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)

P14141

- CAH3_RAT

UniProt

P14141 - CAH3_RAT

Protein

Carbonic anhydrase 3

Gene

Ca3

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Reversible hydration of carbon dioxide. A major participant in the liver response to oxidative stress.

    Catalytic activityi

    H2CO3 = CO2 + H2O.

    Cofactori

    Zinc.

    Enzyme regulationi

    Inhibited by acetazolamide.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi94 – 941Zinc; catalytic
    Metal bindingi96 – 961Zinc; catalytic
    Metal bindingi119 – 1191Zinc; catalytic
    Active sitei127 – 1271By similarity

    GO - Molecular functioni

    1. carbonate dehydratase activity Source: RGD
    2. nickel cation binding Source: Ensembl
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. one-carbon metabolic process Source: InterPro
    2. response to ethanol Source: RGD
    3. response to oxidative stress Source: RGD

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi4.2.1.1. 5301.
    ReactomeiREACT_199186. Reversible hydration of carbon dioxide.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbonic anhydrase 3 (EC:4.2.1.1)
    Alternative name(s):
    Carbonate dehydratase III
    Carbonic anhydrase III
    Short name:
    CA-III
    Gene namesi
    Name:Ca3
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 2

    Organism-specific databases

    RGDi2241. Ca3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: RGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 260259Carbonic anhydrase 3PRO_0000077429Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei182 – 1821S-glutathionyl cysteine1 Publication
    Modified residuei187 – 1871S-glutathionyl cysteine1 Publication

    Post-translational modificationi

    S-thiolated both by thiol-disulfide exchange with glutathione disulfide and by oxyradical-initiated S-thiolation with reduced glutathione.1 Publication
    S-glutathionylated in hepatocytes under oxidative stress.1 Publication

    Keywords - PTMi

    Acetylation, Disulfide bond, Glutathionylation

    Proteomic databases

    PaxDbiP14141.
    PRIDEiP14141.

    PTM databases

    PhosphoSiteiP14141.

    Expressioni

    Tissue specificityi

    Expressed in liver and muscle.1 Publication

    Inductioni

    Repressed by 3,3',4,4',5-pentachlorobiphenyl (PenCB) and 3-methylchlantherene (3MC).2 Publications

    Gene expression databases

    GenevestigatoriP14141.

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-4569746.
    STRINGi10116.ENSRNOP00000014177.

    Structurei

    Secondary structure

    1
    260
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni9 – 113
    Helixi13 – 186
    Helixi21 – 244
    Beta strandi25 – 273
    Helixi35 – 373
    Beta strandi38 – 403
    Beta strandi47 – 504
    Helixi53 – 553
    Beta strandi56 – 616
    Beta strandi66 – 705
    Beta strandi73 – 819
    Beta strandi88 – 9710
    Beta strandi106 – 1094
    Beta strandi115 – 1239
    Helixi125 – 1273
    Helixi130 – 1334
    Beta strandi139 – 15113
    Helixi154 – 1629
    Helixi163 – 1664
    Beta strandi172 – 1743
    Helixi180 – 1834
    Beta strandi190 – 1956
    Beta strandi206 – 2138
    Beta strandi215 – 2173
    Helixi219 – 2257
    Beta strandi229 – 2313
    Beta strandi255 – 2584

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FLJX-ray1.80A2-259[»]
    ProteinModelPortaliP14141.
    SMRiP14141. Positions 2-260.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14141.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni64 – 674Involved in proton transferBy similarity
    Regioni198 – 1992Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the alpha-carbonic anhydrase family.Curated

    Phylogenomic databases

    eggNOGiCOG3338.
    GeneTreeiENSGT00750000117305.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiP14141.
    KOiK01672.
    OMAiEAPFTHF.
    OrthoDBiEOG7WMCK7.
    PhylomeDBiP14141.
    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.
    IPR018441. Carbonic_anhydrase_CA3.
    [Graphical view]
    PANTHERiPTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF96. PTHR18952:SF96. 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.

    P14141-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKEWGYASH NGPEHWHELY PIAKGDNQSP IELHTKDIRH DPSLQPWSVS    50
    YDPGSAKTIL NNGKTCRVVF DDTFDRSMLR GGPLSGPYRL RQFHLHWGSS 100
    DDHGSEHTVD GVKYAAELHL VHWNPKYNTF GEALKQPDGI AVVGIFLKIG 150
    REKGEFQILL DALDKIKTKG KEAPFNHFDP SCLFPACRDY WTYHGSFTTP 200
    PCEECIVWLL LKEPMTVSSD QMAKLRSLFA SAENEPPVPL VGNWRPPQPI 250
    KGRVVRASFK 260
    Length:260
    Mass (Da):29,431
    Last modified:January 23, 2007 - v3
    Checksum:iC3C7DA7DA8793F18
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81A → G in AAA40846. (PubMed:2852973)Curated
    Sequence conflicti34 – 341H → HI AA sequence (PubMed:1899179)Curated
    Sequence conflicti57 – 571K → R AA sequence (PubMed:1899179)Curated
    Sequence conflicti126 – 1261K → DR AA sequence (PubMed:1899179)Curated
    Sequence conflicti130 – 1312FG → SE in AAA40846. (PubMed:2852973)Curated
    Sequence conflicti135 – 1351K → R AA sequence (PubMed:1899179)Curated
    Sequence conflicti189 – 1913DYW → QYP AA sequence (PubMed:1899179)Curated
    Sequence conflicti224 – 2252KL → NV in AAA40846. (PubMed:2852973)Curated
    Sequence conflicti225 – 2262LR → DE AA sequence (PubMed:1899179)Curated
    Sequence conflicti230 – 2301A → G AA sequence (PubMed:1899179)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22413 mRNA. Translation: AAA40846.1.
    AB030829 mRNA. Translation: BAB08111.1.
    AB030830 mRNA. Translation: BAB20673.1.
    AF037072 mRNA. Translation: AAB92558.1.
    BC061980 mRNA. Translation: AAH61980.1.
    PIRiI52551.
    RefSeqiNP_062165.2. NM_019292.4.
    XP_006232178.1. XM_006232116.1.
    UniGeneiRn.1647.

    Genome annotation databases

    EnsembliENSRNOT00000014180; ENSRNOP00000014177; ENSRNOG00000010079.
    GeneIDi54232.
    KEGGirno:54232.
    UCSCiRGD:2241. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22413 mRNA. Translation: AAA40846.1 .
    AB030829 mRNA. Translation: BAB08111.1 .
    AB030830 mRNA. Translation: BAB20673.1 .
    AF037072 mRNA. Translation: AAB92558.1 .
    BC061980 mRNA. Translation: AAH61980.1 .
    PIRi I52551.
    RefSeqi NP_062165.2. NM_019292.4.
    XP_006232178.1. XM_006232116.1.
    UniGenei Rn.1647.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FLJ X-ray 1.80 A 2-259 [» ]
    ProteinModelPortali P14141.
    SMRi P14141. Positions 2-260.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-4569746.
    STRINGi 10116.ENSRNOP00000014177.

    Chemistry

    BindingDBi P14141.

    PTM databases

    PhosphoSitei P14141.

    Proteomic databases

    PaxDbi P14141.
    PRIDEi P14141.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000014180 ; ENSRNOP00000014177 ; ENSRNOG00000010079 .
    GeneIDi 54232.
    KEGGi rno:54232.
    UCSCi RGD:2241. rat.

    Organism-specific databases

    CTDi 12350.
    RGDi 2241. Ca3.

    Phylogenomic databases

    eggNOGi COG3338.
    GeneTreei ENSGT00750000117305.
    HOGENOMi HOG000112637.
    HOVERGENi HBG002837.
    InParanoidi P14141.
    KOi K01672.
    OMAi EAPFTHF.
    OrthoDBi EOG7WMCK7.
    PhylomeDBi P14141.
    TreeFami TF316425.

    Enzyme and pathway databases

    BRENDAi 4.2.1.1. 5301.
    Reactomei REACT_199186. Reversible hydration of carbon dioxide.

    Miscellaneous databases

    EvolutionaryTracei P14141.
    NextBioi 610666.
    PROi P14141.

    Gene expression databases

    Genevestigatori P14141.

    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.
    IPR018441. Carbonic_anhydrase_CA3.
    [Graphical view ]
    PANTHERi PTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF96. PTHR18952:SF96. 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. "Characterisation of cDNA clones for rat muscle carbonic anhydrase III."
      Kelly C.D., Carter N.D., Jeffery S., Edwards Y.H.
      Biosci. Rep. 8:401-406(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Suppression of carbonic anhydrase III in rat liver by a dioxin-related toxic compound, coplanar polychlorinated biphenyl, 3,3',4,4',5-pentachlorobiphenyl."
      Ikeda M., Ishii Y., Kato H., Akazawa D., Hatsumura M., Ishida T., Matsusue K., Yamada H., Oguri K.
      Arch. Biochem. Biophys. 380:159-164(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
      Strain: Wistar.
      Tissue: Liver and Soleus muscle.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ZINC ION AND GLUTATHIONE, GLUTATHIONYLATION AT CYS-182 AND CYS-187.
      Tissue: Liver.
    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: Prostate.
    5. "Carbonic anhydrase III in obese Zucker rats."
      Lynch C.J., Brennan W.A. Jr., Vary T.C., Carter N., Dodgson S.J.
      Am. J. Physiol. 264:E621-E630(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-45 AND 120-142, TISSUE SPECIFICITY.
      Strain: Zucker.
    6. "Analyses of polypeptides in the liver of a novel mutant (LEC rats) to hereditary hepatitis and hepatoma by two-dimensional gel electrophoresis: identification of P29/6.8 as carbonic anhydrase III and triosephosphate isomerase."
      Nagase T., Sugiyama T., Kawata S., Tarui S., Deutsch H.F., Taniguchi N.
      Comp. Biochem. Physiol. 99B:193-201(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-33.
      Tissue: Liver.
    7. "Identification of an abundant S-thiolated rat liver protein as carbonic anhydrase III; characterization of S-thiolation and dethiolation reactions."
      Chai Y.-C., Jung C.-H., Lii C.-K., Ashraf S.S., Hendrich S., Wolf B., Sies H., Thomas J.A.
      Arch. Biochem. Biophys. 284:270-278(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-35; 40-57; 68-76; 81-89; 114-135; 189-201 AND 225-239.
      Tissue: Liver.
    8. Lubec G., Afjehi-Sadat L.
      Submitted (DEC-2006) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 113-125 AND 136-148, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Spinal cord.
    9. "Suppression of carbonic anhydrase III mRNA level by an aryl hydrocarbon receptor ligand in primary cultured hepatocytes of rat."
      Ishii Y., Akazawa D., Aoki Y., Yamada H., Oguri K.
      Biol. Pharm. Bull. 28:1087-1090(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.

    Entry informationi

    Entry nameiCAH3_RAT
    AccessioniPrimary (citable) accession number: P14141
    Secondary accession number(s): O54961, Q9QV77
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 139 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Expressed at much higher levels in the adipocytes of lean Zucker rats than in obese Zucker rats. Expression is higher is the adipocytes of male Zucker rats than in female Zucker rats.

    Keywords - Technical termi

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

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3