CAH2_SHEEP
ID CAH2_SHEEP Reviewed; 260 AA.
AC P00922;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 120.
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 Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP PROTEIN SEQUENCE OF 2-260, AND ACETYLATION AT SER-2.
RX PubMed=4215456; DOI=10.1016/0005-2795(74)90050-6;
RA Tanis R.J., Ferrell R.E., Tashian R.E.;
RT "Amino acid sequence of sheep carbonic anhydrase C.";
RL Biochim. Biophys. Acta 371:534-548(1974).
RN [2]
RP VARIANT THR-36.
RX PubMed=106895; DOI=10.1016/0005-2795(79)90404-5;
RA Mallet B., Gulian J.M., Sciaky M., Laurent G., Charrel M.;
RT "Multiple molecular forms of erythrocyte carbonic anhydrase of sheep.";
RL Biochim. Biophys. Acta 576:290-304(1979).
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 -!- MISCELLANEOUS: One minor and three major forms were isolated
CC chromatographically.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
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DR PIR; A01145; CRSH2.
DR AlphaFoldDB; P00922; -.
DR SMR; P00922; -.
DR STRING; 9940.ENSOARP00000013878; -.
DR iPTMnet; P00922; -.
DR eggNOG; KOG0382; Eukaryota.
DR Proteomes; UP000002356; 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 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:4215456"
FT CHAIN 2..260
FT /note="Carbonic anhydrase 2"
FT /id="PRO_0000077422"
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:0000269|PubMed:106895,
FT ECO:0000269|PubMed:4215456"
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 36
FT /note="K -> T (in one of the major forms)"
FT /evidence="ECO:0000269|PubMed:106895"
SQ SEQUENCE 260 AA; 29211 MW; 5881DD762616363D CRC64;
MSHHWGYGEH NGPEHWHKDF PIADGERQSP VDIDTKAVVP DPALKPLALL YEQAASRRMV
NNGHSFNVEF DDSQDKAVLK DGPLTGTYRL VQFHFHWGSS DDQGSEHTVD RKKYAAELHL
VHWNTKYGDF GTAAQQPDGL AVVGVFLKVG DANPALQKVL DVLDSIKTKG KSADFPNFDP
SSLLKRALNY WTYPGSLTNP PLLESVTWVV LKEPTSVSSQ QMLKFRSLNF NAEGEPELLM
LANWRPAQPL KNRQVRVFPK
