ID CAH3_PIG Reviewed; 260 AA.
AC Q5S1S4; Q0Z809;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 24-JAN-2024, entry version 116.
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 {ECO:0000303|PubMed:17065793};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=17065793; DOI=10.1159/000095232;
RA Wang H.L., Zhu Z.M., Wang H., Yang S.L., Zhao S.H., Li K.;
RT "Molecular characterization and association analysis of porcine CA3.";
RL Cytogenet. Genome Res. 115:129-133(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liu G.Y., Xiong Z.Y.;
RT "Isolation, prediction of one novel swine gene that is differentially
RT expressed in the longissimus dorsi muscle tissues from landrace large white
RT cross combination.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RA Wu J., Deng C.Y., Xiong Y.Z.;
RT "Characterization of the porcine carbonic anhydrase III (CA3) mRNA.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Wu J., Deng C.Y., Xiong Y.Z., Zhou D.H.;
RT "Characterization of the porcine carbonic anhydrase III (CA3) gene.";
RL Submitted (JUN-2006) 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; DQ157048; ABA41599.1; -; Genomic_DNA.
DR EMBL; AY789645; AAV65838.1; -; mRNA.
DR EMBL; AY789514; AAV83540.1; -; mRNA.
DR EMBL; DQ675018; ABG49150.1; -; Genomic_DNA.
DR RefSeq; NP_001008688.1; NM_001008688.1.
DR AlphaFoldDB; Q5S1S4; -.
DR SMR; Q5S1S4; -.
DR STRING; 9823.ENSSSCP00000053920; -.
DR PaxDb; 9823-ENSSSCP00000006551; -.
DR PeptideAtlas; Q5S1S4; -.
DR Ensembl; ENSSSCT00000006734.5; ENSSSCP00000006551.4; ENSSSCG00000006141.5.
DR Ensembl; ENSSSCT00005052521.1; ENSSSCP00005032438.1; ENSSSCG00005032882.1.
DR Ensembl; ENSSSCT00070032097.1; ENSSSCP00070026771.1; ENSSSCG00070016319.1.
DR Ensembl; ENSSSCT00070032110.1; ENSSSCP00070026784.1; ENSSSCG00070016319.1.
DR GeneID; 494016; -.
DR KEGG; ssc:494016; -.
DR CTD; 761; -.
DR VGNC; VGNC:86099; CA3.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000159435; -.
DR HOGENOM; CLU_039326_2_1_1; -.
DR InParanoid; Q5S1S4; -.
DR OMA; WHELYPN; -.
DR OrthoDB; 49814at2759; -.
DR TreeFam; TF316425; -.
DR Reactome; R-SSC-1475029; Reversible hydration of carbon dioxide.
DR Proteomes; UP000008227; Chromosome 4.
DR Proteomes; UP000314985; Chromosome 4.
DR Proteomes; UP000694570; Unplaced.
DR Proteomes; UP000694571; Unplaced.
DR Proteomes; UP000694720; Unplaced.
DR Proteomes; UP000694722; Unplaced.
DR Proteomes; UP000694723; Unplaced.
DR Proteomes; UP000694724; Unplaced.
DR Proteomes; UP000694725; Unplaced.
DR Proteomes; UP000694726; Unplaced.
DR Proteomes; UP000694727; Unplaced.
DR Proteomes; UP000694728; Unplaced.
DR Genevisible; Q5S1S4; SS.
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 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_0000077428"
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:P07451"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P07451"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P07451"
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 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; 29411 MW; 3256EF36BF48FC2F CRC64;
MAKEWGYADH NGPDHWHELY PIAKGDNQSP IELHTKDIKH DPSLLPWTAS YDPGSAKTIL
NNGKTCRVVF DDTYDRSMLR GGPLTAAYRL RQFHLHWGSS DDHGSEHTVD GVKYAAELHL
VHWNSKYNSF ATALKHPDGV AVVGIFLKIG REKGEFQLVL DALDKIKTKG KEAPFTNFNP
SCLFPACRDY WTYHGSFTTP PCEECIVWLL LKEPITVSSD QMAKLRSLYS SAENEPPVPL
VRNWRPPQPI KGRIVKASFK
//
