Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q64444

- CAH4_MOUSE

UniProt

Q64444 - CAH4_MOUSE

Protein

Carbonic anhydrase 4

Gene

Ca4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Reversible hydration of carbon dioxide. May stimulate the sodium/bicarbonate transporter activity of SLC4A4 By similarity.By similarity

    Catalytic activityi

    H2CO3 = CO2 + H2O.

    Cofactori

    Zinc.

    Enzyme regulationi

    Inhibited by acetazolamide.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei87 – 871Proton acceptorBy similarity
    Metal bindingi114 – 1141Zinc; catalytic
    Metal bindingi116 – 1161Zinc; catalytic
    Metal bindingi139 – 1391Zinc; catalytic

    GO - Molecular functioni

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

    GO - Biological processi

    1. bicarbonate transport Source: Ensembl
    2. carbon dioxide transport Source: MGI
    3. one-carbon metabolic process Source: InterPro
    4. organ development Source: Ensembl
    5. regulation of pH Source: MGI
    6. response to drug Source: Ensembl
    7. response to steroid hormone Source: Ensembl

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_199094. Erythrocytes take up carbon dioxide and release oxygen.
    REACT_199096. Reversible hydration of carbon dioxide.
    REACT_199098. Erythrocytes take up oxygen and release carbon dioxide.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbonic anhydrase 4 (EC:4.2.1.1)
    Alternative name(s):
    Carbonate dehydratase IV
    Carbonic anhydrase IV
    Short name:
    CA-IV
    Gene namesi
    Name:Ca4
    Synonyms:Car4
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1096574. Car4.

    Subcellular locationi

    Cell membrane By similarity; Lipid-anchorGPI-anchor By similarity

    GO - Cellular componenti

    1. anchored component of external side of plasma membrane Source: Ensembl
    2. anchored component of plasma membrane Source: MGI
    3. apical plasma membrane Source: Ensembl
    4. brush border membrane Source: Ensembl
    5. endoplasmic reticulum-Golgi intermediate compartment Source: Ensembl
    6. membrane Source: MGI
    7. perinuclear region of cytoplasm Source: Ensembl
    8. rough endoplasmic reticulum Source: Ensembl
    9. sarcolemma Source: Ensembl
    10. sarcoplasmic reticulum Source: Ensembl
    11. secretory granule membrane Source: Ensembl
    12. trans-Golgi network Source: Ensembl
    13. transport vesicle membrane Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 277260Carbonic anhydrase 4PRO_0000004228Add
    BLAST
    Propeptidei278 – 30528Removed in mature formSequence AnalysisPRO_0000004229Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi23 ↔ 35
    Disulfide bondi45 ↔ 222
    Glycosylationi123 – 1231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi214 – 2141N-linked (GlcNAc...)Sequence Analysis
    Lipidationi277 – 2771GPI-anchor amidated serineBy similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    MaxQBiQ64444.
    PaxDbiQ64444.
    PRIDEiQ64444.

    PTM databases

    PhosphoSiteiQ64444.

    Expressioni

    Gene expression databases

    BgeeiQ64444.
    CleanExiMM_CAR4.
    GenevestigatoriQ64444.

    Interactioni

    Subunit structurei

    Interacts with SLC4A4.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Slc4a4O883432EBI-6859308,EBI-771342

    Protein-protein interaction databases

    IntActiQ64444. 2 interactions.
    MINTiMINT-4089751.

    Structurei

    Secondary structure

    1
    305
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi25 – 295
    Beta strandi30 – 334
    Helixi38 – 403
    Helixi43 – 464
    Beta strandi47 – 493
    Helixi57 – 593
    Beta strandi70 – 734
    Beta strandi78 – 847
    Beta strandi86 – 927
    Beta strandi96 – 1005
    Beta strandi108 – 11710
    Beta strandi119 – 1235
    Beta strandi125 – 1295
    Beta strandi135 – 14410
    Beta strandi156 – 16813
    Helixi171 – 1733
    Helixi174 – 1796
    Helixi180 – 1823
    Beta strandi189 – 1957
    Helixi198 – 2003
    Helixi204 – 2063
    Beta strandi210 – 2156
    Beta strandi226 – 2338
    Beta strandi235 – 2384
    Helixi239 – 24810
    Beta strandi250 – 2523
    Beta strandi275 – 2773

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZNCX-ray2.80A22-279[»]
    3ZNCX-ray2.80A22-279[»]
    ProteinModelPortaliQ64444.
    SMRiQ64444. Positions 22-279.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ64444.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni218 – 2192Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the alpha-carbonic anhydrase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3338.
    GeneTreeiENSGT00750000117527.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiQ64444.
    KOiK18246.
    OMAiKGTSRNV.
    OrthoDBiEOG7MD4QN.
    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.
    IPR018343. Carbonic_anhydrase_CA4.
    [Graphical view]
    PANTHERiPTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF95. PTHR18952:SF95. 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.

    Q64444-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQLLLALLAL AYVAPSTEDS GWCYEIQTKD PRSSCLGPEK WPGACKENQQ    50
    SPINIVTART KVNPRLTPFI LVGYDQKQQW PIKNNQHTVE MTLGGGACII 100
    GGDLPARYEA VQLHLHWSNG NDNGSEHSID GRHFAMEMHI VHKKLTSSKE 150
    DSKDKFAVLA FMIEVGDKVN KGFQPLVEAL PSISKPHSTS TVRESSLQDM 200
    LPPSTKMYTY FRYNGSLTTP NCDETVIWTV YKQPIKIHKN QFLEFSKNLY 250
    YDEDQKLNMK DNVRPLQPLG KRQVFKSHAP GQLLSLPLPT LLVPTLTCLV 300
    ANFLQ 305
    Length:305
    Mass (Da):34,351
    Last modified:November 1, 1997 - v1
    Checksum:iEEE988FF52732884
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U37091 Genomic DNA. Translation: AAC52569.1.
    BC012704 mRNA. Translation: AAH12704.1.
    CCDSiCCDS25190.1.
    RefSeqiNP_031633.1. NM_007607.2.
    UniGeneiMm.1641.

    Genome annotation databases

    EnsembliENSMUST00000103194; ENSMUSP00000099483; ENSMUSG00000000805.
    GeneIDi12351.
    KEGGimmu:12351.
    UCSCiuc007krg.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U37091 Genomic DNA. Translation: AAC52569.1 .
    BC012704 mRNA. Translation: AAH12704.1 .
    CCDSi CCDS25190.1.
    RefSeqi NP_031633.1. NM_007607.2.
    UniGenei Mm.1641.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ZNC X-ray 2.80 A 22-279 [» ]
    3ZNC X-ray 2.80 A 22-279 [» ]
    ProteinModelPortali Q64444.
    SMRi Q64444. Positions 22-279.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q64444. 2 interactions.
    MINTi MINT-4089751.

    PTM databases

    PhosphoSitei Q64444.

    Proteomic databases

    MaxQBi Q64444.
    PaxDbi Q64444.
    PRIDEi Q64444.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000103194 ; ENSMUSP00000099483 ; ENSMUSG00000000805 .
    GeneIDi 12351.
    KEGGi mmu:12351.
    UCSCi uc007krg.2. mouse.

    Organism-specific databases

    CTDi 12351.
    MGIi MGI:1096574. Car4.

    Phylogenomic databases

    eggNOGi COG3338.
    GeneTreei ENSGT00750000117527.
    HOGENOMi HOG000112637.
    HOVERGENi HBG002837.
    InParanoidi Q64444.
    KOi K18246.
    OMAi KGTSRNV.
    OrthoDBi EOG7MD4QN.
    TreeFami TF316425.

    Enzyme and pathway databases

    Reactomei REACT_199094. Erythrocytes take up carbon dioxide and release oxygen.
    REACT_199096. Reversible hydration of carbon dioxide.
    REACT_199098. Erythrocytes take up oxygen and release carbon dioxide.

    Miscellaneous databases

    EvolutionaryTracei Q64444.
    NextBioi 281004.
    PROi Q64444.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q64444.
    CleanExi MM_CAR4.
    Genevestigatori Q64444.

    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.
    IPR018343. Carbonic_anhydrase_CA4.
    [Graphical view ]
    PANTHERi PTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF95. PTHR18952:SF95. 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. "Molecular cloning of the mouse gene coding for carbonic anhydrase IV."
      Tamai S., Cody L.B., Sly W.S.
      Biochem. Genet. 34:31-43(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/SvJ.
      Tissue: Liver.
    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: Colon.
    3. "Direct extracellular interaction between carbonic anhydrase IV and the human NBC1 sodium/bicarbonate co-transporter."
      Alvarez B.V., Loiselle F.B., Supuran C.T., Schwartz G.J., Casey J.R.
      Biochemistry 42:12321-12329(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLC4A4.
    4. "Structures of murine carbonic anhydrase IV and human carbonic anhydrase II complexed with brinzolamide: molecular basis of isozyme-drug discrimination."
      Stams T., Chen Y., Boriack-Sjodin P.A., Hurt J.D., Liao J., May J.A., Dean T., Laipis P., Silverman D.N., Christianson D.W.
      Protein Sci. 7:556-563(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH INHIBITOR AND ZINC ION.

    Entry informationi

    Entry nameiCAH4_MOUSE
    AccessioniPrimary (citable) accession number: Q64444
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 126 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, 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