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Q9Y2D0

- CAH5B_HUMAN

UniProt

Q9Y2D0 - CAH5B_HUMAN

Protein

Carbonic anhydrase 5B, mitochondrial

Gene

CA5B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      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 coumarins, sulfonamide derivatives such as acetazolamide (AZA), saccharin and Foscarnet (phosphonoformate trisodium salt).4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi130 – 1301Zinc; catalyticBy similarity
    Metal bindingi132 – 1321Zinc; catalyticBy similarity
    Metal bindingi155 – 1551Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. carbonate dehydratase activity Source: ProtInc
    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. 2681.
    ReactomeiREACT_121123. Reversible hydration of carbon dioxide.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbonic anhydrase 5B, mitochondrial (EC:4.2.1.1)
    Alternative name(s):
    Carbonate dehydratase VB
    Carbonic anhydrase VB
    Short name:
    CA-VB
    Gene namesi
    Name:CA5B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:1378. CA5B.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome
    2. mitochondrion Source: ProtInc

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25993.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3333MitochondrionAdd
    BLAST
    Chaini34 – 317284Carbonic anhydrase 5B, mitochondrialPRO_0000004237Add
    BLAST

    Proteomic databases

    PaxDbiQ9Y2D0.
    PRIDEiQ9Y2D0.

    PTM databases

    PhosphoSiteiQ9Y2D0.

    Expressioni

    Tissue specificityi

    Strongest expression in heart, pancreas, kidney, placenta, lung, and skeletal muscle. Not expressed in liver.

    Gene expression databases

    ArrayExpressiQ9Y2D0.
    BgeeiQ9Y2D0.
    CleanExiHS_CA5B.
    GenevestigatoriQ9Y2D0.

    Organism-specific databases

    HPAiHPA012618.

    Interactioni

    Protein-protein interaction databases

    BioGridi116403. 1 interaction.
    STRINGi9606.ENSP00000314099.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y2D0.
    SMRiQ9Y2D0. Positions 61-297.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni235 – 2362Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the alpha-carbonic anhydrase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG3338.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiQ9Y2D0.
    KOiK01672.
    OMAiIKHKDTL.
    PhylomeDBiQ9Y2D0.
    TreeFamiTF316425.

    Family and domain databases

    Gene3Di3.10.200.10. 1 hit.
    InterProiIPR018437. CA-VB_mt.
    IPR001148. Carbonic_anhydrase_a.
    IPR023561. Carbonic_anhydrase_a-class.
    IPR018338. Carbonic_anhydrase_a-class_CS.
    [Graphical view]
    PANTHERiPTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF25. PTHR18952:SF25. 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.

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

    Q9Y2D0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVVMNSLRVI LQASPGKLLW RKFQIPRFMP ARPCSLYTCT YKTRNRALHP    50
    LWESVDLVPG GDRQSPINIR WRDSVYDPGL KPLTISYDPA TCLHVWNNGY 100
    SFLVEFEDST DKSVIKGGPL EHNYRLKQFH FHWGAIDAWG SEHTVDSKCF 150
    PAELHLVHWN AVRFENFEDA ALEENGLAVI GVFLKLGKHH KELQKLVDTL 200
    PSIKHKDALV EFGSFDPSCL MPTCPDYWTY SGSLTTPPLS ESVTWIIKKQ 250
    PVEVDHDQLE QFRTLLFTSE GEKEKRMVDN FRPLQPLMNR TVRSSFRHDY 300
    VLNVQAKPKP ATSQATP 317
    Length:317
    Mass (Da):36,434
    Last modified:November 1, 1999 - v1
    Checksum:i7CA11920EFF2588A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB021660 mRNA. Translation: BAA76671.1.
    AK291050 mRNA. Translation: BAF83739.1.
    CH471074 Genomic DNA. Translation: EAW98897.1.
    BC028142 mRNA. Translation: AAH28142.1.
    CCDSiCCDS14171.1.
    RefSeqiNP_009151.1. NM_007220.3.
    XP_005274499.1. XM_005274442.2.
    UniGeneiHs.653287.

    Genome annotation databases

    EnsembliENST00000318636; ENSP00000314099; ENSG00000169239.
    ENST00000454127; ENSP00000417021; ENSG00000169239.
    GeneIDi11238.
    KEGGihsa:11238.
    UCSCiuc004cxe.3. human.

    Polymorphism databases

    DMDMi8928041.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB021660 mRNA. Translation: BAA76671.1 .
    AK291050 mRNA. Translation: BAF83739.1 .
    CH471074 Genomic DNA. Translation: EAW98897.1 .
    BC028142 mRNA. Translation: AAH28142.1 .
    CCDSi CCDS14171.1.
    RefSeqi NP_009151.1. NM_007220.3.
    XP_005274499.1. XM_005274442.2.
    UniGenei Hs.653287.

    3D structure databases

    ProteinModelPortali Q9Y2D0.
    SMRi Q9Y2D0. Positions 61-297.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116403. 1 interaction.
    STRINGi 9606.ENSP00000314099.

    Chemistry

    BindingDBi Q9Y2D0.
    ChEMBLi CHEMBL3969.

    PTM databases

    PhosphoSitei Q9Y2D0.

    Polymorphism databases

    DMDMi 8928041.

    Proteomic databases

    PaxDbi Q9Y2D0.
    PRIDEi Q9Y2D0.

    Protocols and materials databases

    DNASUi 11238.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000318636 ; ENSP00000314099 ; ENSG00000169239 .
    ENST00000454127 ; ENSP00000417021 ; ENSG00000169239 .
    GeneIDi 11238.
    KEGGi hsa:11238.
    UCSCi uc004cxe.3. human.

    Organism-specific databases

    CTDi 11238.
    GeneCardsi GC0XP015706.
    HGNCi HGNC:1378. CA5B.
    HPAi HPA012618.
    MIMi 300230. gene.
    neXtProti NX_Q9Y2D0.
    PharmGKBi PA25993.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3338.
    HOGENOMi HOG000112637.
    HOVERGENi HBG002837.
    InParanoidi Q9Y2D0.
    KOi K01672.
    OMAi IKHKDTL.
    PhylomeDBi Q9Y2D0.
    TreeFami TF316425.

    Enzyme and pathway databases

    BRENDAi 4.2.1.1. 2681.
    Reactomei REACT_121123. Reversible hydration of carbon dioxide.

    Miscellaneous databases

    GeneWikii CA5B.
    GenomeRNAii 11238.
    NextBioi 42774.
    PROi Q9Y2D0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y2D0.
    Bgeei Q9Y2D0.
    CleanExi HS_CA5B.
    Genevestigatori Q9Y2D0.

    Family and domain databases

    Gene3Di 3.10.200.10. 1 hit.
    InterProi IPR018437. CA-VB_mt.
    IPR001148. Carbonic_anhydrase_a.
    IPR023561. Carbonic_anhydrase_a-class.
    IPR018338. Carbonic_anhydrase_a-class_CS.
    [Graphical view ]
    PANTHERi PTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF25. PTHR18952:SF25. 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. "Human mitochondrial carbonic anhydrase VB: cDNA cloning, mRNA expression, subcellular localization, and mapping to chromosome X."
      Fujikawa-Adachi K., Nishimori I., Taguchi T., Onishi S.
      J. Biol. Chem. 274:21228-21233(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
      Tissue: Pancreas.
    2. "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].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Blood.
    5. "Saccharin inhibits carbonic anhydrases: possible explanation for its unpleasant metallic aftertaste."
      Koehler K., Hillebrecht A., Schulze Wischeler J., Innocenti A., Heine A., Supuran C.T., Klebe G.
      Angew. Chem. Int. Ed. Engl. 46:7697-7699(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    6. "Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-ray crystal structure of the antiviral drug foscarnet complexed to human carbonic anhydrase I."
      Temperini C., Innocenti A., Guerri A., Scozzafava A., Rusconi S., Supuran C.T.
      Bioorg. Med. Chem. Lett. 17:2210-2215(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    7. "A thiabendazole sulfonamide shows potent inhibitory activity against mammalian and nematode alpha-carbonic anhydrases."
      Crocetti L., Maresca A., Temperini C., Hall R.A., Scozzafava A., Muehlschlegel F.A., Supuran C.T.
      Bioorg. Med. Chem. Lett. 19:1371-1375(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    8. "Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new class of suicide inhibitors."
      Maresca A., Temperini C., Vu H., Pham N.B., Poulsen S.-A., Scozzafava A., Quinn R.J., Supuran C.T.
      J. Am. Chem. Soc. 131:3057-3062(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.

    Entry informationi

    Entry nameiCAH5B_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y2D0
    Secondary accession number(s): A8K4T5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 122 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3