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P13634

- CAH1_MOUSE

UniProt

P13634 - CAH1_MOUSE

Protein

Carbonic anhydrase 1

Gene

Ca1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 4 (03 Oct 2012)
      Previous versions | rss
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    Functioni

    Reversible hydration of carbon dioxide.

    Catalytic activityi

    H2CO3 = CO2 + H2O.

    Cofactori

    Zinc.

    Enzyme regulationi

    Inhibited by acetazolamide.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei65 – 651Proton acceptorBy similarity
    Metal bindingi95 – 951Zinc; catalytic
    Metal bindingi97 – 971Zinc; catalytic
    Metal bindingi120 – 1201Zinc; catalytic
    Active sitei129 – 1291By similarity
    Binding sitei200 – 2001SubstrateBy similarity

    GO - Molecular functioni

    1. carbonate dehydratase activity Source: UniProtKB-EC
    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_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 1 (EC:4.2.1.1)
    Alternative name(s):
    Carbonate dehydratase I
    Carbonic anhydrase I
    Short name:
    CA-I
    Gene namesi
    Name:Ca1
    Synonyms:Car1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:88268. Car1.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi apparatus Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 261260Carbonic anhydrase 1PRO_0000077413Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP13634.
    PRIDEiP13634.

    PTM databases

    PhosphoSiteiP13634.

    Expressioni

    Gene expression databases

    ArrayExpressiP13634.
    CleanExiMM_CAR1.
    GenevestigatoriP13634.

    Interactioni

    Protein-protein interaction databases

    BioGridi198481. 2 interactions.
    IntActiP13634. 1 interaction.
    MINTiMINT-4089732.

    Structurei

    3D structure databases

    ProteinModelPortaliP13634.
    SMRiP13634. Positions 5-261.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni200 – 2012Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the alpha-carbonic anhydrase family.Curated

    Phylogenomic databases

    eggNOGiCOG3338.
    GeneTreeiENSGT00750000117305.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiP13634.
    KOiK01672.
    OMAiVTWIICK.
    OrthoDBiEOG7WMCK7.
    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.
    IPR018442. Carbonic_anhydrase_CA1.
    [Graphical view]
    PANTHERiPTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF82. PTHR18952:SF82. 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.

    P13634-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASADWGYGS ENGPDQWSKL YPIANGNNQS PIDIKTSEAN HDSSLKPLSI    50
    SYNPATAKEI VNVGHSFHVI FDDSSNQSVL KGGPLADSYR LTQFHFHWGN 100
    SNDHGSEHTV DGTRYSGELH LVHWNSAKYS SASEAISKAD GLAILGVLMK 150
    VGPANPSLQK VLDALNSVKT KGKRAPFTNF DPSSLLPSSL DYWTYFGSLT 200
    HPPLHESVTW VICKDSISLS PEQLAQLRGL LSSAEGEPAV PVLSNHRPPQ 250
    PLKGRTVRAS F 261
    Length:261
    Mass (Da):28,331
    Last modified:October 3, 2012 - v4
    Checksum:iD179AA7BA38EDF0E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti238 – 2381P → S in AAA37354. (PubMed:3104601)Curated
    Sequence conflicti238 – 2381P → S in AAA50291. (PubMed:3104601)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M32452 mRNA. Translation: AAA37354.1.
    L36655
    , M28197, L36650, L36651, L36652, L36653, L36654 Genomic DNA. Translation: AAA50291.1.
    AK003066 mRNA. Translation: BAB22544.1.
    AK146372 mRNA. Translation: BAE27121.1.
    AK162331 mRNA. Translation: BAE36857.1.
    AK167969 mRNA. Translation: BAE39964.1.
    AK172076 mRNA. Translation: BAE42813.1.
    AC167976 Genomic DNA. No translation available.
    CH466577 Genomic DNA. Translation: EDL05133.1.
    BC110681 mRNA. Translation: AAI10682.1.
    BC132432 mRNA. Translation: AAI32433.1.
    BC132434 mRNA. Translation: AAI32435.1.
    BC011223 mRNA. Translation: AAH11223.1.
    CCDSiCCDS17248.1.
    PIRiA26344.
    RefSeqiNP_001077426.1. NM_001083957.1.
    NP_033929.2. NM_009799.4.
    XP_006530112.1. XM_006530049.1.
    UniGeneiMm.273195.

    Genome annotation databases

    EnsembliENSMUST00000094365; ENSMUSP00000091925; ENSMUSG00000027556.
    ENSMUST00000181860; ENSMUSP00000137926; ENSMUSG00000027556.
    GeneIDi12346.
    KEGGimmu:12346.
    UCSCiuc008oqp.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M32452 mRNA. Translation: AAA37354.1 .
    L36655
    , M28197 , L36650 , L36651 , L36652 , L36653 , L36654 Genomic DNA. Translation: AAA50291.1 .
    AK003066 mRNA. Translation: BAB22544.1 .
    AK146372 mRNA. Translation: BAE27121.1 .
    AK162331 mRNA. Translation: BAE36857.1 .
    AK167969 mRNA. Translation: BAE39964.1 .
    AK172076 mRNA. Translation: BAE42813.1 .
    AC167976 Genomic DNA. No translation available.
    CH466577 Genomic DNA. Translation: EDL05133.1 .
    BC110681 mRNA. Translation: AAI10682.1 .
    BC132432 mRNA. Translation: AAI32433.1 .
    BC132434 mRNA. Translation: AAI32435.1 .
    BC011223 mRNA. Translation: AAH11223.1 .
    CCDSi CCDS17248.1.
    PIRi A26344.
    RefSeqi NP_001077426.1. NM_001083957.1.
    NP_033929.2. NM_009799.4.
    XP_006530112.1. XM_006530049.1.
    UniGenei Mm.273195.

    3D structure databases

    ProteinModelPortali P13634.
    SMRi P13634. Positions 5-261.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198481. 2 interactions.
    IntActi P13634. 1 interaction.
    MINTi MINT-4089732.

    PTM databases

    PhosphoSitei P13634.

    Proteomic databases

    PaxDbi P13634.
    PRIDEi P13634.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000094365 ; ENSMUSP00000091925 ; ENSMUSG00000027556 .
    ENSMUST00000181860 ; ENSMUSP00000137926 ; ENSMUSG00000027556 .
    GeneIDi 12346.
    KEGGi mmu:12346.
    UCSCi uc008oqp.1. mouse.

    Organism-specific databases

    CTDi 12346.
    MGIi MGI:88268. Car1.

    Phylogenomic databases

    eggNOGi COG3338.
    GeneTreei ENSGT00750000117305.
    HOGENOMi HOG000112637.
    HOVERGENi HBG002837.
    InParanoidi P13634.
    KOi K01672.
    OMAi VTWIICK.
    OrthoDBi EOG7WMCK7.
    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

    NextBioi 280986.
    PROi P13634.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P13634.
    CleanExi MM_CAR1.
    Genevestigatori P13634.

    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.
    IPR018442. Carbonic_anhydrase_CA1.
    [Graphical view ]
    PANTHERi PTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF82. PTHR18952:SF82. 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 evolution of the carbonic anhydrase genes: calculation of divergence time for mouse carbonic anhydrase I and II."
      Fraser P.J., Curtis P.J.
      J. Mol. Evol. 23:294-299(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The mouse carbonic anhydrase I gene contains two tissue-specific promoters."
      Fraser P.J., Cummings P., Curtis P.J.
      Mol. Cell. Biol. 9:3308-3313(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Brain.
    3. "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: BALB/c, C57BL/6J and NOD.
      Tissue: Cecum and Spleen.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Brain and Colon.

    Entry informationi

    Entry nameiCAH1_MOUSE
    AccessioniPrimary (citable) accession number: P13634
    Secondary accession number(s): Q3TS19, Q9DC84
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: October 3, 2012
    Last modified: October 1, 2014
    This is version 128 of the entry and version 4 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