ID   CAH1_LOTGI              Reviewed;         395 AA.
AC   B3A0P2;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Putative carbonic anhydrase 1;
DE            EC=4.2.1.1 {ECO:0000250|UniProtKB:P00921};
DE   AltName: Full=Putative carbonate dehydratase 1;
DE   Flags: Precursor;
OS   Lottia gigantea (Giant owl limpet).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX   NCBI_TaxID=225164;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND IDENTIFICATION.
RC   TISSUE=Mantle {ECO:0000269|Ref.1};
RA   Richardson P., Lucas S., Rokhsar D., Wang M., Lindquist E.A.;
RT   "DOE Joint Genome Institute Lottia gigantea EST project.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 36-47; 54-64; 72-92; 97-145; 148-281; 285-319; 323-365
RP   AND 371-395, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Shell;
RX   PubMed=23145877; DOI=10.1111/febs.12062;
RA   Marie B., Jackson D.J., Ramos-Silva P., Zanella-Cleon I., Guichard N.,
RA   Marin F.;
RT   "The shell-forming proteome of Lottia gigantea reveals both deep
RT   conservations and lineage-specific novelties.";
RL   FEBS J. 280:214-232(2013).
CC   -!- FUNCTION: Reversible hydration of carbon dioxide.
CC       {ECO:0000250|UniProtKB:P00921}.
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:P00921};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P00921};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23145877}.
CC   -!- TISSUE SPECIFICITY: Component of the acid-insoluble and acid-soluble
CC       organic matrix of calcified layers of the shell (at protein level).
CC       {ECO:0000269|PubMed:23145877}.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000255}.
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DR   EMBL; FC624150; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; FC625698; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_009047380.1; XM_009049132.1.
DR   AlphaFoldDB; B3A0P2; -.
DR   SMR; B3A0P2; -.
DR   EnsemblMetazoa; LotgiT238082; LotgiP238082; LotgiG238082.
DR   GeneID; 20250653; -.
DR   KEGG; lgi:LOTGIDRAFT_238082; -.
DR   CTD; 20250653; -.
DR   HOGENOM; CLU_698865_0_0_1; -.
DR   OrthoDB; 1377476at2759; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.10.200.10; -; 2.
DR   InterPro; IPR001148; CA_dom.
DR   InterPro; IPR036398; CA_dom_sf.
DR   InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR   PANTHER; PTHR18952; PTHR18952; 2.
DR   Pfam; PF00194; Carb_anhydrase; 2.
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   Direct protein sequencing; Lyase; Metal-binding; Secreted; Signal; Zinc.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..395
FT                   /note="Putative carbonic anhydrase 1"
FT                   /id="PRO_0000415261"
FT   DOMAIN          42..365
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   BINDING         139
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00921"
FT   BINDING         141
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00921"
FT   BINDING         165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00921"
FT   CONFLICT        126..130
FT                   /note="GSPVG -> EVQWV (in Ref. 1; FC625698)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   395 AA;  44718 MW;  B542C7D9A22AC7BC CRC64;
     MKLQGAGCVV AAVLGALFIV NVESHFHKPE LQLCKAFGEP CISYDVRSTI GPRCWFKLEF
     PREKCCNENG KRQSPIDIPD VKSIYKVPQK LRYSSRKFVG HLENTGIQPA FKRKVGADKV
     YLEGIGSPVG KRYFIENVHF HVGVRHKERQ TENTLNGRSF DGEAHIVHIR EDFGDLKEAA
     NHPQGLLVIS IFLSTSKGER RRDGFDDLIE MIQDVQEFEE EDGPCANVKI PDIFKFKQLI
     PFHPVWPICK KTFPVADDSD NSGSGVVCNF YLPNGLCGEK KESKINPNEL LADDPEYYVF
     NGGLTTPPCS ESVLWLVAKQ PRKVSVFYPY VVRNMETQRE GEIIGDFGNL RPLQDLNDRP
     VFLVRFRLKR NWEHGDTAAN DNDAMDSPFS VLGIN