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P23589

- CAH5A_MOUSE

UniProt

P23589 - CAH5A_MOUSE

Protein

Carbonic anhydrase 5A, mitochondrial

Gene

Ca5a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Reversible hydration of carbon dioxide. Low activity.

    Catalytic activityi

    H2CO3 = CO2 + H2O.

    Cofactori

    Zinc.

    Enzyme regulationi

    Inhibited by acetazolamide.By similarity

    pH dependencei

    Optimum pH is 7-8.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei94 – 941Curated
    Metal bindingi124 – 1241Zinc; catalytic
    Metal bindingi126 – 1261Zinc; catalytic
    Metal bindingi149 – 1491Zinc; catalytic
    Active sitei158 – 1581By similarity
    Active sitei161 – 1611Curated

    GO - Molecular functioni

    1. carbonate dehydratase activity Source: MGI
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. gluconeogenesis Source: MGI
    2. 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 5A, mitochondrial (EC:4.2.1.1)
    Alternative name(s):
    Carbonate dehydratase VA
    Short name:
    CA Y
    Carbonic anhydrase VA
    Short name:
    CA-VA
    Gene namesi
    Name:Ca5a
    Synonyms:Ca5, Car5, Car5a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:101946. Car5a.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi94 – 941Y → A: Normal activity. 2 Publications
    Mutagenesisi94 – 941Y → H: Normal activity. Enhanced proton transfer due to removal of the steric hindrance of F-95; when associated with A-95. 2 Publications
    Mutagenesisi95 – 951F → A: Normal activity. Enhanced proton transfer; when associated with H-94 or C-161. 3 Publications
    Mutagenesisi121 – 1211K → C: Normal activity. 1 Publication
    Mutagenesisi161 – 1611Y → A: Normal activity. 3 Publications
    Mutagenesisi161 – 1611Y → C: Normal activity. Enhanced proton transfer; when associated with A-95. 3 Publications
    Mutagenesisi161 – 1611Y → H: Normal activity. 3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2929Mitochondrion1 PublicationAdd
    BLAST
    Chaini30 – 299270Carbonic anhydrase 5A, mitochondrialPRO_0000004235Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei66 – 661N6-succinyllysine1 Publication

    Proteomic databases

    MaxQBiP23589.
    PaxDbiP23589.
    PRIDEiP23589.

    PTM databases

    PhosphoSiteiP23589.

    Expressioni

    Tissue specificityi

    Liver.

    Gene expression databases

    BgeeiP23589.
    CleanExiMM_CAR5A.
    GenevestigatoriP23589.

    Interactioni

    Protein-protein interaction databases

    IntActiP23589. 1 interaction.
    MINTiMINT-4089763.

    Structurei

    Secondary structure

    1
    299
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi65 – 673
    Beta strandi68 – 703
    Beta strandi75 – 806
    Helixi83 – 853
    Beta strandi86 – 916
    Beta strandi93 – 1008
    Beta strandi104 – 1129
    Beta strandi118 – 12710
    Beta strandi136 – 1394
    Beta strandi145 – 15410
    Turni155 – 1573
    Helixi161 – 1644
    Beta strandi171 – 18212
    Helixi185 – 1917
    Helixi192 – 1965
    Beta strandi203 – 2053
    Helixi211 – 2144
    Beta strandi221 – 2266
    Beta strandi237 – 2448
    Beta strandi246 – 2483
    Helixi250 – 2567
    Beta strandi260 – 2623
    Beta strandi264 – 2663
    Beta strandi286 – 2905

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DMXX-ray2.45A/B53-299[»]
    1DMYX-ray2.45A/B53-299[»]
    1KEQX-ray1.88A/B53-299[»]
    1URTX-ray2.80A52-299[»]
    ProteinModelPortaliP23589.
    SMRiP23589. Positions 55-290.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23589.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni229 – 2302Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the alpha-carbonic anhydrase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG3338.
    GeneTreeiENSGT00750000117305.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiP23589.
    KOiK01672.
    OMAiFFQVEFD.
    OrthoDBiEOG7WMCK7.
    PhylomeDBiP23589.
    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.

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

    P23589-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRRDPRKPL AILRHVGLLC ATGPQRWRFQ HSCAEEHSNC ARHPLWTGPV    50
    SSAEGTRQSP INIQWKDSVY DPQLAPLRVS YDAASCRYLW NTGYFFQVEF 100
    DDSCEDSGIS GGPLGNHYRL KQFHFHWGAT DEWGSEHAVD GHTYPAELHL 150
    VHWNSTKYEN YKKASVGENG LAVIGVFLKL GAHHQALQKL VDVLPEVRHK 200
    DTQVAMGPFD PSCLLPACRD YWTYPGSLTT PPLAESVTWI VQKTPVEVSP 250
    SQLSTFRTLL FSGRGEEEDV MVNNYRPLQP LRDRKLRSSF RLDRTKMRS 299
    Length:299
    Mass (Da):34,072
    Last modified:November 1, 1995 - v2
    Checksum:i2698CABA00686151
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti151 – 1533VHW → FM in strain: BIO-HTT.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51971 mRNA. Translation: CAA36233.1.
    BC030174 mRNA. Translation: AAH30174.1.
    CCDSiCCDS22731.1.
    PIRiS12579.
    RefSeqiNP_031634.2. NM_007608.2.
    UniGeneiMm.116761.

    Genome annotation databases

    EnsembliENSMUST00000057653; ENSMUSP00000060457; ENSMUSG00000025317.
    GeneIDi12352.
    KEGGimmu:12352.
    UCSCiuc009nsf.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51971 mRNA. Translation: CAA36233.1 .
    BC030174 mRNA. Translation: AAH30174.1 .
    CCDSi CCDS22731.1.
    PIRi S12579.
    RefSeqi NP_031634.2. NM_007608.2.
    UniGenei Mm.116761.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DMX X-ray 2.45 A/B 53-299 [» ]
    1DMY X-ray 2.45 A/B 53-299 [» ]
    1KEQ X-ray 1.88 A/B 53-299 [» ]
    1URT X-ray 2.80 A 52-299 [» ]
    ProteinModelPortali P23589.
    SMRi P23589. Positions 55-290.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P23589. 1 interaction.
    MINTi MINT-4089763.

    Chemistry

    BindingDBi P23589.

    PTM databases

    PhosphoSitei P23589.

    Proteomic databases

    MaxQBi P23589.
    PaxDbi P23589.
    PRIDEi P23589.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000057653 ; ENSMUSP00000060457 ; ENSMUSG00000025317 .
    GeneIDi 12352.
    KEGGi mmu:12352.
    UCSCi uc009nsf.2. mouse.

    Organism-specific databases

    CTDi 12352.
    MGIi MGI:101946. Car5a.

    Phylogenomic databases

    eggNOGi COG3338.
    GeneTreei ENSGT00750000117305.
    HOGENOMi HOG000112637.
    HOVERGENi HBG002837.
    InParanoidi P23589.
    KOi K01672.
    OMAi FFQVEFD.
    OrthoDBi EOG7WMCK7.
    PhylomeDBi P23589.
    TreeFami TF316425.

    Enzyme and pathway databases

    Reactomei REACT_199096. Reversible hydration of carbon dioxide.

    Miscellaneous databases

    EvolutionaryTracei P23589.
    NextBioi 281008.
    PROi P23589.
    SOURCEi Search...

    Gene expression databases

    Bgeei P23589.
    CleanExi MM_CAR5A.
    Genevestigatori P23589.

    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. "Nucleotide and derived amino-acid sequence of a cDNA encoding a new mouse carbonic anhydrase."
      Amor-Gueret M., Levi-Strauss M.
      Nucleic Acids Res. 18:1646-1646(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BIO-HTT.
      Tissue: Liver.
    2. "Mitochondrial carbonic anhydrase (isozyme V) in mouse and rat: cDNA cloning, expression, subcellular localization, processing, and tissue distribution."
      Nagao Y., Srinivasan M., Platero J.S., Svendrowski M., Waheed A., Sly W.S.
      Proc. Natl. Acad. Sci. U.S.A. 91:10330-10334(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 30-41.
      Tissue: Liver.
    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].
      Strain: FVB/N.
      Tissue: Liver.
    4. "Introduction of histidine analogs leads to enhanced proton transfer in carbonic anhydrase V."
      Earnhardt J.N., Wright S.K., Qian M., Tu C., Laipis P.J., Viola R.E., Silverman D.N.
      Arch. Biochem. Biophys. 361:264-270(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF PHE-95; LYS-121 AND TYR-161.
    5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    6. "Structure determination of murine mitochondrial carbonic anhydrase V at 2.45-A resolution: implications for catalytic proton transfer and inhibitor design."
      Boriack-Sjodin P.A., Heck R.W., Laipis P.J., Silverman D.N., Christianson D.W.
      Proc. Natl. Acad. Sci. U.S.A. 92:10949-10953(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 55-299 IN COMPLEX WITH INHIBITORS AND ZINC ION, MUTAGENESIS OF TYR-94.
    7. "Structure-based design of an intramolecular proton transfer site in murine carbonic anhydrase V."
      Heck R.W., Boriack-Sjodin P.A., Qian M., Tu C., Christianson D.W., Laipis P.J., Silverman D.N.
      Biochemistry 35:11605-11611(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 52-299 IN COMPLEX WITH ZINC ION, MUTAGENESIS OF TYR-94; PHE-95 AND TYR-161.
    8. "Crystal structure of F65A/Y131C-methylimidazole carbonic anhydrase V reveals architectural features of an engineered proton shuttle."
      Jude K.M., Wright S.K., Tu C., Silverman D.N., Viola R.E., Christianson D.W.
      Biochemistry 41:2485-2491(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 55-299 IN COMPLEX WITH INHIBITORS AND ZINC ION, MUTAGENESIS OF PHE-95 AND TYR-161.

    Entry informationi

    Entry nameiCAH5A_MOUSE
    AccessioniPrimary (citable) accession number: P23589
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 141 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3