ID H9KWT2_CALJA Unreviewed; 352 AA.
AC H9KWT2;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 2.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU367011};
DE EC=4.2.1.1 {ECO:0000256|RuleBase:RU367011};
GN Name=CA12 {ECO:0000313|Ensembl:ENSCJAP00000020785.3};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000020785.3, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000020785.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000020785.3}
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|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 AlphaFoldDB; H9KWT2; -.
DR Ensembl; ENSCJAT00000021971.4; ENSCJAP00000020785.3; ENSCJAG00000011284.4.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000159282; -.
DR TreeFam; TF316425; -.
DR Proteomes; UP000008225; Chromosome 10.
DR Bgee; ENSCJAG00000011284; Expressed in kidney and 4 other cell types or tissues.
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 CDD; cd03126; alpha_CA_XII_XIV; 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: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:UP000008225};
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..352
FT /note="Carbonic anhydrase"
FT /evidence="ECO:0000256|RuleBase:RU367011"
FT /id="PRO_5025085168"
FT TRANSMEM 298..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..287
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
SQ SEQUENCE 352 AA; 38926 MW; 1B13D804D6EB6C9D CRC64;
MPQHSLHAAA VLLLVILKEQ PSSPAPVNGK VSACPDGENS WSKKYPSCGG LLQSPIDLHS
DILQYDASLT PLTFQGYNLS ANEQFLLTNN GHSVKLTLPS DMHIQGLQSR YSAIQLHLHW
GNPKDPHGSE HTISGEHFAA ELHIVHYNSD LYPDASSASN KSEGLAVLAV LIEMGSFNPS
YDKIFSHLQR VKYKGQEAFI PGFNIEELLP ERTAEYYRYQ GSLTTPPCNP TVLWTVFRNP
VQISQEQLLA LETALYCTDM DDPSPREMVN NFRQVQKFDE RLVYTSFPKV EVCPAAGLSL
GVILSLALAG VLGICIVLVV SVWLFRRKSN KKGGNRGVIY KPATKEETEA HA
//