ID A0A0D9RL45_CHLSB Unreviewed; 261 AA.
AC A0A0D9RL45;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU367011};
DE EC=4.2.1.1 {ECO:0000256|RuleBase:RU367011};
GN Name=CA1 {ECO:0000313|Ensembl:ENSCSAP00000009334.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000009334.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000009334.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000009334.1}
RP IDENTIFICATION.
RG Ensembl;
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|ARBA:ARBA00000943,
CC ECO:0000256|RuleBase:RU367011};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=urea = cyanamide + H2O; Xref=Rhea:RHEA:23056,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:16698; EC=4.2.1.69;
CC Evidence={ECO:0000256|ARBA:ARBA00036058};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU367011};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000256|ARBA:ARBA00010718, ECO:0000256|RuleBase:RU367011}.
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DR EMBL; AQIB01087648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007999193.1; XM_008001002.1.
DR RefSeq; XP_007999194.1; XM_008001003.1.
DR RefSeq; XP_007999196.1; XM_008001005.1.
DR AlphaFoldDB; A0A0D9RL45; -.
DR STRING; 60711.ENSCSAP00000009334; -.
DR Ensembl; ENSCSAT00000011255.1; ENSCSAP00000009334.1; ENSCSAG00000013161.1.
DR GeneID; 103237067; -.
DR CTD; 759; -.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000161270; -.
DR OMA; NGPEQWG; -.
DR OrthoDB; 49814at2759; -.
DR BioGRID-ORCS; 103237067; 0 hits in 9 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 8.
DR Bgee; ENSCSAG00000013161; Expressed in blood and 2 other cell types or tissues.
DR GO; GO:0004064; F:arylesterase activity; IEA:Ensembl.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0018820; F:cyanamide hydratase activity; IEA:Ensembl.
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:SF271; CARBONIC ANHYDRASE 1; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lyase {ECO:0000256|RuleBase:RU367011};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367011};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT DOMAIN 4..261
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
FT REGION 238..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 261 AA; 28947 MW; 0637634E2B0E582B CRC64;
MASPDWGYDD KNGPEQWSKL YPIANGNNQS PVDIKTSETK HDTSLKPISV SYNPATAKEI
INVGHSFHVN FEDNDNRSVL KGGPLSDSYR LFQFHFHWGS TNEYGSEHTV DGVKYSSELH
VAHWNSAKYS SLAEAVSKAD GLAVIGVLMK VGEANPKLQK VLDALHAIKT KGKRAPFTNF
DPSTLFPSSL DFWTYSGSLT HPPLYESVTW IICKESISVS SEQLAQFRSL LSNVEGDNPV
PIQHNNRPTQ PLKGRTVRAS F
//
