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Database: UniProt
Entry: Q20781
LinkDB: Q20781
Original site: Q20781 
ID   CAH1_CAEEL              Reviewed;         365 AA.
AC   Q20781;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=Putative carbonic anhydrase-like protein 1;
DE   Flags: Precursor;
GN   Name=cah-1; ORFNames=F54D8.4;
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Has lost two of the three potential zinc-binding residues and
CC       therefore may not be active. {ECO:0000305}.
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DR   EMBL; FO080874; CCD67410.1; -; Genomic_DNA.
DR   PIR; F88449; F88449.
DR   RefSeq; NP_001309492.1; NM_001322586.1.
DR   AlphaFoldDB; Q20781; -.
DR   SMR; Q20781; -.
DR   STRING; 6239.F54D8.4a.1; -.
DR   PaxDb; 6239-F54D8-4; -.
DR   EnsemblMetazoa; F54D8.4a.1; F54D8.4a.1; WBGene00000279.
DR   GeneID; 186231; -.
DR   KEGG; cel:CELE_F54D8.4; -.
DR   UCSC; F54D8.4; c. elegans.
DR   AGR; WB:WBGene00000279; -.
DR   WormBase; F54D8.4a; CE51243; WBGene00000279; cah-1.
DR   eggNOG; KOG0382; Eukaryota.
DR   GeneTree; ENSGT00940000169337; -.
DR   HOGENOM; CLU_039326_7_1_1; -.
DR   InParanoid; Q20781; -.
DR   OMA; QMPRIRI; -.
DR   OrthoDB; 49814at2759; -.
DR   PhylomeDB; Q20781; -.
DR   PRO; PR:Q20781; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00000279; Expressed in anatomical system and 4 other cell types or tissues.
DR   ExpressionAtlas; Q20781; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:InterPro.
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   CDD; cd03121; alpha_CARP_X_XI_like; 1.
DR   Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 2.
DR   InterPro; IPR041878; Alpha_CARP_X/XI.
DR   InterPro; IPR001148; CA_dom.
DR   InterPro; IPR036398; CA_dom_sf.
DR   InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR   PANTHER; PTHR18952; CARBONIC ANHYDRASE; 1.
DR   PANTHER; PTHR18952:SF138; CARBONIC ANHYDRASE-RELATED PROTEIN 10; 1.
DR   Pfam; PF00194; Carb_anhydrase; 1.
DR   SMART; SM01057; Carb_anhydrase; 1.
DR   SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR   PROSITE; PS51144; ALPHA_CA_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..365
FT                   /note="Putative carbonic anhydrase-like protein 1"
FT                   /id="PRO_0000004254"
FT   DOMAIN          28..356
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   ACT_SITE        223
FT                   /evidence="ECO:0000250"
FT   BINDING         295..296
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         295
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   365 AA;  42442 MW;  4071A2349AF41380 CRC64;
     MRFECSHFPL FLIILTCHIS PLKSSQNYQW SYDSDVFGGP HFWGLVEKDW WMCKKGRLQS
     PIDIQPDRLL FDASVKPVSY AELNFFLIIY LTISLKLMRY IFTCAHLFAC NKKLGTWNRI
     FGANIAKFRA WVVYIIIFHA QVPQLQVVSE FVNTGQMVRV RIGYSSKKPS VNITSGPLYG
     YRYRVQRIDF HMGRKNENGS EHTINGRRFP MEVQLVAYNT DLYPNFTSAS KSPHGIAILS
     VLVDFGPETN QELIKLTIAT ASISYKDQRV QLADFEPWRL LPFTRDIITY EGSLTSPGCH
     ETVTWIILNQ PIFIKKEHFE EWSHLYLSME GAEKVPVAPN FRKIQETNNR LVRTNIQHKV
     WIFLS
//
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