ID   CAH1_MACMU              Reviewed;         261 AA.
AC   P00916;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   02-SEP-2026, entry version 138.
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;
DE   AltName: Full=Cyanamide hydratase CA1;
DE            EC=4.2.1.69 {ECO:0000250|UniProtKB:P00915};
GN   Name=CA1;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-261, AND ACETYLATION AT ALA-2.
RX   PubMed=6776950; DOI=10.1016/0006-291x(80)91191-2;
RA   Henriksson D., Tanis R.J., Tashian R.E.;
RT   "The amino acid sequence of carbonic anhydrase I from the rhesus macaque.";
RL   Biochem. Biophys. Res. Commun. 96:135-142(1980).
CC   -!- FUNCTION: Catalyzes the reversible hydration of carbon dioxide. Can
CC       hydrate cyanamide to urea. {ECO:0000250|UniProtKB:P00915}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrogencarbonate + H(+) = 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=urea = cyanamide + H2O; Xref=Rhea:RHEA:23056,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:16698; EC=4.2.1.69;
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   PIR; A01139; CRMQ1R.
DR   AlphaFoldDB; P00916; -.
DR   SMR; P00916; -.
DR   FunCoup; P00916; 155.
DR   STRING; 9544.ENSMMUP00000079046; -.
DR   BindingDB; P00916; -.
DR   ChEMBL; CHEMBL4105729; -.
DR   iPTMnet; P00916; -.
DR   PaxDb; 9544-ENSMMUP00000079046; -.
DR   eggNOG; KOG0382; Eukaryota.
DR   InParanoid; P00916; -.
DR   Proteomes; UP000006718; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0004089; F:carbonate dehydratase activity; ISS:UniProtKB.
DR   GO; GO:0018820; F:cyanamide hydratase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   FunFam; 3.10.200.10:FF:000001; Carbonic anhydrase 2; 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:SF282; CARBONIC ANHYDRASE 1; 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; Lyase; Metal-binding;
KW   Reference proteome; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:6776950"
FT   CHAIN           2..261
FT                   /note="Carbonic anhydrase 1"
FT                   /id="PRO_0000077410"
FT   DOMAIN          4..261
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   REGION          238..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000269|PubMed:6776950"
SQ   SEQUENCE   261 AA;  28936 MW;  330428FA5D2DB5E0 CRC64;
     MASPDWGYDD KNGPEQWSKL YPIANGNNQS PVDIKTSEAK HDTSLKPISV SYNPATAKEI
     INVGHSFHVN FEDNDNRSVL KGGPFSDSYR LFQFHFHWGS SNEYGSEHTV DGVKYSSELH
     IVHWNSAKYS SLAEAVSKAD GLAVIGVLMK VGEANPKLQK VLDALHAIKT KGKRAPFTNF
     DPSTLLPSSL DFWTYSGSLT HPPLYESVTW IICKESISVS SEQLAQFRSL LSNVEGSNPV
     PIQRNNRPTQ PLKGRTVRAS F
//