ID   CAHZ_DANRE              Reviewed;         260 AA.
AC   Q92051;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Carbonic anhydrase;
DE            EC=4.2.1.1;
DE   AltName: Full=Carbonate dehydratase;
GN   Name=cahz; Synonyms=cah-z;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=9089083; DOI=10.1007/pl00006163;
RA   Peterson R.E., Tu C., Linser P.J.;
RT   "Isolation and characterization of a carbonic anhydrase homologue from the
RT   zebrafish (Danio rerio).";
RL   J. Mol. Evol. 44:432-439(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Reversible hydration of carbon dioxide.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000305}.
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DR   EMBL; U55177; AAB82303.1; -; mRNA.
DR   EMBL; BC065611; AAH65611.1; -; mRNA.
DR   PIR; T08463; T08463.
DR   RefSeq; NP_571185.1; NM_131110.1.
DR   AlphaFoldDB; Q92051; -.
DR   SMR; Q92051; -.
DR   STRING; 7955.ENSDARP00000022592; -.
DR   PaxDb; Q92051; -.
DR   Ensembl; ENSDART00000013411; ENSDARP00000022592; ENSDARG00000011166.
DR   GeneID; 30331; -.
DR   KEGG; dre:30331; -.
DR   CTD; 30331; -.
DR   ZFIN; ZDB-GENE-980526-39; cahz.
DR   eggNOG; KOG0382; Eukaryota.
DR   GeneTree; ENSGT00940000166576; -.
DR   HOGENOM; CLU_039326_2_1_1; -.
DR   InParanoid; Q92051; -.
DR   OMA; IIMSHSW; -.
DR   OrthoDB; 1377476at2759; -.
DR   PhylomeDB; Q92051; -.
DR   TreeFam; TF316425; -.
DR   Reactome; R-DRE-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR   Reactome; R-DRE-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR   Reactome; R-DRE-1475029; Reversible hydration of carbon dioxide.
DR   PRO; PR:Q92051; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 2.
DR   Bgee; ENSDARG00000011166; Expressed in spleen and 37 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IMP:ZFIN.
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; IMP:ZFIN.
DR   GO; GO:0042539; P:hypotonic salinity response; IDA:ZFIN.
DR   GO; GO:0006730; P:one-carbon metabolic process; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Lyase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..260
FT                   /note="Carbonic anhydrase"
FT                   /id="PRO_0000077442"
FT   DOMAIN          3..259
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        64
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   ACT_SITE        127
FT                   /evidence="ECO:0000250"
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"
SQ   SEQUENCE   260 AA;  28677 MW;  35C0C871B13A6256 CRC64;
     MAHAWGYGPA DGPESWAESF PIANGPRQSP IDIVPTQAQH DPSLKHLKLK YDPATTKSIL
     NNGHSFQVDF VDDDNSSTLA GGPITGIYRL RQFHFHWGSS DDKGSEHTIA GTKFPCELHL
     VHWNTKYPNF GEAASKPDGL AVVGVFLKIG AANPRLQKVL DALDDIKSKG RQTTFANFDP
     KTLLPASLDY WTYEGSLTTP PLLESVTWIV LKEPISVSPA QMAKFRSLLF SSEGETPCCM
     VDNYRPPQPL KGRKVRASFK