CAH1_SHEEP
ID CAH1_SHEEP Reviewed; 261 AA.
AC P48282;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 113.
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 Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Dorset; TISSUE=Ruminal epithelium;
RX PubMed=8690670; DOI=10.2527/1996.742345x;
RA Wang L.Q., Baldwin R.L., Jesse B.W.;
RT "Isolation and characterization of a cDNA clone encoding ovine type I
RT carbonic anhydrase.";
RL J. Anim. Sci. 74:345-353(1996).
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; L42178; AAC41634.1; -; mRNA.
DR RefSeq; NP_001009771.1; NM_001009771.1.
DR AlphaFoldDB; P48282; -.
DR SMR; P48282; -.
DR STRING; 9940.ENSOARP00000014236; -.
DR Ensembl; ENSOART00020012090; ENSOARP00020009960; ENSOARG00020007556.
DR GeneID; 443309; -.
DR KEGG; oas:443309; -.
DR CTD; 759; -.
DR eggNOG; KOG0382; Eukaryota.
DR Proteomes; UP000002356; 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 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_0000077416"
FT DOMAIN 4..261
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT REGION 22..41
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:0000250|UniProtKB:P00915"
SQ SEQUENCE 261 AA; 28898 MW; EA1E908F44F171CE CRC64;
MASPDWGYDG ENGPEHWCKL HPIANGNNQS PIDIKTSETK RDPSLKPLSI SYNPATAKEI
VNVGHSFHVN FEDSDNRSVL KGGPLPESYR LRQFHFHWGS TDDCGSEHLV DGATFSAELH
LVHWNSAKYP SFADAASQAD GLVVVGVLMK VGQANPNLQK VLDALKTVKT KNKKAPFTNF
DPSVLLPSCP DYWAYFGSLT HPPLHESVTW IIFKETISVS AEQLAQFRSL LANAEGDKEV
CIKQNYRPPQ PLKGRTVKAS F
