ID   CAH2_CAEEL              Reviewed;         337 AA.
AC   Q18932;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 3.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Putative carbonic anhydrase-like protein 2;
DE   Flags: Precursor;
GN   Name=cah-2; ORFNames=D1022.8;
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).
RN   [2]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-188, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Bristol N2;
RX   PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA   Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA   Taoka M., Takahashi N., Isobe T.;
RT   "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT   elegans and suggests an atypical translocation mechanism for integral
RT   membrane proteins.";
RL   Mol. Cell. Proteomics 6:2100-2109(2007).
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; FO080995; CCD68342.1; -; Genomic_DNA.
DR   PIR; T34196; T34196.
DR   RefSeq; NP_495567.3; NM_063166.6.
DR   AlphaFoldDB; Q18932; -.
DR   SMR; Q18932; -.
DR   BioGRID; 39553; 4.
DR   DIP; DIP-25432N; -.
DR   IntAct; Q18932; 1.
DR   STRING; 6239.D1022.8; -.
DR   iPTMnet; Q18932; -.
DR   EPD; Q18932; -.
DR   PaxDb; Q18932; -.
DR   PRIDE; Q18932; -.
DR   EnsemblMetazoa; D1022.8.1; D1022.8.1; WBGene00000280.
DR   GeneID; 174218; -.
DR   KEGG; cel:CELE_D1022.8; -.
DR   UCSC; D1022.8; c. elegans.
DR   CTD; 174218; -.
DR   WormBase; D1022.8; CE31777; WBGene00000280; cah-2.
DR   eggNOG; KOG0382; Eukaryota.
DR   HOGENOM; CLU_039326_7_1_1; -.
DR   InParanoid; Q18932; -.
DR   OMA; HAINGYS; -.
DR   OrthoDB; 1377476at2759; -.
DR   PhylomeDB; Q18932; -.
DR   PRO; PR:Q18932; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00000280; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
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; -; 1.
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; PTHR18952; 1.
DR   Pfam; PF00194; Carb_anhydrase; 1.
DR   SMART; SM01057; Carb_anhydrase; 1.
DR   SUPFAM; SSF51069; SSF51069; 1.
DR   PROSITE; PS51144; ALPHA_CA_2; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..337
FT                   /note="Putative carbonic anhydrase-like protein 2"
FT                   /id="PRO_0000004255"
FT   DOMAIN          17..274
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   ACT_SITE        140
FT                   /evidence="ECO:0000250"
FT   BINDING         212..213
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        188
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17761667"
SQ   SEQUENCE   337 AA;  37631 MW;  4DFE8DF46FF0458A CRC64;
     MIPWLLTACI YPCVIGPDFW GLLHGDWRMC TAGQMQSPVN IDPSQLLYDP HLMPINIEGN
     IVEAVFENTG QLPVVTVKDL PNRPTINITG GPTMPYRYKL HQISVHFGRA DEGEKGSEHT
     VDRVRFPAEI QLLAYNSALY PNFSVAMTSP RGLLAVSVIV DIGKTTSVEL RRLTVASQSI
     NYKGQTTNLT DFQPSALLPK TSHYVTYEGS LTFPGCHETV TWVILNNPIY ITNDDLQIWN
     EMQKTETKQP EPSYMTPAYR PLKSLNGRLV RTNINVGSKQ STVSSSCPSN VYVEMGYQAN
     PGRNKRNDSV SRRYVPTSEV FEIDSIRPDD VSKAGSF