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Q9QZA0

- CAH5B_MOUSE

UniProt

Q9QZA0 - CAH5B_MOUSE

Protein

Carbonic anhydrase 5B, mitochondrial

Gene

Ca5b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 2 (09 May 2003)
      Previous versions | rss
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    Functioni

    Reversible hydration of carbon dioxide.

    Catalytic activityi

    H2CO3 = CO2 + H2O.

    Cofactori

    Zinc.By similarity

    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: MGI
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. one-carbon metabolic process Source: InterPro

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_199096. 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
    Synonyms:Car5b
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:1926249. Car5b.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3333MitochondrionBy similarityAdd
    BLAST
    Chaini34 – 317284Carbonic anhydrase 5B, mitochondrialPRO_0000004238Add
    BLAST

    Proteomic databases

    MaxQBiQ9QZA0.
    PaxDbiQ9QZA0.
    PRIDEiQ9QZA0.

    PTM databases

    PhosphoSiteiQ9QZA0.

    Expressioni

    Gene expression databases

    BgeeiQ9QZA0.
    CleanExiMM_CAR5B.
    GenevestigatoriQ9QZA0.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9QZA0.
    SMRiQ9QZA0. 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.
    GeneTreeiENSGT00750000117305.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiQ9QZA0.
    KOiK01672.
    OMAiIKHKDTL.
    OrthoDBiEOG7WMCK7.
    PhylomeDBiQ9QZA0.
    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.

    Q9QZA0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVMNHLRVI LQVSSSTLPW RRCWVPRLVP RRSCSLYTCT YRTRNRALPP    50
    LWENLDLVPA GDRQSPINIR WRDSVYDPGL KPLTISYDPA TCLHIWNNGY 100
    SFLVEFEDST DKSVVEGGPL EHNYRLKQFH FHWGAIDAWG SEHTVDSKCY 150
    PAELHLVHWN AVKFESFEDA ALEENGLAVI GVFLKLGKHH KELQKLVDTL 200
    PSIKHKDTLV EFGSFDPSCL MPTCPDYWTY SGSLTTPPLS ESVTWIIKKQ 250
    PVEVDRDQLE QFRTLLFTSE GEKEKRMVDN FRPLQPLMNR TVRSSFRHDY 300
    VLNIQVKPKP TASEVTP 317
    Length:317
    Mass (Da):36,623
    Last modified:May 9, 2003 - v2
    Checksum:i719016A75305BFD3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti269 – 2691S → F in BAC39501. (PubMed:16141072)Curated
    Sequence conflicti308 – 3081P → A in AAF08291. (PubMed:10677517)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF192978 mRNA. Translation: AAF08291.1.
    AK085670 mRNA. Translation: BAC39501.1.
    BC034413 mRNA. Translation: AAH34413.1.
    CCDSiCCDS30515.1.
    RefSeqiNP_851832.2. NM_181315.4.
    UniGeneiMm.180953.

    Genome annotation databases

    EnsembliENSMUST00000033739; ENSMUSP00000033739; ENSMUSG00000031373.
    GeneIDi56078.
    KEGGimmu:56078.
    UCSCiuc009uvb.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF192978 mRNA. Translation: AAF08291.1 .
    AK085670 mRNA. Translation: BAC39501.1 .
    BC034413 mRNA. Translation: AAH34413.1 .
    CCDSi CCDS30515.1.
    RefSeqi NP_851832.2. NM_181315.4.
    UniGenei Mm.180953.

    3D structure databases

    ProteinModelPortali Q9QZA0.
    SMRi Q9QZA0. Positions 61-297.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q9QZA0.

    Proteomic databases

    MaxQBi Q9QZA0.
    PaxDbi Q9QZA0.
    PRIDEi Q9QZA0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033739 ; ENSMUSP00000033739 ; ENSMUSG00000031373 .
    GeneIDi 56078.
    KEGGi mmu:56078.
    UCSCi uc009uvb.2. mouse.

    Organism-specific databases

    CTDi 56078.
    MGIi MGI:1926249. Car5b.

    Phylogenomic databases

    eggNOGi COG3338.
    GeneTreei ENSGT00750000117305.
    HOGENOMi HOG000112637.
    HOVERGENi HBG002837.
    InParanoidi Q9QZA0.
    KOi K01672.
    OMAi IKHKDTL.
    OrthoDBi EOG7WMCK7.
    PhylomeDBi Q9QZA0.
    TreeFami TF316425.

    Enzyme and pathway databases

    Reactomei REACT_199096. Reversible hydration of carbon dioxide.

    Miscellaneous databases

    NextBioi 311872.
    PROi Q9QZA0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9QZA0.
    CleanExi MM_CAR5B.
    Genevestigatori Q9QZA0.

    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. "Mitochondrial carbonic anhydrase CA VB: differences in tissue distribution and pattern of evolution from those of CA VA suggest distinct physiological roles."
      Shah G.N., Hewett-Emmett D., Grubb J.H., Migas M.C., Fleming R.E., Waheed A., Sly W.S.
      Proc. Natl. Acad. Sci. U.S.A. 97:1677-1682(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Kidney.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Mammary gland.
    3. "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: Kidney.

    Entry informationi

    Entry nameiCAH5B_MOUSE
    AccessioniPrimary (citable) accession number: Q9QZA0
    Secondary accession number(s): Q8C3J9, Q8K014
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 9, 2003
    Last modified: October 1, 2014
    This is version 112 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3