    PROSITEi PS00162. ALPHA_CA_1. 1 hit.
    PS51144. ALPHA_CA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 111 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