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)

Q9WVT6

- CAH14_MOUSE

UniProt

Q9WVT6 - CAH14_MOUSE

Protein

Carbonic anhydrase 14

Gene

Ca14

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 118 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Reversible hydration of carbon dioxide.

    Catalytic activityi

    H2CO3 = CO2 + H2O.

    Cofactori

    Zinc.

    Enzyme regulationi

    Inhibited by acetazolamide.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei84 – 841Proton acceptorBy similarity
    Metal bindingi109 – 1091Zinc; catalytic
    Metal bindingi111 – 1111Zinc; catalytic
    Metal bindingi135 – 1351Zinc; catalytic
    Active sitei144 – 1441By similarity

    GO - Molecular functioni

    1. carbonate dehydratase activity Source: MGI
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. carbon dioxide transport Source: MGI
    2. metabolic process Source: GOC
    3. regulation of pH Source: MGI

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi4.2.1.1. 2605.
    ReactomeiREACT_199096. Reversible hydration of carbon dioxide.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbonic anhydrase 14 (EC:4.2.1.1)
    Alternative name(s):
    Carbonate dehydratase XIV
    Carbonic anhydrase XIV
    Short name:
    CA-XIV
    Gene namesi
    Name:Ca14
    Synonyms:Car14, Catm
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:1344341. Car14.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1515Sequence AnalysisAdd
    BLAST
    Chaini16 – 337322Carbonic anhydrase 14PRO_0000004252Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi40 ↔ 2211 Publication
    Glycosylationi213 – 2131N-linked (GlcNAc...)1 Publication
    Modified residuei325 – 3251PhosphoserineBy similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ9WVT6.
    PRIDEiQ9WVT6.

    PTM databases

    PhosphoSiteiQ9WVT6.

    Expressioni

    Tissue specificityi

    Most abundant in the kidney and heart, followed by the skeletal muscle, brain, lung and liver.

    Gene expression databases

    ArrayExpressiQ9WVT6.
    BgeeiQ9WVT6.
    CleanExiMM_CAR14.
    GenevestigatoriQ9WVT6.

    Structurei

    Secondary structure

    1
    337
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi24 – 263
    Turni30 – 323
    Helixi33 – 364
    Helixi38 – 414
    Turni52 – 543
    Beta strandi65 – 673
    Turni68 – 703
    Beta strandi77 – 815
    Beta strandi86 – 894
    Beta strandi95 – 1017
    Beta strandi103 – 11210
    Beta strandi122 – 1254
    Beta strandi131 – 14010
    Turni141 – 1433
    Helixi147 – 1504
    Beta strandi157 – 16610
    Helixi172 – 1787
    Helixi179 – 1846
    Beta strandi190 – 1934
    Helixi198 – 2014
    Beta strandi209 – 2146
    Beta strandi225 – 2328
    Beta strandi234 – 2363
    Helixi238 – 2458
    Beta strandi249 – 2557

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RJ5X-ray2.81A/B18-278[»]
    1RJ6X-ray2.90A/B18-278[»]
    ProteinModelPortaliQ9WVT6.
    SMRiQ9WVT6. Positions 20-278.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9WVT6.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini16 – 290275ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini312 – 33726CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei291 – 31121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni217 – 2182Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the alpha-carbonic anhydrase family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG3338.
    GeneTreeiENSGT00660000095420.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiQ9WVT6.
    KOiK01672.
    OMAiHWPASYP.
    OrthoDBiEOG7WMCK7.
    PhylomeDBiQ9WVT6.
    TreeFamiTF316425.

    Family and domain databases

    Gene3Di3.10.200.10. 1 hit.
    InterProiIPR001148. Carbonic_anhydrase_a.
    IPR023561. Carbonic_anhydrase_a-class.
    IPR018431. Carbonic_anhydrase_CA14.
    [Graphical view]
    PANTHERiPTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF84. PTHR18952:SF84. 1 hit.
    PfamiPF00194. Carb_anhydrase. 1 hit.
    [Graphical view]
    SMARTiSM01057. Carb_anhydrase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51069. SSF51069. 1 hit.
    PROSITEiPS51144. ALPHA_CA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9WVT6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLFFALLLKV TWILAADGGH HWTYEGPHGQ DHWPTSYPEC GGDAQSPINI    50
    QTDSVIFDPD LPAVQPHGYD QLGTEPLDLH NNGHTVQLSL PPTLHLGGLP 100
    RKYTAAQLHL HWGQRGSLEG SEHQINSEAT AAELHVVHYD SQSYSSLSEA 150
    AQKPQGLAVL GILIEVGETE NPAYDHILSR LHEIRYKDQK TSVPPFSVRE 200
    LFPQQLEQFF RYNGSLTTPP CYQSVLWTVF NRRAQISMGQ LEKLQETLSS 250
    TEEDPSEPLV QNYRVPQPLN QRTIFASFIQ AGPLYTTGEM LGLGVGILAG 300
    CLCLLLAVYF IAQKIRKKRL GNRKSVVFTS ARATTEA 337
    Length:337
    Mass (Da):37,505
    Last modified:November 1, 1999 - v1
    Checksum:i32F02F4DB78AC0C9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB005450 mRNA. Translation: BAA78709.1.
    BC046995 mRNA. Translation: AAH46995.1.
    CCDSiCCDS17625.1.
    RefSeqiNP_035927.1. NM_011797.2.
    UniGeneiMm.489647.

    Genome annotation databases

    EnsembliENSMUST00000036181; ENSMUSP00000036983; ENSMUSG00000038526.
    GeneIDi23831.
    KEGGimmu:23831.
    UCSCiuc008qls.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB005450 mRNA. Translation: BAA78709.1 .
    BC046995 mRNA. Translation: AAH46995.1 .
    CCDSi CCDS17625.1.
    RefSeqi NP_035927.1. NM_011797.2.
    UniGenei Mm.489647.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RJ5 X-ray 2.81 A/B 18-278 [» ]
    1RJ6 X-ray 2.90 A/B 18-278 [» ]
    ProteinModelPortali Q9WVT6.
    SMRi Q9WVT6. Positions 20-278.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    DrugBanki DB00819. Acetazolamide.

    PTM databases

    PhosphoSitei Q9WVT6.

    Proteomic databases

    PaxDbi Q9WVT6.
    PRIDEi Q9WVT6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000036181 ; ENSMUSP00000036983 ; ENSMUSG00000038526 .
    GeneIDi 23831.
    KEGGi mmu:23831.
    UCSCi uc008qls.1. mouse.

    Organism-specific databases

    CTDi 23831.
    MGIi MGI:1344341. Car14.

    Phylogenomic databases

    eggNOGi COG3338.
    GeneTreei ENSGT00660000095420.
    HOGENOMi HOG000112637.
    HOVERGENi HBG002837.
    InParanoidi Q9WVT6.
    KOi K01672.
    OMAi HWPASYP.
    OrthoDBi EOG7WMCK7.
    PhylomeDBi Q9WVT6.
    TreeFami TF316425.

    Enzyme and pathway databases

    BRENDAi 4.2.1.1. 2605.
    Reactomei REACT_199096. Reversible hydration of carbon dioxide.

    Miscellaneous databases

    EvolutionaryTracei Q9WVT6.
    NextBioi 303497.
    PROi Q9WVT6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9WVT6.
    Bgeei Q9WVT6.
    CleanExi MM_CAR14.
    Genevestigatori Q9WVT6.

    Family and domain databases

    Gene3Di 3.10.200.10. 1 hit.
    InterProi IPR001148. Carbonic_anhydrase_a.
    IPR023561. Carbonic_anhydrase_a-class.
    IPR018431. Carbonic_anhydrase_CA14.
    [Graphical view ]
    PANTHERi PTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF84. PTHR18952:SF84. 1 hit.
    Pfami PF00194. Carb_anhydrase. 1 hit.
    [Graphical view ]
    SMARTi SM01057. Carb_anhydrase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51069. SSF51069. 1 hit.
    PROSITEi PS51144. ALPHA_CA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of CA XIV, a novel membrane-bound carbonic anhydrase from mouse kidney."
      Mori K., Ogawa Y., Ebihara K., Tamura N., Tashiro K., Kuwahara T., Mukoyama M., Sugawara A., Ozaki S., Tanaka I., Nakao K.
      J. Biol. Chem. 274:15701-15705(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Kidney.
    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: Retina.
    3. "Expression, assay, and structure of the extracellular domain of murine carbonic anhydrase XIV: implications for selective inhibition of membrane-associated isozymes."
      Whittington D.A., Grubb J.H., Waheed A., Shah G.N., Sly W.S., Christianson D.W.
      J. Biol. Chem. 279:7223-7228(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 18-278 ALONE AND IN COMPLEX WITH ACETAZOLAMIDE, DISULFIDE BOND, ZINC-BINDING SITES, ENZYME REGULATION, GLYCOSYLATION AT ASN-213.

    Entry informationi

    Entry nameiCAH14_MOUSE
    AccessioniPrimary (citable) accession number: Q9WVT6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 118 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