CAH1_MACMU
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 03-AUG-2022, entry version 126.
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 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.
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 PIR; A01139; CRMQ1R.
DR AlphaFoldDB; P00916; -.
DR SMR; P00916; -.
DR STRING; 9544.ENSMMUP00000018892; -.
DR BindingDB; P00916; -.
DR ChEMBL; CHEMBL4105729; -.
DR iPTMnet; P00916; -.
DR PRIDE; P00916; -.
DR eggNOG; KOG0382; Eukaryota.
DR InParanoid; P00916; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:InterPro.
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 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
