ID   A0A2K5U949_MACFA        Unreviewed;       336 AA.
AC   A0A2K5U949;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU367011};
DE            EC=4.2.1.1 {ECO:0000256|RuleBase:RU367011};
GN   Name=CA6 {ECO:0000313|Ensembl:ENSMFAP00000008891.2};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000008891.2, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000008891.2, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000008891.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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         ECO:0000256|RuleBase:RU367011};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU367011};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000256|ARBA:ARBA00010718, ECO:0000256|RuleBase:RU367011}.
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DR   AlphaFoldDB; A0A2K5U949; -.
DR   STRING; 9541.ENSMFAP00000008891; -.
DR   Ensembl; ENSMFAT00000021162.2; ENSMFAP00000008891.2; ENSMFAG00000001059.2.
DR   VEuPathDB; HostDB:ENSMFAG00000001059; -.
DR   GeneTree; ENSGT00940000160409; -.
DR   OrthoDB; 49814at2759; -.
DR   Proteomes; UP000233100; Chromosome 1.
DR   Bgee; ENSMFAG00000001059; Expressed in lymph node and 4 other cell types or tissues.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; IEA:Ensembl.
DR   CDD; cd03125; alpha_CA_VI; 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; IPR018338; Carbonic_anhydrase_a-class_CS.
DR   PANTHER; PTHR18952; CARBONIC ANHYDRASE; 1.
DR   PANTHER; PTHR18952:SF110; CARBONIC ANHYDRASE 6; 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};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU367011};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW   Signal {ECO:0000256|RuleBase:RU367011};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|RuleBase:RU367011"
FT   CHAIN           22..336
FT                   /note="Carbonic anhydrase"
FT                   /evidence="ECO:0000256|RuleBase:RU367011"
FT                   /id="PRO_5030001042"
FT   DOMAIN          25..282
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000259|PROSITE:PS51144"
FT   REGION          279..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..326
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   336 AA;  37886 MW;  E31C23430D4E0296 CRC64;
     MCSTMRALVP LLSLFLLGGQ AQHGSDWTYS EGALDEAHWP QHYPACGGQR QSPINLQRTK
     VRYNPALKGL KLTGYETQEG EFPMVNNGHT VQISLPSTMR MTAADGTVYI AQQMHFHWGG
     ASSKIRGSEH TVDGIRHVIE IHVVHYNSKY KSYETAQDAP DGLAVLAAFV EVKDYPENTY
     YSSFISHLAN IKYPGQTTTL TGLDIRDMLP KNLQHYYSYD GSLTTPPCTE NVHWFVLADF
     VKLSRTQVWK LENSLLDHHN KTIQNDYRRT QPLNHRVVES NFPNQGKGHL ASREKTKSKS
     KAHVNTPPLG SRQPRSLSSN TVKTHKDNIL GTRRAF
//