CAH2_BOVIN
ID CAH2_BOVIN Reviewed; 260 AA.
AC P00921; Q3ZBJ5; Q865Y7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 170.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Bone marrow;
RA Daigle R., Castro I., Desrochers M., Charest P.-M.;
RT "Full length cDNA of bovine carbonic anhydrase II.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-260.
RC TISSUE=Erythrocyte;
RX PubMed=826282; DOI=10.1016/s0300-9084(76)80085-5;
RA Sciaky M., Limozin N., Filippi-Foveau D., Gulian J.M., Laurent-Tabusse G.;
RT "Primary structure of bovine erythrocyte carbonic carbonic anhydrase CI.
RT II. Complete sequence.";
RL Biochimie 58:1071-1082(1976).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=19093; DOI=10.1016/s0300-9084(77)80146-6;
RA Gulian J.M., Limozin N., Mallet B., di Costanzo J., Charrel M.;
RT "Genetic independence of two forms of carbonic anhydrase from bovine
RT erythrocytes.";
RL Biochimie 59:293-302(1977).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 2-260 IN COMPLEX WITH ZINC ION.
RX PubMed=15039588; DOI=10.1107/s0907444904003166;
RA Saito R., Sato T., Ikai A., Tanaka N.;
RT "Structure of bovine carbonic anhydrase II at 1.95 A resolution.";
RL Acta Crystallogr. D 60:792-795(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 1-254 IN COMPLEX WITH ANTIBODY.
RX PubMed=11342547; DOI=10.1074/jbc.m102107200;
RA Desmyter A., Decanniere K., Muyldermans S., Wyns L.;
RT "Antigen specificity and high affinity binding provided by one single loop
RT of a camel single-domain antibody.";
RL J. Biol. Chem. 276:26285-26290(2001).
CC -!- FUNCTION: Catalyzes the reversible hydration of carbon dioxide (By
CC similarity). Involved in the regulation of fluid secretion into the
CC anterior chamber of the eye (By similarity). Essential for bone
CC resorption and osteoclast differentiation (By similarity). Contributes
CC to intracellular pH regulation in the duodenal upper villous epithelium
CC during proton-coupled peptide absorption (By similarity). Stimulates
CC the chloride-bicarbonate exchange activity of SLC26A6 (By similarity).
CC {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:0000269|PubMed:15039588};
CC -!- ACTIVITY REGULATION: Inhibited by acetazolamide.
CC {ECO:0000250|UniProtKB:P00918}.
CC -!- SUBUNIT: Interacts with SLC4A4. Interaction with SLC4A7 regulates
CC 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.
CC {ECO:0000250|UniProtKB:P00918}.
CC -!- MISCELLANEOUS: One minor and two major forms were isolated
CC chromatographically.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/CA/";
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DR EMBL; AY240020; AAO85140.1; -; mRNA.
DR EMBL; BC103260; AAI03261.1; -; mRNA.
DR PIR; A01144; CRBO2.
DR RefSeq; NP_848667.1; NM_178572.2.
DR PDB; 1G6V; X-ray; 3.50 A; A=1-254.
DR PDB; 1V9E; X-ray; 1.95 A; A/B=2-260.
DR PDB; 1V9I; X-ray; 2.95 A; C=2-260.
DR PDB; 4CNR; X-ray; 2.29 A; A/B/C/D=1-260.
DR PDB; 4CNV; X-ray; 1.62 A; A=1-260.
DR PDB; 4CNW; X-ray; 2.03 A; A/B=1-260.
DR PDB; 4CNX; X-ray; 1.23 A; A=1-260.
DR PDB; 5A25; X-ray; 1.90 A; A/B=1-260.
DR PDB; 5EZT; X-ray; 1.54 A; X=4-260.
DR PDB; 6SKS; X-ray; 1.75 A; A=1-260.
DR PDB; 6SKT; X-ray; 1.90 A; A=1-260.
DR PDB; 6SKV; X-ray; 1.75 A; A=1-260.
DR PDBsum; 1G6V; -.
DR PDBsum; 1V9E; -.
DR PDBsum; 1V9I; -.
DR PDBsum; 4CNR; -.
DR PDBsum; 4CNV; -.
DR PDBsum; 4CNW; -.
DR PDBsum; 4CNX; -.
DR PDBsum; 5A25; -.
DR PDBsum; 5EZT; -.
DR PDBsum; 6SKS; -.
DR PDBsum; 6SKT; -.
DR PDBsum; 6SKV; -.
DR AlphaFoldDB; P00921; -.
DR PCDDB; P00921; -.
DR SASBDB; P00921; -.
DR SMR; P00921; -.
DR IntAct; P00921; 1.
DR MINT; P00921; -.
DR STRING; 9913.ENSBTAP00000023581; -.
DR BindingDB; P00921; -.
DR ChEMBL; CHEMBL2283; -.
DR DrugCentral; P00921; -.
DR PaxDb; P00921; -.
DR PeptideAtlas; P00921; -.
DR PRIDE; P00921; -.
DR ABCD; P00921; 1 sequenced antibody.
DR GeneID; 280740; -.
DR KEGG; bta:280740; -.
DR CTD; 760; -.
DR eggNOG; KOG0382; Eukaryota.
DR InParanoid; P00921; -.
DR OrthoDB; 1377476at2759; -.
DR BRENDA; 4.2.1.1; 908.
DR EvolutionaryTrace; P00921; -.
DR PRO; PR:P00921; -.
DR Proteomes; UP000009136; Unplaced.
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 3D-structure; Acetylation; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Lyase; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:19093,
FT ECO:0000269|PubMed:826282"
FT CHAIN 2..260
FT /note="Carbonic anhydrase 2"
FT /id="PRO_0000077417"
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:0000269|PubMed:15039588"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:15039588"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:15039588"
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 57
FT /note="R -> Q (in one of the major forms)"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:4CNX"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:4CNX"
FT TURN 16..19
FT /evidence="ECO:0007829|PDB:4CNX"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:4CNX"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:5EZT"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:1G6V"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:4CNV"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:4CNX"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:4CNX"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:4CNX"
FT STRAND 73..81
FT /evidence="ECO:0007829|PDB:4CNX"
FT STRAND 88..97
FT /evidence="ECO:0007829|PDB:4CNX"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:1G6V"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:4CNX"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:4CNX"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:4CNX"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:4CNX"
FT STRAND 139..151
FT /evidence="ECO:0007829|PDB:4CNX"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:4CNX"
FT HELIX 161..166
FT /evidence="ECO:0007829|PDB:4CNX"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:1G6V"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:4CNX"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:4CNX"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:4CNX"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:4CNX"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:4CNX"
FT HELIX 219..225
FT /evidence="ECO:0007829|PDB:4CNX"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:4CNX"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:4CNX"
SQ SEQUENCE 260 AA; 29114 MW; A89412C23FFD19A7 CRC64;
MSHHWGYGKH NGPEHWHKDF PIANGERQSP VDIDTKAVVQ DPALKPLALV YGEATSRRMV
NNGHSFNVEY DDSQDKAVLK DGPLTGTYRL VQFHFHWGSS DDQGSEHTVD RKKYAAELHL
VHWNTKYGDF GTAAQQPDGL AVVGVFLKVG DANPALQKVL DALDSIKTKG KSTDFPNFDP
GSLLPNVLDY WTYPGSLTTP PLLESVTWIV LKEPISVSSQ QMLKFRTLNF NAEGEPELLM
LANWRPAQPL KNRQVRGFPK
