ID   A0A2K5ZBI7_MANLE        Unreviewed;       447 AA.
AC   A0A2K5ZBI7;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU367011};
DE            EC=4.2.1.1 {ECO:0000256|RuleBase:RU367011};
GN   Name=CA9 {ECO:0000313|Ensembl:ENSMLEP00000025179.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000025179.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000025179.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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_011835512.1; XM_011980122.1.
DR   AlphaFoldDB; A0A2K5ZBI7; -.
DR   STRING; 9568.ENSMLEP00000025179; -.
DR   Ensembl; ENSMLET00000048707.1; ENSMLEP00000025179.1; ENSMLEG00000036778.1.
DR   GeneID; 105539707; -.
DR   KEGG; mleu:105539707; -.
DR   CTD; 768; -.
DR   GeneTree; ENSGT00940000161646; -.
DR   OMA; MNFRATQ; -.
DR   OrthoDB; 49814at2759; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0140677; F:molecular function activator activity; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0002009; P:morphogenesis of an epithelium; IEA:Ensembl.
DR   GO; GO:0046903; P:secretion; IEA:Ensembl.
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:SF18; CARBONIC ANHYDRASE 9; 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:UP000233140};
KW   Signal {ECO:0000256|SAM:SignalP}; 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..37
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           38..447
FT                   /note="Carbonic anhydrase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014442291"
FT   TRANSMEM        403..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          127..378
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000259|PROSITE:PS51144"
FT   REGION          41..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..76
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..99
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..129
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   447 AA;  48469 MW;  2E037F1DAA7330E9 CRC64;
     MAPLCPSPWL PLLIPAPAPG LTVQLLLSLL LLVPAHPQRL PRMQEDSPLG GGSSGEDDPL
     HEEDLLSEED PPREEDPPRE EDLPEVKPKS EEEGSLKLED LPTVEAPGDP QEPQNNAHGD
     KEGDNQRHWR YGGDPPWPQV SPACAGRFQS PVDIRPQLAA FCPALRPLEL LGFELPLLPE
     LRLRNNGHSV QLTLPSGLEM ALGPGREYRA LQLHLHWGAA GRPGSEHTVE GHRFPAEIHV
     VHLSTAYARV EEALGLPGGL AVLAAFLEEG PEENSAYEQL LSHLEEIAEE GSETQVPGLD
     VSALLPSDLS RYFRYEGSLT TPPCAQGVIW TVFNQTVMLS AKQLHTLSDA LWGPGDSRLQ
     LNFRVTQPLN GRVIEASFPA GVDSSPRAAE PVQLNSCLAA GDILALVFGL LFAVTSVAFL
     VQMRRQHRRG TKGGVSYHPA EVAETGA
//