CAH1_MOUSE
ID CAH1_MOUSE Reviewed; 261 AA.
AC P13634; Q3TS19; Q9DC84;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 4.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Carbonic anhydrase 1;
DE EC=4.2.1.1 {ECO:0000250|UniProtKB:P00915};
DE AltName: Full=Carbonate dehydratase I;
DE AltName: Full=Carbonic anhydrase I;
DE Short=CA-I;
GN Name=Ca1; Synonyms=Car1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3104601; DOI=10.1007/bf02100637;
RA Fraser P.J., Curtis P.J.;
RT "Molecular evolution of the carbonic anhydrase genes: calculation of
RT divergence time for mouse carbonic anhydrase I and II.";
RL J. Mol. Evol. 23:294-299(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=2571923; DOI=10.1128/mcb.9.8.3308-3313.1989;
RA Fraser P.J., Cummings P., Curtis P.J.;
RT "The mouse carbonic anhydrase I gene contains two tissue-specific
RT promoters.";
RL Mol. Cell. Biol. 9:3308-3313(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, C57BL/6J, and NOD; TISSUE=Cecum, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Brain, and Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the reversible hydration of carbon dioxide.
CC {ECO:0000250|UniProtKB:P00915}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17544; EC=4.2.1.1;
CC Evidence={ECO:0000250|UniProtKB:P00915};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00915};
CC -!- ACTIVITY REGULATION: Inhibited by acetazolamide.
CC {ECO:0000250|UniProtKB:P00915}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B0BNN3}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M32452; AAA37354.1; -; mRNA.
DR EMBL; L36655; AAA50291.1; -; Genomic_DNA.
DR EMBL; M28197; AAA50291.1; JOINED; Genomic_DNA.
DR EMBL; L36650; AAA50291.1; JOINED; Genomic_DNA.
DR EMBL; L36651; AAA50291.1; JOINED; Genomic_DNA.
DR EMBL; L36652; AAA50291.1; JOINED; Genomic_DNA.
DR EMBL; L36653; AAA50291.1; JOINED; Genomic_DNA.
DR EMBL; L36654; AAA50291.1; JOINED; Genomic_DNA.
DR EMBL; AK003066; BAB22544.1; -; mRNA.
DR EMBL; AK146372; BAE27121.1; -; mRNA.
DR EMBL; AK162331; BAE36857.1; -; mRNA.
DR EMBL; AK167969; BAE39964.1; -; mRNA.
DR EMBL; AK172076; BAE42813.1; -; mRNA.
DR EMBL; AC167976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466577; EDL05133.1; -; Genomic_DNA.
DR EMBL; BC110681; AAI10682.1; -; mRNA.
DR EMBL; BC132432; AAI32433.1; -; mRNA.
DR EMBL; BC132434; AAI32435.1; -; mRNA.
DR EMBL; BC011223; AAH11223.1; -; mRNA.
DR CCDS; CCDS17248.1; -.
DR PIR; A26344; A26344.
DR RefSeq; NP_001077426.1; NM_001083957.1.
DR RefSeq; NP_033929.2; NM_009799.4.
DR RefSeq; XP_011246439.1; XM_011248137.1.
DR AlphaFoldDB; P13634; -.
DR SMR; P13634; -.
DR BioGRID; 198481; 3.
DR STRING; 10090.ENSMUSP00000091925; -.
DR iPTMnet; P13634; -.
DR PhosphoSitePlus; P13634; -.
DR CPTAC; non-CPTAC-3566; -.
DR EPD; P13634; -.
DR jPOST; P13634; -.
DR PaxDb; P13634; -.
DR PeptideAtlas; P13634; -.
DR PRIDE; P13634; -.
DR ProteomicsDB; 281756; -.
DR Antibodypedia; 1380; 663 antibodies from 41 providers.
DR DNASU; 12346; -.
DR Ensembl; ENSMUST00000094365; ENSMUSP00000091925; ENSMUSG00000027556.
DR Ensembl; ENSMUST00000181860; ENSMUSP00000137926; ENSMUSG00000027556.
DR GeneID; 12346; -.
DR KEGG; mmu:12346; -.
DR UCSC; uc008oqp.1; mouse.
DR CTD; 12346; -.
DR MGI; MGI:88268; Car1.
DR VEuPathDB; HostDB:ENSMUSG00000027556; -.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000161270; -.
DR HOGENOM; CLU_039326_2_1_1; -.
DR InParanoid; P13634; -.
DR OMA; DYGSEHT; -.
DR OrthoDB; 1377476at2759; -.
DR PhylomeDB; P13634; -.
DR TreeFam; TF316425; -.
DR Reactome; R-MMU-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR Reactome; R-MMU-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR Reactome; R-MMU-1475029; Reversible hydration of carbon dioxide.
DR BioGRID-ORCS; 12346; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Car1; mouse.
DR PRO; PR:P13634; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P13634; protein.
DR Bgee; ENSMUSG00000027556; Expressed in right colon and 47 other tissues.
DR ExpressionAtlas; P13634; baseline and differential.
DR Genevisible; P13634; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004064; F:arylesterase activity; ISO:MGI.
DR GO; GO:0004089; F:carbonate dehydratase activity; ISO:MGI.
DR GO; GO:0016836; F:hydro-lyase activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR Gene3D; 3.10.200.10; -; 1.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR InterPro; IPR018338; Carbonic_anhydrase_a-class_CS.
DR InterPro; IPR018442; Carbonic_anhydrase_CA1.
DR PANTHER; PTHR18952; PTHR18952; 1.
DR PANTHER; PTHR18952:SF82; PTHR18952:SF82; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; SSF51069; 1.
DR PROSITE; PS00162; ALPHA_CA_1; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Lyase; Metal-binding; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00915"
FT CHAIN 2..261
FT /note="Carbonic anhydrase 1"
FT /id="PRO_0000077413"
FT DOMAIN 4..261
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT REGION 239..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 65
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00915"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00915"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00915"
FT BINDING 200..201
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00915"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P00915"
FT CONFLICT 238
FT /note="P -> S (in Ref. 1; AAA37354/AAA50291)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 261 AA; 28331 MW; D179AA7BA38EDF0E CRC64;
MASADWGYGS ENGPDQWSKL YPIANGNNQS PIDIKTSEAN HDSSLKPLSI SYNPATAKEI
VNVGHSFHVI FDDSSNQSVL KGGPLADSYR LTQFHFHWGN SNDHGSEHTV DGTRYSGELH
LVHWNSAKYS SASEAISKAD GLAILGVLMK VGPANPSLQK VLDALNSVKT KGKRAPFTNF
DPSSLLPSSL DYWTYFGSLT HPPLHESVTW VICKDSISLS PEQLAQLRGL LSSAEGEPAV
PVLSNHRPPQ PLKGRTVRAS F
