ID   A0A3Q3WBD8_MOLML        Unreviewed;       539 AA.
AC   A0A3Q3WBD8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Carbonic anhydrase 6 {ECO:0000256|ARBA:ARBA00014200};
DE            EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925};
DE   AltName: Full=Carbonate dehydratase VI {ECO:0000256|ARBA:ARBA00031549};
DE   AltName: Full=Carbonic anhydrase VI {ECO:0000256|ARBA:ARBA00032196};
OS   Mola mola (Ocean sunfish) (Tetraodon mola).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Molidae; Mola.
OX   NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000011808.1, ECO:0000313|Proteomes:UP000261620};
RN   [1] {ECO:0000313|Ensembl:ENSMMOP00000011808.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Reversible hydration of carbon dioxide. Its role in saliva is
CC       unknown. {ECO:0000256|ARBA:ARBA00025355}.
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:0000256|ARBA:ARBA00000943};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000256|ARBA:ARBA00010718}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01172}.
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DR   AlphaFoldDB; A0A3Q3WBD8; -.
DR   STRING; 94237.ENSMMOP00000011808; -.
DR   Ensembl; ENSMMOT00000012008.1; ENSMMOP00000011808.1; ENSMMOG00000008843.1.
DR   OMA; HWATKYP; -.
DR   Proteomes; UP000261620; Unplaced.
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   CDD; cd03125; alpha_CA_VI; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1.
DR   InterPro; IPR001148; CA_dom.
DR   InterPro; IPR036398; CA_dom_sf.
DR   InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001759; Pentraxin-related.
DR   PANTHER; PTHR18952; CARBONIC ANHYDRASE; 1.
DR   PANTHER; PTHR18952:SF110; CARBONIC ANHYDRASE 6; 1.
DR   Pfam; PF00194; Carb_anhydrase; 1.
DR   Pfam; PF00354; Pentaxin; 1.
DR   PRINTS; PR00895; PENTAXIN.
DR   SMART; SM01057; Carb_anhydrase; 1.
DR   SMART; SM00159; PTX; 1.
DR   SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS51144; ALPHA_CA_2; 1.
DR   PROSITE; PS51828; PTX_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000261620};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..539
FT                   /note="Carbonic anhydrase 6"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018776197"
FT   DOMAIN          25..282
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000259|PROSITE:PS51144"
SQ   SEQUENCE   539 AA;  60692 MW;  AE1E746E6B02D68F CRC64;
     MELLSVFVSA LLVCVVFAGI PHDGIHWTYT EGALDQIHWP DKYPACGGKK QSPIDIQRRS
     VRHNPDIMQL ELSGYDAQKG NFLMSNNGHS VQIDLPPTMV ISKGLPGKYT AVQMHLHWGG
     WDLEASGAEH TVDGIRYMAE LHVVHYNSDK YKSFTEARDK PDGLAVLAFF YDDGHFENTY
     YSDFISNLVK IKYAGQSMNI SSIDVRSMLP ENLNHFFRYQ GSLTTPPCYE SILWTVFDTP
     ITLSHNQIRK LESTLMDIDN KTLWNDYRMA QPLNDRVVES SFLPRLGKGT FCRQDEIESR
     LLKIEGLITS LGKHIHSSGA RGTRPTRYES RGLFPLVLSF QEKNAGGYAL ARLSHSITLN
     AFTVCMHILP EFEEDNTIIS YASDSSENEL MITVSEDRDS REVGLWIGNE FVNLPHNYRT
     HDWTNYCITW SSQSGGADLW INGRVGEQRS LKSGYMISSS GMLILGKNQD GLLGISDAHT
     FVGKMTDVNV WDYVLTTADI RDQMSCERNS TAVGNVFSWG TTPLSLYGGV QLDGHYRCS
//