CAH2_MOUSE
ID CAH2_MOUSE Reviewed; 260 AA.
AC P00920; Q6LDQ7; Q7TPE1; Q9DCT3; Q9DCY9;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 4.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Carbonic anhydrase 2;
DE EC=4.2.1.1 {ECO:0000250|UniProtKB:P00918};
DE AltName: Full=Carbonate dehydratase II;
DE AltName: Full=Carbonic anhydrase II;
DE Short=CA-II;
GN Name=Ca2; Synonyms=Car2;
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=6420240; DOI=10.1016/0378-1119(83)90237-8;
RA Curtis P.J., Withers E., Demuth D., Watt R., Venta P.J., Tashian R.E.;
RT "The nucleotide sequence and derived amino acid sequence of cDNA coding for
RT mouse carbonic anhydrase II.";
RL Gene 25:325-332(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2995362; DOI=10.1016/s0021-9258(17)38996-2;
RA Venta P.J., Montgomery J.C., Hewett-Emmett D., Wiebauer K., Tashian R.E.;
RT "Structure and exon to protein domain relationships of the mouse carbonic
RT anhydrase II gene.";
RL J. Biol. Chem. 260:12130-12135(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 MRNA].
RC STRAIN=FVB/N; TISSUE=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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77.
RX PubMed=3000449; DOI=10.1016/0167-4781(85)90006-5;
RA Venta P.J., Montgomery J.C., Hewett-Emmett D., Tashian R.E.;
RT "Comparison of the 5' regions of human and mouse carbonic anhydrase II
RT genes and identification of possible regulatory elements.";
RL Biochim. Biophys. Acta 826:195-201(1985).
RN [6]
RP PROTEIN SEQUENCE OF 19-53; 58-80; 90-111; 114-126; 133-167 AND 213-226, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 155-178 AND 214-240.
RX PubMed=6187736; DOI=10.1016/s0021-9258(18)32645-0;
RA Curtis P.J.;
RT "Cloning of mouse carbonic anhydrase mRNA and its induction in mouse
RT erythroleukemic cells.";
RL J. Biol. Chem. 258:4459-4463(1983).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 241-260.
RX PubMed=6331255; DOI=10.1111/j.1749-6632.1984.tb12355.x;
RA Venta P.J., Montgomery J.C., Wiebauer K., Hewett-Emmett D., Tashian R.E.;
RT "Organization of the mouse and human carbonic anhydrase II genes.";
RL Ann. N. Y. Acad. Sci. 429:309-323(1984).
RN [9]
RP FUNCTION.
RX PubMed=20150244; DOI=10.1152/ajpgi.00293.2009;
RA Simpson J.E., Walker N.M., Supuran C.T., Soleimani M., Clarke L.L.;
RT "Putative anion transporter-1 (Pat-1, Slc26a6) contributes to intracellular
RT pH regulation during H+-dipeptide transport in duodenal villous
RT epithelium.";
RL Am. J. Physiol. 298:G683-G691(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND IDENTIFICATION BY
RP 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 (By
CC similarity). Involved in the regulation of fluid secretion into the
CC anterior chamber of the eye (By similarity). Essential for bone
CC resorption and osteoclast differentiation (By similarity). Contributes
CC to intracellular pH regulation in the duodenal upper villous epithelium
CC during proton-coupled peptide absorption (By similarity). Stimulates
CC the chloride-bicarbonate exchange activity of SLC26A6 (By similarity).
CC {ECO:0000250|UniProtKB:P00918}.
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:P00918};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00921};
CC -!- ACTIVITY REGULATION: Inhibited by acetazolamide.
CC {ECO:0000250|UniProtKB:P00918}.
CC -!- SUBUNIT: Interacts with SLC4A4 (By similarity). Interaction with SLC4A7
CC regulates SLC4A7 transporter activity (By similarity). Interacts with
CC SLC26A6 (By similarity). {ECO:0000250|UniProtKB:P00918}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00918}. Cell
CC membrane {ECO:0000250|UniProtKB:P00918}. Note=Colocalized with SLC26A6
CC at the surface of the cell membrane in order to form a bicarbonate
CC transport metabolon. Displaced from the cytosolic surface of the cell
CC membrane by PKC in phorbol myristate acetate (PMA)-induced cells.
CC {ECO:0000250|UniProtKB:P00918}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; K00811; AAA37356.1; -; mRNA.
DR EMBL; M81022; AAA37357.1; -; Genomic_DNA.
DR EMBL; M81016; AAA37357.1; JOINED; Genomic_DNA.
DR EMBL; M81017; AAA37357.1; JOINED; Genomic_DNA.
DR EMBL; M81018; AAA37357.1; JOINED; Genomic_DNA.
DR EMBL; M81019; AAA37357.1; JOINED; Genomic_DNA.
DR EMBL; M81020; AAA37357.1; JOINED; Genomic_DNA.
DR EMBL; M81021; AAA37357.1; JOINED; Genomic_DNA.
DR EMBL; AK002333; BAB22019.1; -; mRNA.
DR EMBL; AK002498; BAB22146.2; -; mRNA.
DR EMBL; BC055291; AAH55291.1; -; mRNA.
DR EMBL; M25944; AAA39505.1; -; mRNA.
DR CCDS; CCDS17251.1; -.
DR PIR; A23900; CRMS2.
DR RefSeq; NP_033931.4; NM_009801.4.
DR RefSeq; XP_006530113.1; XM_006530050.1.
DR AlphaFoldDB; P00920; -.
DR SMR; P00920; -.
DR BioGRID; 198483; 9.
DR IntAct; P00920; 2.
DR STRING; 10090.ENSMUSP00000029078; -.
DR ChEMBL; CHEMBL3689; -.
DR iPTMnet; P00920; -.
DR PhosphoSitePlus; P00920; -.
DR SwissPalm; P00920; -.
DR CPTAC; non-CPTAC-3303; -.
DR CPTAC; non-CPTAC-3365; -.
DR EPD; P00920; -.
DR jPOST; P00920; -.
DR MaxQB; P00920; -.
DR PaxDb; P00920; -.
DR PeptideAtlas; P00920; -.
DR PRIDE; P00920; -.
DR ProteomicsDB; 265421; -.
DR Antibodypedia; 677; 689 antibodies from 42 providers.
DR DNASU; 12349; -.
DR Ensembl; ENSMUST00000029078; ENSMUSP00000029078; ENSMUSG00000027562.
DR GeneID; 12349; -.
DR KEGG; mmu:12349; -.
DR UCSC; uc008oqt.2; mouse.
DR CTD; 12349; -.
DR MGI; MGI:88269; Car2.
DR VEuPathDB; HostDB:ENSMUSG00000027562; -.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000160385; -.
DR HOGENOM; CLU_039326_2_1_1; -.
DR InParanoid; P00920; -.
DR OMA; SADFPNF; -.
DR OrthoDB; 1377476at2759; -.
DR PhylomeDB; P00920; -.
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; 12349; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Car2; mouse.
DR PRO; PR:P00920; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P00920; protein.
DR Bgee; ENSMUSG00000027562; Expressed in fetal liver hematopoietic progenitor cell and 272 other tissues.
DR ExpressionAtlas; P00920; baseline and differential.
DR Genevisible; P00920; MM.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005902; C:microvillus; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004064; F:arylesterase activity; ISO:MGI.
DR GO; GO:0004089; F:carbonate dehydratase activity; IDA:MGI.
DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0038166; P:angiotensin-activated signaling pathway; ISS:UniProtKB.
DR GO; GO:0015670; P:carbon dioxide transport; IMP:MGI.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IMP:MGI.
DR GO; GO:0070050; P:neuron cellular homeostasis; IMP:MGI.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR GO; GO:0045780; P:positive regulation of bone resorption; ISO:MGI.
DR GO; GO:0032849; P:positive regulation of cellular pH reduction; IMP:MGI.
DR GO; GO:2001150; P:positive regulation of dipeptide transmembrane transport; IMP:UniProtKB.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; ISO:MGI.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IGI:MGI.
DR GO; GO:0044070; P:regulation of anion transport; ISS:UniProtKB.
DR GO; GO:2001225; P:regulation of chloride transport; IMP:MGI.
DR GO; GO:0051453; P:regulation of intracellular pH; IMP:UniProtKB.
DR GO; GO:0006885; P:regulation of pH; IC:MGI.
DR GO; GO:0046903; P:secretion; IMP:MGI.
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 PANTHER; PTHR18952; PTHR18952; 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; Cell membrane; Cytoplasm; Direct protein sequencing; Lyase;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT CHAIN 2..260
FT /note="Carbonic anhydrase 2"
FT /id="PRO_0000077419"
FT DOMAIN 3..259
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT ACT_SITE 64
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT ACT_SITE 67
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT ACT_SITE 127
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT BINDING 198..199
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27139"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT CONFLICT 39
FT /note="Q -> H (in Ref. 1; AAA37356 and 4; AAH55291)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="I -> Y (in Ref. 1; AAA37356 and 2; AAA37357)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="E -> D (in Ref. 2; AAA37357)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 260 AA; 29033 MW; 095760368D446AA6 CRC64;
MSHHWGYSKH NGPENWHKDF PIANGDRQSP VDIDTATAQH DPALQPLLIS YDKAASKSIV
NNGHSFNVEF DDSQDNAVLK GGPLSDSYRL IQFHFHWGSS DGQGSEHTVN KKKYAAELHL
VHWNTKYGDF GKAVQQPDGL AVLGIFLKIG PASQGLQKVL EALHSIKTKG KRAAFANFDP
CSLLPGNLDY WTYPGSLTTP PLLECVTWIV LREPITVSSE QMSHFRTLNF NEEGDAEEAM
VDNWRPAQPL KNRKIKASFK
