CAH3_BOVIN
ID CAH3_BOVIN Reviewed; 260 AA.
AC Q3SZX4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Carbonic anhydrase 3;
DE EC=4.2.1.1 {ECO:0000250|UniProtKB:P07451};
DE AltName: Full=Carbonate dehydratase III;
DE AltName: Full=Carbonic anhydrase III;
DE Short=CA-III;
GN Name=CA3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Reversible hydration of carbon dioxide.
CC {ECO:0000250|UniProtKB:P07451}.
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:P07451};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P07451};
CC -!- ACTIVITY REGULATION: Inhibited by acetazolamide.
CC {ECO:0000250|UniProtKB:P07451}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P07451}.
CC -!- PTM: S-thiolated both by thiol-disulfide exchange with glutathione
CC disulfide and by oxyradical-initiated S-thiolation with reduced
CC glutathione. {ECO:0000250|UniProtKB:P14141}.
CC -!- PTM: S-glutathionylated in hepatocytes under oxidative stress.
CC {ECO:0000250|UniProtKB:P14141}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; BC102666; AAI02667.1; -; mRNA.
DR RefSeq; NP_001029609.1; NM_001034437.1.
DR AlphaFoldDB; Q3SZX4; -.
DR SMR; Q3SZX4; -.
DR STRING; 9913.ENSBTAP00000020243; -.
DR BindingDB; Q3SZX4; -.
DR ChEMBL; CHEMBL1944498; -.
DR DrugCentral; Q3SZX4; -.
DR PaxDb; Q3SZX4; -.
DR PeptideAtlas; Q3SZX4; -.
DR PRIDE; Q3SZX4; -.
DR Ensembl; ENSBTAT00000020243; ENSBTAP00000020243; ENSBTAG00000015214.
DR GeneID; 513212; -.
DR KEGG; bta:513212; -.
DR CTD; 761; -.
DR VEuPathDB; HostDB:ENSBTAG00000015214; -.
DR VGNC; VGNC:26653; CA3.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000159435; -.
DR HOGENOM; CLU_039326_2_1_1; -.
DR InParanoid; Q3SZX4; -.
DR OMA; ERWHENY; -.
DR OrthoDB; 1377476at2759; -.
DR TreeFam; TF316425; -.
DR Reactome; R-BTA-1475029; Reversible hydration of carbon dioxide.
DR PRO; PR:Q3SZX4; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000015214; Expressed in gluteus medius and 95 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR GO; GO:0016151; F:nickel cation binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
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; IPR018441; Carbonic_anhydrase_CA3.
DR PANTHER; PTHR18952; PTHR18952; 1.
DR PANTHER; PTHR18952:SF127; PTHR18952:SF127; 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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Glutathionylation; Lyase; Metal-binding;
KW Phosphoprotein; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P07450"
FT CHAIN 2..260
FT /note="Carbonic anhydrase 3"
FT /id="PRO_0000262533"
FT DOMAIN 3..259
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT REGION 64..67
FT /note="Involved in proton transfer"
FT /evidence="ECO:0000250|UniProtKB:P07451"
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-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P07450"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 73
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 127
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 182
FT /note="S-glutathionyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 187
FT /note="S-glutathionyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 216
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
SQ SEQUENCE 260 AA; 29370 MW; F78A6E7E9C47028B CRC64;
MAKEWGYADH NGPDHWHELF PNAKGENQSP IELNTKEISH DPSLKPWTAS YDPGSAKTIL
NNGKTCRVVF DDTYDRSMLR GGPLAAPYRL RQFHLHWGSS DDHGSEHSVD GVKYAAELHL
VHWNSKYNSY ATALKHADGI AVVGVFLKIG REKGEFQLLL DALDKIKTKG KEAPFNNFNP
SCLFPACRDY WTYHGSFTTP PCEECIVWLL LKEPITVSSD QIAKLRTLYS SAENEPPVPL
VRNWRPPQPI KGRIVKASFK
