CAH1_HORSE
ID CAH1_HORSE Reviewed; 261 AA.
AC P00917;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 121.
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 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 2-261, AND VARIANTS ASP-55; GLY-66; GLY-82; PHE-84;
RP HIS-116; GLY-158; ARG-184; TYR-213; ARG-223 AND ALA-225.
RX PubMed=6773961; DOI=10.1016/s0021-9258(19)70546-8;
RA Jabusch J.R., Bray R.P., Deutsch H.F.;
RT "Sequence of the low activity equine erythrocyte carbonic anhydrase and
RT delineation of the amino acid substitutions in various polymorphic forms.";
RL J. Biol. Chem. 255:9196-9204(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 -!- POLYMORPHISM: The sequence shown is that of the electrophoretically
CC homogeneous D isozyme. {ECO:0000269|PubMed:6773961}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
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DR PIR; A01140; CRHO1D.
DR STRING; 9796.ENSECAP00000007854; -.
DR BindingDB; P00917; -.
DR ChEMBL; CHEMBL4105955; -.
DR PaxDb; P00917; -.
DR PeptideAtlas; P00917; -.
DR InParanoid; P00917; -.
DR Proteomes; UP000002281; 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:0000250|UniProtKB:P00915,
FT ECO:0000269|PubMed:6773961"
FT CHAIN 2..261
FT /note="Carbonic anhydrase 1"
FT /id="PRO_0000077408"
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"
FT VARIANT 55
FT /note="A -> D (in isozyme T)"
FT /evidence="ECO:0000269|PubMed:6773961"
FT VARIANT 66
FT /note="S -> G (in homogeneous D isozyme)"
FT /evidence="ECO:0000269|PubMed:6773961"
FT VARIANT 82
FT /note="D -> G (in isozyme A2)"
FT /evidence="ECO:0000269|PubMed:6773961"
FT VARIANT 84
FT /note="P -> F (in isozyme A2)"
FT /evidence="ECO:0000269|PubMed:6773961"
FT VARIANT 116
FT /note="S -> H (in homogeneous D isozyme)"
FT /evidence="ECO:0000269|PubMed:6773961"
FT VARIANT 158
FT /note="L -> G (in homogeneous D isozyme)"
FT /evidence="ECO:0000269|PubMed:6773961"
FT VARIANT 184
FT /note="S -> R (in isozyme A1 and isozyme B)"
FT /evidence="ECO:0000269|PubMed:6773961"
FT VARIANT 213
FT /note="C -> Y (in homogeneous D isozyme)"
FT /evidence="ECO:0000269|PubMed:6773961"
FT VARIANT 223
FT /note="Q -> R (in isozyme B)"
FT /evidence="ECO:0000269|PubMed:6773961"
FT VARIANT 225
FT /note="S -> A (in homogeneous D isozyme)"
FT /evidence="ECO:0000269|PubMed:6773961"
FT UNSURE 12
FT /note="N or D"
FT UNSURE 25
FT /note="N or D"
FT UNSURE 27
FT /note="N or D"
FT UNSURE 28
FT /note="N or D"
SQ SEQUENCE 261 AA; 29025 MW; E2DD4D1BDAE62353 CRC64;
MAHSDWGYDS PNGPZEWVKL YPIANGNNQS PIDIKTSETK HDTSLKPFSV SYDPATAKEI
VNVGHSFQVK FEDSDNRSVL KDGPLPGSYR LVQFHFHWGS TDDYGSEHTV DGVKYSAELH
LVHWNSSKYS SFDEASSQAD GLAILGVLMK VGEANPKLQK VLDALNEVKT KGKKAPFKNF
DPSSLLPSSP DYWTYSGSLT HPPLYESVTW IVCKENISIS SQQLSQFRSL LSNVEGGKAV
PIQHNNRPPQ PLKGRTVRAF F
