ID   CAH1_BOVIN              Reviewed;         261 AA.
AC   Q1LZA1;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Carbonic anhydrase 1;
DE            EC=4.2.1.1 {ECO:0000250|UniProtKB:P00915};
DE   AltName: Full=Carbonate dehydratase I;
DE   AltName: Full=Carbonic anhydrase I;
DE            Short=CA-I;
GN   Name=CA1;
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=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible hydration of carbon dioxide.
CC       {ECO:0000250|UniProtKB:P00915}.
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:P00915};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P00915};
CC   -!- ACTIVITY REGULATION: Inhibited by acetazolamide.
CC       {ECO:0000250|UniProtKB:P00915}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B0BNN3}.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000305}.
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DR   EMBL; BC116126; AAI16127.1; -; mRNA.
DR   RefSeq; NP_001068934.1; NM_001075466.1.
DR   AlphaFoldDB; Q1LZA1; -.
DR   SMR; Q1LZA1; -.
DR   STRING; 9913.ENSBTAP00000043090; -.
DR   PaxDb; Q1LZA1; -.
DR   PeptideAtlas; Q1LZA1; -.
DR   Ensembl; ENSBTAT00000045723; ENSBTAP00000043090; ENSBTAG00000032236.
DR   GeneID; 510801; -.
DR   KEGG; bta:510801; -.
DR   CTD; 759; -.
DR   VEuPathDB; HostDB:ENSBTAG00000032236; -.
DR   eggNOG; KOG0382; Eukaryota.
DR   GeneTree; ENSGT00940000161270; -.
DR   HOGENOM; CLU_039326_2_1_1; -.
DR   InParanoid; Q1LZA1; -.
DR   OMA; ERFHFHD; -.
DR   OrthoDB; 1377476at2759; -.
DR   TreeFam; TF316425; -.
DR   Reactome; R-BTA-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR   Reactome; R-BTA-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR   Reactome; R-BTA-1475029; Reversible hydration of carbon dioxide.
DR   Proteomes; UP000009136; Chromosome 14.
DR   Bgee; ENSBTAG00000032236; Expressed in caecum and 36 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IBA:GO_Central.
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   InterPro; IPR018442; Carbonic_anhydrase_CA1.
DR   PANTHER; PTHR18952; PTHR18952; 1.
DR   PANTHER; PTHR18952:SF82; PTHR18952:SF82; 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; Lyase; Metal-binding; Reference proteome; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P00915"
FT   CHAIN           2..261
FT                   /note="Carbonic anhydrase 1"
FT                   /id="PRO_0000262536"
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:P00915"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00915"
FT   BINDING         120
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00915"
FT   BINDING         200..201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00918"
FT   BINDING         200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00915"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P00915"
SQ   SEQUENCE   261 AA;  28822 MW;  65317265D77C3179 CRC64;
     MASPDWGYDG ENGPEHWGKL YPIANGNNQS PIDIKTSETK RDPSLKPLSV SYNPATAKEI
     VNVGHSFHVN FEDSDNRSVL KGGPLSESYR LRQFHFHWGI TDDCGSEHLV DGAKFSAELH
     LVHWNSAKYP SFADAASQAD GLALIGVLVK VGQANPNLQK VLDALKAVKN KNKKAPFTNF
     DPSVLLPPSL DYWAYSGSLT HPPLHESVTW IIFKETISVS SEQLAQFRSL LANAEGDREV
     HIKQNNRPPQ PLNGRTVKAS F