ID CAH15_MOUSE Reviewed; 324 AA.
AC Q99N23;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 149.
DE RecName: Full=Carbonic anhydrase 15;
DE EC=4.2.1.1;
DE AltName: Full=Carbonate dehydratase XV;
DE AltName: Full=Carbonic anhydrase XV;
DE Short=CA-XV;
DE Flags: Precursor;
GN Name=Ca15; Synonyms=Car15;
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=C57BL/6J; TISSUE=Kidney;
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 TISSUE=Kidney;
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 [3]
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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: Reversible hydration of carbon dioxide. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Repressed by coumarins.
CC {ECO:0000269|PubMed:19206230}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; AF231122; AAK16671.1; -; mRNA.
DR EMBL; BC019975; AAH19975.1; -; mRNA.
DR CCDS; CCDS49784.1; -.
DR RefSeq; NP_085035.1; NM_030558.2.
DR AlphaFoldDB; Q99N23; -.
DR SMR; Q99N23; -.
DR STRING; 10090.ENSMUSP00000113400; -.
DR BindingDB; Q99N23; -.
DR ChEMBL; CHEMBL5973; -.
DR DrugCentral; Q99N23; -.
DR GlyCosmos; Q99N23; 3 sites, No reported glycans.
DR GlyGen; Q99N23; 3 sites.
DR PhosphoSitePlus; Q99N23; -.
DR jPOST; Q99N23; -.
DR MaxQB; Q99N23; -.
DR PaxDb; 10090-ENSMUSP00000113400; -.
DR ProteomicsDB; 273898; -.
DR DNASU; 80733; -.
DR Ensembl; ENSMUST00000118960.2; ENSMUSP00000113400.2; ENSMUSG00000090236.4.
DR GeneID; 80733; -.
DR KEGG; mmu:80733; -.
DR UCSC; uc007ymg.1; mouse.
DR AGR; MGI:1931324; -.
DR CTD; 80733; -.
DR MGI; MGI:1931324; Car15.
DR VEuPathDB; HostDB:ENSMUSG00000090236; -.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000162972; -.
DR HOGENOM; CLU_039326_2_0_1; -.
DR InParanoid; Q99N23; -.
DR OMA; AWCYDSQ; -.
DR OrthoDB; 49814at2759; -.
DR PhylomeDB; Q99N23; -.
DR TreeFam; TF316425; -.
DR BRENDA; 4.2.1.1; 3474.
DR SABIO-RK; Q99N23; -.
DR BioGRID-ORCS; 80733; 2 hits in 77 CRISPR screens.
DR PRO; PR:Q99N23; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q99N23; Protein.
DR Bgee; ENSMUSG00000090236; Expressed in islet of Langerhans and 105 other cell types or tissues.
DR Genevisible; Q99N23; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0004089; F:carbonate dehydratase activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR CDD; cd03117; alpha_CA_IV_XV_like; 1.
DR Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1.
DR InterPro; IPR041874; CA4/CA15.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR PANTHER; PTHR18952; CARBONIC ANHYDRASE; 1.
DR PANTHER; PTHR18952:SF134; CARBONIC ANHYDRASE 15; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Lyase; Metal-binding; Reference proteome; Secreted; Signal;
KW Zinc.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..324
FT /note="Carbonic anhydrase 15"
FT /id="PRO_0000004253"
FT DOMAIN 23..293
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT REGION 269..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 90
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT ACT_SITE 155
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 231..232
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 324 AA; 35482 MW; D285DD086476372F CRC64;
MWALDFLLSF LLIQLAAQVD SSGTWCYDSQ DPKCGPAHWK ELAPACGGPT QSPINIDLRL
VQRDYTLKPF IFQGYDSAPQ DPWVLENDGH TVLLRVNSCQ QNCPAIRGAG LPSPEYRLLQ
LHFHWGSPGH QGSEHSLDEK HGSMEMHMVH MNTKYQSMED ARSQPDGFAI LAVLLVEEDR
DNTNFSAIVS GLKNLSSPGV AVNLTSTFAL ASLLPSALRL LRYYRYSGSL TTPGCEPAVL
WTVFENTVPI GHAQVVQFQA VLQTGPPGLH PRPLTSNFRP QQPLGGRRIS ASPEASVRSS
VSTLPCLHLA LVGLGVGLRL WQGP
//
