CAH2_CHICK
ID CAH2_CHICK Reviewed; 260 AA.
AC P07630;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 173.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hubbard White Mountain; TISSUE=Testis;
RX PubMed=7926806; DOI=10.1016/0378-1119(94)90072-8;
RA Mezquita J., Pau M., Mezquita C.;
RT "A novel carbonic anhydrase II mRNA isolated from mature chicken testis
RT displays a TATA box and other promoter sequences in a leader 5'
RT untranslated region not present in somatic tissues.";
RL Gene 147:231-235(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=White leghorn;
RX PubMed=3029691; DOI=10.1093/nar/15.2.753;
RA Yoshihara C.M., Lee J.-D., Dodgson J.B.;
RT "The chicken carbonic anhydrase II gene: evidence for a recent shift in
RT intron position.";
RL Nucleic Acids Res. 15:753-770(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-260.
RC STRAIN=White leghorn; TISSUE=Retina;
RX PubMed=3102231; DOI=10.1111/j.1432-1033.1987.tb10550.x;
RA Rogers J.H.;
RT "Sequence of carbonic anhydrase II cDNA from chick retina.";
RL Eur. J. Biochem. 162:119-122(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 222-260.
RC TISSUE=Retina;
RX PubMed=1969140; DOI=10.1093/nar/18.4.1049;
RA Godbout R., Andison R., Upton C., Day R.;
RT "Utilization of the second polyadenylation signal at the 3' end of the
RT chicken carbonic anhydrase II gene.";
RL Nucleic Acids Res. 18:1049-1049(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-87.
RX PubMed=6331256; DOI=10.1111/j.1749-6632.1984.tb12357.x;
RA Yoshihara C.M., Federspiel M., Dodgson J.B.;
RT "Isolation of the chicken carbonic anhydrase II gene.";
RL Ann. N. Y. Acad. Sci. 429:332-334(1984).
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:P00921};
CC -!- ACTIVITY REGULATION: Inhibited by acetazolamide.
CC {ECO:0000250|UniProtKB:P00918}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00918}. Cell
CC membrane {ECO:0000250|UniProtKB:P00918}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; Z14957; CAA78681.1; -; mRNA.
DR EMBL; X12639; CAA31175.1; -; mRNA.
DR EMBL; X06000; CAA29417.1; -; Genomic_DNA.
DR EMBL; X06001; CAA29417.1; JOINED; Genomic_DNA.
DR EMBL; X06002; CAA29417.1; JOINED; Genomic_DNA.
DR EMBL; X06003; CAA29417.1; JOINED; Genomic_DNA.
DR EMBL; X06004; CAA29417.1; JOINED; Genomic_DNA.
DR EMBL; X06005; CAA29417.1; JOINED; Genomic_DNA.
DR EMBL; X04810; CAA28501.1; -; mRNA.
DR EMBL; X17378; CAA35250.1; -; mRNA.
DR EMBL; M25943; AAA48646.1; -; mRNA.
DR PIR; JC2580; JC2580.
DR RefSeq; NP_990648.1; NM_205317.1.
DR AlphaFoldDB; P07630; -.
DR SMR; P07630; -.
DR STRING; 9031.ENSGALP00000025525; -.
DR PaxDb; P07630; -.
DR Ensembl; ENSGALT00000052439; ENSGALP00000056391; ENSGALG00000030781.
DR GeneID; 396257; -.
DR KEGG; gga:396257; -.
DR CTD; 760; -.
DR VEuPathDB; HostDB:geneid_396257; -.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000160385; -.
DR HOGENOM; CLU_039326_2_1_1; -.
DR InParanoid; P07630; -.
DR OMA; SADFPNF; -.
DR OrthoDB; 1377476at2759; -.
DR PhylomeDB; P07630; -.
DR TreeFam; TF316425; -.
DR Reactome; R-GGA-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR Reactome; R-GGA-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR Reactome; R-GGA-1475029; Reversible hydration of carbon dioxide.
DR PRO; PR:P07630; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000030781; Expressed in lung and 13 other tissues.
DR GO; GO:0045177; C:apical part of cell; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004089; F:carbonate dehydratase activity; IDA:AgBase.
DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015670; P:carbon dioxide transport; IBA:GO_Central.
DR GO; GO:0071244; P:cellular response to carbon dioxide; IDA:AgBase.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
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 Cell membrane; Cytoplasm; Lyase; Membrane; Metal-binding;
KW Reference proteome; 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_0000077423"
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:0000250|UniProtKB:P00918"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00918"
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"
FT SITE 67
FT /note="Fine-tunes the proton-transfer properties of H-64"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT CONFLICT 5
FT /note="W -> L (in Ref. 3; CAA28501)"
FT /evidence="ECO:0000305"
FT CONFLICT 8
FT /note="D -> G (in Ref. 5; AAA48646)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="V -> S (in Ref. 5; AAA48646)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="L -> V (in Ref. 2; CAA31175/CAA29417)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 260 AA; 29008 MW; 6723309BC77A4950 CRC64;
MSHHWGYDSH NGPAHWHEHF PIANGERQSP IAISTKAARY DPALKPLSFS YDAGTAKAIV
NNGHSFNVEF DDSSDKSVLQ GGALDGVYRL VQFHIHWGSC EGQGSEHTVD GVKYDAELHI
VHWNVKYGKF AEALKHPDGL AVVGIFMKVG NAKPEIQKVV DALNSIQTKG KQASFTNFDP
TGLLPPCRDY WTYPGSLTTP PLHECVIWHV LKEPITVSSE QMCKLRGLCF SAENEPVCRM
VDNWRPCQPL KSREVRASFQ
