ID A0A2Y9R1L0_TRIMA Unreviewed; 353 AA.
AC A0A2Y9R1L0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU367011};
DE EC=4.2.1.1 {ECO:0000256|RuleBase:RU367011};
GN Name=LOC101356619 {ECO:0000313|RefSeq:XP_023585468.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023585468.1};
RN [1] {ECO:0000313|RefSeq:XP_023585468.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Reversible hydration of carbon dioxide.
CC {ECO:0000256|RuleBase:RU367011}.
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|RuleBase:RU367011};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU367011};
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000256|ARBA:ARBA00010718, ECO:0000256|RuleBase:RU367011}.
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DR RefSeq; XP_023585468.1; XM_023729700.1.
DR AlphaFoldDB; A0A2Y9R1L0; -.
DR Proteomes; UP000248480; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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; IPR018338; Carbonic_anhydrase_a-class_CS.
DR PANTHER; PTHR18952; CARBONIC ANHYDRASE; 1.
DR PANTHER; PTHR18952:SF19; CARBONIC ANHYDRASE 12; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR PROSITE; PS00162; ALPHA_CA_1; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|RuleBase:RU367011}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367011};
KW Reference proteome {ECO:0000313|Proteomes:UP000248480};
KW Signal {ECO:0000256|RuleBase:RU367011};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU367011"
FT CHAIN 25..353
FT /note="Carbonic anhydrase"
FT /evidence="ECO:0000256|RuleBase:RU367011"
FT /id="PRO_5025093895"
FT TRANSMEM 298..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..289
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
SQ SEQUENCE 353 AA; 39631 MW; C81487A9933BA630 CRC64;
MPHRSLHAAA VLLLVILKEQ PSSPAPLNGS KWTYVGPDGE RSWSKKYSSC GGLMQSPIDL
HSDIIQYDAS LVPLEFQGYN VSANEQFILT NNGHSVKLSL TPNMYLLGLP FRYSATQLHL
HWGDQSNPHG SEHTISGRHF AAELHIVHYN SDLYPNASTA SNKSKGLAVL AVLIEMGSFN
PSYDKIFSHL QDVKYKGQEV PVPGFNVKEL LPERPEEFYR YMGSLTTPPC NPTVVWTVFR
NPVQISAEQL LALETALYYT HVDDPSRKEM VNNFRQVQKL DERLVYVSFR QDLTYEGLSV
GIILSVVLAG ILGICIVLGV FIWLFRRKKS KKGDSNKGVI YKRAIKKETE AHS
//
