CAH2_RABIT
ID CAH2_RABIT Reviewed; 260 AA.
AC P00919;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Carbonic anhydrase 2;
DE EC=4.2.1.1 {ECO:0000250|UniProtKB:P00918};
DE AltName: Full=Carbonate dehydratase II;
DE AltName: Full=Carbonic anhydrase II;
DE Short=CA-II;
GN Name=CA2;
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 PROTEIN SEQUENCE OF 2-260.
RX PubMed=416851; DOI=10.1016/0005-2795(78)90541-x;
RA Ferrell R.E., Stroup S.K., Tanis R.J., Tashian R.E.;
RT "Amino acid sequence of rabbit carbonic anhydrase II.";
RL Biochim. Biophys. Acta 533:1-11(1978).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-239.
RC STRAIN=New Zealand white; TISSUE=Kidney;
RX PubMed=8285209; DOI=10.1152/ajprenal.1993.265.6.f764;
RA Schwartz G.J., Winkler C.A., Zavilowitz B.J., Bargiello T.;
RT "Carbonic anhydrase II mRNA is induced in rabbit kidney cortex during
RT chronic metabolic acidosis.";
RL Am. J. Physiol. 265:F764-F772(1993).
CC -!- FUNCTION: Catalyzes the reversible hydration of carbon dioxide.
CC Involved in the regulation of fluid secretion into the anterior chamber
CC of the eye. Essential for bone resorption and osteoclast
CC differentiation. Contributes to intracellular pH regulation in the
CC duodenal upper villous epithelium during proton-coupled peptide
CC absorption. Stimulates the chloride-bicarbonate exchange activity of
CC SLC26A6. {ECO:0000250|UniProtKB:P00918}.
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:P00918};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00921};
CC -!- ACTIVITY REGULATION: Inhibited by acetazolamide.
CC {ECO:0000250|UniProtKB:P00918}.
CC -!- SUBUNIT: Interacts with SLC4A4 and SLC26A6. Interaction with SLC4A7
CC regulates SLC4A7 transporter activity (By similarity).
CC {ECO:0000250|UniProtKB:P00918}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00918}. Cell
CC membrane {ECO:0000250|UniProtKB:P00918}. Note=Colocalized with SLC26A6
CC at the surface of the cell membrane in order to form a bicarbonate
CC transport metabolon. Displaced from the cytosolic surface of the cell
CC membrane by PKC in phorbol myristate acetate (PMA)-induced cells (By
CC similarity). {ECO:0000250|UniProtKB:P00918}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; M98395; AAA80531.1; -; mRNA.
DR PIR; A01142; CRRB2.
DR RefSeq; NP_001182637.1; NM_001195708.1.
DR AlphaFoldDB; P00919; -.
DR SMR; P00919; -.
DR STRING; 9986.ENSOCUP00000010096; -.
DR Ensembl; ENSOCUT00000011742; ENSOCUP00000010096; ENSOCUG00000011742.
DR GeneID; 100009156; -.
DR KEGG; ocu:100009156; -.
DR CTD; 760; -.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000160385; -.
DR HOGENOM; CLU_039326_2_1_1; -.
DR InParanoid; P00919; -.
DR OMA; SADFPNF; -.
DR OrthoDB; 1377476at2759; -.
DR TreeFam; TF316425; -.
DR Proteomes; UP000001811; Chromosome 3.
DR Bgee; ENSOCUG00000011742; Expressed in blood and 15 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0038166; P:angiotensin-activated signaling pathway; ISS:UniProtKB.
DR GO; GO:2001150; P:positive regulation of dipeptide transmembrane transport; ISS:UniProtKB.
DR GO; GO:0044070; P:regulation of anion transport; ISS:UniProtKB.
DR GO; GO:0051453; P:regulation of intracellular pH; ISS:UniProtKB.
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 PANTHER; PTHR18952; PTHR18952; 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 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cytoplasm; Direct protein sequencing; Lyase;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:416851"
FT CHAIN 2..260
FT /note="Carbonic anhydrase 2"
FT /id="PRO_0000077420"
FT DOMAIN 3..259
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT ACT_SITE 64
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
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:P00918"
FT BINDING 198..199
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT SITE 7
FT /note="Fine-tunes the proton-transfer properties of H-64"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT SITE 62
FT /note="Fine-tunes the proton-transfer properties of H-64"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT SITE 67
FT /note="Fine-tunes the proton-transfer properties of H-64"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27139"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT VARIANT 204
FT /note="E -> Q"
FT CONFLICT 24
FT /note="N -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="N -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="C -> S (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="T -> S (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="Q -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="D -> N (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 260 AA; 29500 MW; 1601916B7D8A2828 CRC64;
MSHHWGYGKH NGPEHWHKDF PIANGERQSP IDIDTNAAKH DPSLKPLRVC YEHPISRRII
NNGHSFNVEF DDSHDKTVLK EGPLEGTYRL IQFHFHWGSS DGQGSEHTVN KKKYAAELHL
VHWNTKYGDF GKAVKHPDGL AVLGIFLKIG SATPGLQKVV DTLSSIKTKG KSVDFTDFDP
RGLLPESLDY WTYPGSLTTP PLLECVTWIV LKEPITVSSE QMLKFRNLNF NKEAEPEEPM
VDNWRPTQPL KGRQVKASFV
