CAH12_RABIT
ID CAH12_RABIT Reviewed; 355 AA.
AC Q9MZ30;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Carbonic anhydrase 12 {ECO:0000250|UniProtKB:O43570};
DE EC=4.2.1.1 {ECO:0000250|UniProtKB:O43570};
DE AltName: Full=Carbonate dehydratase XII;
DE AltName: Full=Carbonic anhydrase XII;
DE Short=CA-XII;
DE Flags: Precursor;
GN Name=CA12 {ECO:0000250|UniProtKB:O43570};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney cortex;
RX PubMed=12388401; DOI=10.1152/ajprenal.00370.2001;
RA Schwartz G.J., Kittelberger A.M., Watkins R.H., O'Reilly M.A.;
RT "Carbonic anhydrase XII mRNA encodes a hydratase that is differentially
RT expressed along the rabbit nephron.";
RL Am. J. Physiol. 284:F399-F410(2003).
CC -!- FUNCTION: Reversible hydration of carbon dioxide.
CC {ECO:0000250|UniProtKB:O43570}.
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:0000250|UniProtKB:O43570};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:O43570};
CC -!- ACTIVITY REGULATION: Inhibited by acetazolamide.
CC {ECO:0000250|UniProtKB:O43570}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O43570}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:O43570}; Single-
CC pass type I membrane protein {ECO:0000250|UniProtKB:O43570}. Cell
CC membrane {ECO:0000250|UniProtKB:O43570}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; AF263367; AAF91392.2; -; mRNA.
DR RefSeq; NP_001075555.1; NM_001082086.1.
DR AlphaFoldDB; Q9MZ30; -.
DR SMR; Q9MZ30; -.
DR STRING; 9986.ENSOCUP00000004000; -.
DR GeneID; 100008777; -.
DR KEGG; ocu:100008777; -.
DR CTD; 771; -.
DR eggNOG; KOG0382; Eukaryota.
DR InParanoid; Q9MZ30; -.
DR OrthoDB; 1377476at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.10.200.10; -; 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 InterPro; IPR018430; Carbonic_anhydrase_CA12.
DR PANTHER; PTHR18952; PTHR18952; 1.
DR PANTHER; PTHR18952:SF19; PTHR18952:SF19; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; SSF51069; 1.
DR PROSITE; PS00162; ALPHA_CA_1; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Lyase; Membrane;
KW Metal-binding; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Zinc.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..355
FT /note="Carbonic anhydrase 12"
FT /id="PRO_0000004250"
FT TOPO_DOM 25..303
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..289
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT ACT_SITE 94
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O43570"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O43570"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O43570"
FT BINDING 226..227
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..230
FT /evidence="ECO:0000250|UniProtKB:O43570"
SQ SEQUENCE 355 AA; 39591 MW; 5B468580EBA437D5 CRC64;
MPVGSLRAAA VLLLGIAQLP PSSAAPRNGS KWTYVGADGE RSWFKKYPSC GGRLQSPIDL
HGDTLQYDAS LTPLEFQGYN VSADKQFNLT NDGHSVRLNL PPDMYLQGLP SRYTATQLHL
HWGNRNDPYG SEHTVGGKQF AAELHIVHYN SDSYPDISTA SNKSEGLAVL AVLIEKGYFN
PYYDRIFSFL RYVKYKGQNV RIPTFNIEEL LPEKPAEYYR YRGSLTTPPC YPSVLWTVFR
NPVTISQEQL LALQTALYFT RADDPAPREM INNFRPIQNF GVRLVHASFQ EVQILPGTGL
SVGIILSVAL AGVLGICIVL AVCIWFFRRK KGSKKGDNKG VIYNPAIKME TEAHA
