ID CAH3_HORSE Reviewed; 260 AA.
AC P07450;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 24-JAN-2024, entry version 146.
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 Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP PROTEIN SEQUENCE OF 2-260, AND ACETYLATION AT ALA-2.
RX PubMed=3922970; DOI=10.1016/s0021-9258(18)88946-3;
RA Wendorff K.M., Nishita T., Jabusch J.R., Deutsch H.F.;
RT "The sequence of equine muscle carbonic anhydrase.";
RL J. Biol. Chem. 260:6129-6132(1985).
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 PIR; A22612; A22612.
DR RefSeq; NP_001157426.1; NM_001163954.1.
DR AlphaFoldDB; P07450; -.
DR SMR; P07450; -.
DR STRING; 9796.ENSECAP00000006508; -.
DR iPTMnet; P07450; -.
DR PaxDb; 9796-ENSECAP00000006508; -.
DR PeptideAtlas; P07450; -.
DR Ensembl; ENSECAT00000008659.4; ENSECAP00000006508.3; ENSECAG00000044498.1.
DR GeneID; 100050125; -.
DR KEGG; ecb:100050125; -.
DR CTD; 761; -.
DR GeneTree; ENSGT00940000159435; -.
DR HOGENOM; CLU_039326_2_1_1; -.
DR InParanoid; P07450; -.
DR OrthoDB; 49814at2759; -.
DR TreeFam; TF316425; -.
DR Proteomes; UP000002281; Chromosome 9.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004089; F:carbonate dehydratase 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 CDD; cd03119; alpha_CA_I_II_III_XIII; 1.
DR Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 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; CARBONIC ANHYDRASE; 1.
DR PANTHER; PTHR18952:SF127; CARBONIC ANHYDRASE 3; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR PROSITE; PS00162; ALPHA_CA_1; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Glutathionylation;
KW Lyase; Metal-binding; Phosphoprotein; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3922970"
FT CHAIN 2..260
FT /note="Carbonic anhydrase 3"
FT /id="PRO_0000077425"
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:0000269|PubMed:3922970"
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 129
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 176
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P16015"
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; 29511 MW; 0BDECDE7C88FED3B CRC64;
MAKEWGYADH NGPDHWHEFY PIAKGDNQSP IELHTKDINH DPSLKAWTAS YDPGSAKTIL
NNGRTCRVVF DDTYDRSMLR GGPLTAPYRL RQFHLHWGSS DDHGSEHTVD GVKYAAELHL
VHWNPKYNTY GGALKQPDGI AVVGVFLKIG REKGEFQLFL DALDKIKTKG KEAPFTNFDP
SCLFPTCRDY WTYRGSFTTP PCEECIVWLL LKEPITVSSD QVAKLRSLFS SAENEPPVPL
VRNWRPPQPL KGRVVRASFK
//
