CAH2_TRIHK
ID CAH2_TRIHK Reviewed; 260 AA.
AC Q8UWA5;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Carbonic anhydrase 2;
DE EC=4.2.1.1 {ECO:0000250|UniProtKB:P00918};
DE AltName: Full=Carbonate dehydratase II;
DE AltName: Full=Carbonic anhydrase II;
DE Short=CA-II;
GN Name=ca2;
OS Tribolodon hakonensis (Big-scaled redfin) (Leuciscus hakonensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Leuciscidae; Pseudaspininae; Tribolodon.
OX NCBI_TaxID=151740;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12531781; DOI=10.1152/ajpregu.00267.2002;
RA Hirata T., Kaneko T., Ono T., Nakazato T., Furukawa N., Hasegawa S.,
RA Wakabayashi S., Shigekawa M., Chang M.H., Romero M.F., Hirose S.;
RT "Mechanism of acid adaptation of a fish living in a pH 3.5 lake.";
RL Am. J. Physiol. 284:R1199-R1212(2003).
CC -!- FUNCTION: Catalyzes the reversible hydration of carbon dioxide.
CC {ECO:0000250|UniProtKB:P00918}.
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:P00918};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00918};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00918}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; AB055617; BAB83090.1; -; mRNA.
DR AlphaFoldDB; Q8UWA5; -.
DR SMR; Q8UWA5; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; 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 PANTHER; PTHR18952; PTHR18952; 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 Cytoplasm; Lyase; Metal-binding; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT CHAIN 2..260
FT /note="Carbonic anhydrase 2"
FT /id="PRO_0000077424"
FT DOMAIN 3..259
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT ACT_SITE 64
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 198..199
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT SITE 7
FT /note="Fine-tunes the proton-transfer properties of H-64"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT SITE 62
FT /note="Fine-tunes the proton-transfer properties of H-64"
FT /evidence="ECO:0000250|UniProtKB:P00918"
SQ SEQUENCE 260 AA; 29133 MW; DA1D13C98307B88F CRC64;
MSHGWGYADH NGPQKWCENF PIANGPRQSP IDIQTKGASY DDTLKPLKLK YDPTTSLDIL
NNGHSFQVTF ADDNDSSMLT EGPISGKYRL KQFHFHWGAS DGKGSEHTVD GKCYPAELHL
VHWNTKYASF GEAANKPDGL AVVGVFLQIG EDNPKLQKIL DAMDAIKSKG KQTSFTNFDP
TCLLPKSLEY WTYPGSLTTP PLYESVTWIV CKQPISVSSE QMKKFRSLLF TAEEEKACCM
VNNYRPPQPL KDRKVCASFK
