ID   CAH5_CAEEL              Reviewed;         310 AA.
AC   Q10462;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 3.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Putative carbonic anhydrase 5;
DE            EC=4.2.1.1;
DE   AltName: Full=Carbonate dehydratase 5;
DE   Flags: Precursor;
GN   Name=cah-5; ORFNames=R173.1;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000305}.
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DR   EMBL; FO080190; CCD61848.1; -; Genomic_DNA.
DR   PIR; T16772; T16772.
DR   RefSeq; NP_509186.3; NM_076785.4.
DR   AlphaFoldDB; Q10462; -.
DR   SMR; Q10462; -.
DR   STRING; 6239.R173.1; -.
DR   EPD; Q10462; -.
DR   PaxDb; Q10462; -.
DR   PeptideAtlas; Q10462; -.
DR   EnsemblMetazoa; R173.1.1; R173.1.1; WBGene00000283.
DR   GeneID; 180972; -.
DR   KEGG; cel:CELE_R173.1; -.
DR   UCSC; R173.1; c. elegans.
DR   CTD; 180972; -.
DR   WormBase; R173.1; CE36560; WBGene00000283; cah-5.
DR   eggNOG; KOG0382; Eukaryota.
DR   GeneTree; ENSGT00940000172445; -.
DR   HOGENOM; CLU_039326_2_0_1; -.
DR   InParanoid; Q10462; -.
DR   OMA; GGLKHRY; -.
DR   OrthoDB; 1377476at2759; -.
DR   PhylomeDB; Q10462; -.
DR   Reactome; R-CEL-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR   Reactome; R-CEL-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR   Reactome; R-CEL-1475029; Reversible hydration of carbon dioxide.
DR   PRO; PR:Q10462; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00000283; Expressed in larva and 3 other tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IBA:GO_Central.
DR   GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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   3: Inferred from homology;
KW   Lyase; Metal-binding; Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..310
FT                   /note="Putative carbonic anhydrase 5"
FT                   /id="PRO_0000004256"
FT   DOMAIN          26..280
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   BINDING         117
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         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   BINDING         223..224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   310 AA;  34862 MW;  696A8ED5355DB186 CRC64;
     MPSHLLVLSL LVALLVVVSC GPGSDHGWGY DENNGPDTWQ GKCQNHLKQS PIDIRAPDVD
     YALLHRMHFL NYDMDGKIEL SNTGRTLFAG GFESWQHKQP MIQGGGLKHR YKLAQFHLHW
     GQNDAVGSEH AMGSLHYPAE LHLVHVREGL TLKEALSRPD GLAVVGVFLA KTNDPVANKF
     SPISERLHDL RHSGNKTELK NFRTKYVLPL DTEAFYRYEG SLTTPDCSEA VIWTVLAEPM
     AISSHQLHLL RQLHNKELVK SDKNYRPLQP LNGRRIQYRP SKLDRAMICS SFATTSVIIT
     YVAILSAMLI