CAH13_MOUSE
ID CAH13_MOUSE Reviewed; 262 AA.
AC Q9D6N1; Q3UBM2;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Carbonic anhydrase 13;
DE EC=4.2.1.1 {ECO:0000269|PubMed:14600151};
DE AltName: Full=Carbonate dehydratase XIII;
DE AltName: Full=Carbonic anhydrase XIII;
DE Short=CA-XIII;
GN Name=Ca13; Synonyms=Car13;
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].
RC STRAIN=C3H/HeJ;
RA Hewett-Emmett D., Shimmin L.C.;
RT "Characterization and evolution of two new members of the alpha-carbonic
RT anhydrase gene family in mouse: Car13 and Car15.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone, Bone marrow, and Tongue;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [4]
RP CATALYTIC ACTIVITY, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=14600151; DOI=10.1074/jbc.m308984200;
RA Lehtonen J., Shen B., Vihinen M., Casini A., Scozzafava A., Supuran C.T.,
RA Parkkila A.-K., Saarnio J., Kivelae A.J., Waheed A., Sly W.S., Parkkila S.;
RT "Characterization of CA XIII, a novel member of the carbonic anhydrase
RT isozyme family.";
RL J. Biol. Chem. 279:2719-2727(2004).
RN [5]
RP ACTIVITY REGULATION.
RX PubMed=17314045; DOI=10.1016/j.bmcl.2007.01.113;
RA Temperini C., Innocenti A., Guerri A., Scozzafava A., Rusconi S.,
RA Supuran C.T.;
RT "Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-ray
RT crystal structure of the antiviral drug foscarnet complexed to human
RT carbonic anhydrase I.";
RL Bioorg. Med. Chem. Lett. 17:2210-2215(2007).
RN [6]
RP ACTIVITY REGULATION.
RX PubMed=19186056; DOI=10.1016/j.bmcl.2009.01.038;
RA Crocetti L., Maresca A., Temperini C., Hall R.A., Scozzafava A.,
RA Muehlschlegel F.A., Supuran C.T.;
RT "A thiabendazole sulfonamide shows potent inhibitory activity against
RT mammalian and nematode alpha-carbonic anhydrases.";
RL Bioorg. Med. Chem. Lett. 19:1371-1375(2009).
RN [7]
RP ACTIVITY REGULATION.
RX PubMed=19206230; DOI=10.1021/ja809683v;
RA Maresca A., Temperini C., Vu H., Pham N.B., Poulsen S.-A., Scozzafava A.,
RA Quinn R.J., Supuran C.T.;
RT "Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new
RT class of suicide inhibitors.";
RL J. Am. Chem. Soc. 131:3057-3062(2009).
CC -!- FUNCTION: Reversible hydration of carbon dioxide.
CC {ECO:0000269|PubMed:14600151}.
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:0000269|PubMed:14600151};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q8N1Q1};
CC -!- ACTIVITY REGULATION: Inhibited by coumarins, sulfonamide derivatives
CC such as acetazolamide (AZA) and Foscarnet (phosphonoformate trisodium
CC salt). {ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:19186056,
CC ECO:0000269|PubMed:19206230}.
CC -!- TISSUE SPECIFICITY: Expressed in spleen, lung, kidney, heart, brain,
CC skeletal muscle and testis. {ECO:0000269|PubMed:14600151}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; AF231123; AAK16672.1; -; mRNA.
DR EMBL; AK010166; BAB26742.1; -; mRNA.
DR EMBL; AK150871; BAE29922.1; -; mRNA.
DR EMBL; AK150897; BAE29942.1; -; mRNA.
DR EMBL; AK151519; BAE30468.1; -; mRNA.
DR EMBL; AK151978; BAE30845.1; -; mRNA.
DR EMBL; AK153080; BAE31705.1; -; mRNA.
DR EMBL; AK153258; BAE31849.1; -; mRNA.
DR EMBL; AK153353; BAE31927.1; -; mRNA.
DR EMBL; AK162621; BAE36996.1; -; mRNA.
DR EMBL; BC064050; AAH64050.1; -; mRNA.
DR CCDS; CCDS17247.1; -.
DR RefSeq; NP_078771.1; NM_024495.5.
DR AlphaFoldDB; Q9D6N1; -.
DR SMR; Q9D6N1; -.
DR STRING; 10090.ENSMUSP00000029071; -.
DR BindingDB; Q9D6N1; -.
DR ChEMBL; CHEMBL2186; -.
DR DrugCentral; Q9D6N1; -.
DR GuidetoPHARMACOLOGY; 2748; -.
DR iPTMnet; Q9D6N1; -.
DR PhosphoSitePlus; Q9D6N1; -.
DR MaxQB; Q9D6N1; -.
DR PaxDb; Q9D6N1; -.
DR PeptideAtlas; Q9D6N1; -.
DR PRIDE; Q9D6N1; -.
DR ProteomicsDB; 265420; -.
DR Antibodypedia; 12589; 204 antibodies from 29 providers.
DR DNASU; 71934; -.
DR Ensembl; ENSMUST00000029071; ENSMUSP00000029071; ENSMUSG00000027555.
DR GeneID; 71934; -.
DR KEGG; mmu:71934; -.
DR UCSC; uc008oqo.2; mouse.
DR CTD; 71934; -.
DR MGI; MGI:1931322; Car13.
DR VEuPathDB; HostDB:ENSMUSG00000027555; -.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000160659; -.
DR HOGENOM; CLU_039326_2_1_1; -.
DR InParanoid; Q9D6N1; -.
DR OMA; PIHWNEL; -.
DR OrthoDB; 1377476at2759; -.
DR PhylomeDB; Q9D6N1; -.
DR TreeFam; TF316425; -.
DR BRENDA; 4.2.1.1; 3474.
DR Reactome; R-MMU-1475029; Reversible hydration of carbon dioxide.
DR BioGRID-ORCS; 71934; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q9D6N1; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9D6N1; protein.
DR Bgee; ENSMUSG00000027555; Expressed in meninx and 201 other tissues.
DR Genevisible; Q9D6N1; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:MGI.
DR GO; GO:0043209; C:myelin sheath; IDA: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; 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 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 Lyase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..262
FT /note="Carbonic anhydrase 13"
FT /id="PRO_0000077441"
FT DOMAIN 4..261
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
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:Q8N1Q1"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8N1Q1"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8N1Q1"
FT BINDING 200..201
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00918"
SQ SEQUENCE 262 AA; 29522 MW; E3CA4674C1CF4A12 CRC64;
MARLSWGYGE HNGPIHWNEL FPIADGDQQS PIEIKTKEVK YDSSLRPLSI KYDPASAKII
SNSGHSFNVD FDDTEDKSVL RGGPLTGNYR LRQFHLHWGS ADDHGSEHVV DGVRYAAELH
VVHWNSDKYP SFVEAAHESD GLAVLGVFLQ IGEHNPQLQK ITDILDSIKE KGKQTRFTNF
DPLCLLPSSW DYWTYPGSLT VPPLLESVTW IVLKQPISIS SQQLARFRSL LCTAEGESAA
FLLSNHRPPQ PLKGRRVRAS FY
