CAH4_BOVIN
ID CAH4_BOVIN Reviewed; 312 AA.
AC Q95323; A5PKL8;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Carbonic anhydrase 4;
DE EC=4.2.1.1 {ECO:0000250|UniProtKB:P22748};
DE AltName: Full=Carbonate dehydratase IV;
DE AltName: Full=Carbonic anhydrase IV;
DE Short=CA-IV;
DE Flags: Precursor;
GN Name=CA4;
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 STRAIN=Holstein; TISSUE=Kidney;
RA Tamai S.;
RT "Bos taurus carbonic anhydrase IV (bovine carbonic anhydrase IV) mRNA,
RT complete cds.";
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible hydration of carbon dioxide into
CC bicarbonate and protons and thus is essential to maintaining
CC intracellular and extracellular pH. May stimulate the
CC sodium/bicarbonate transporter activity of SLC4A4 that acts in pH
CC homeostasis. It is essential for acid overload removal from the retina
CC and retina epithelium, and acid release in the choriocapillaris in the
CC choroid. {ECO:0000250|UniProtKB:P22748}.
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:P22748};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10749;
CC Evidence={ECO:0000250|UniProtKB:P22748};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10750;
CC Evidence={ECO:0000250|UniProtKB:P22748};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P22748};
CC -!- ACTIVITY REGULATION: Inhibited by acetazolamide. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SLC4A4. {ECO:0000250|UniProtKB:P22748}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P22748};
CC Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P22748}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; U58870; AAB09466.1; -; mRNA.
DR EMBL; BC142534; AAI42535.1; -; mRNA.
DR RefSeq; NP_776322.1; NM_173897.1.
DR AlphaFoldDB; Q95323; -.
DR SMR; Q95323; -.
DR STRING; 9913.ENSBTAP00000023909; -.
DR BindingDB; Q95323; -.
DR ChEMBL; CHEMBL281; -.
DR DrugCentral; Q95323; -.
DR PaxDb; Q95323; -.
DR PRIDE; Q95323; -.
DR Ensembl; ENSBTAT00000023909; ENSBTAP00000023909; ENSBTAG00000017969.
DR GeneID; 280741; -.
DR KEGG; bta:280741; -.
DR CTD; 762; -.
DR VEuPathDB; HostDB:ENSBTAG00000017969; -.
DR VGNC; VGNC:26654; CA4.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000155690; -.
DR HOGENOM; CLU_039326_2_2_1; -.
DR InParanoid; Q95323; -.
DR OMA; SHWCYEI; -.
DR OrthoDB; 1377476at2759; -.
DR TreeFam; TF316425; -.
DR PRO; PR:Q95323; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000017969; Expressed in cortex of kidney and 93 other tissues.
DR ExpressionAtlas; Q95323; baseline.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004089; F:carbonate dehydratase activity; IBA:GO_Central.
DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR CDD; cd03117; alpha_CA_IV_XV_like; 1.
DR Gene3D; 3.10.200.10; -; 1.
DR InterPro; IPR041874; CA4/CA15.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR InterPro; IPR018343; Carbonic_anhydrase_CA4.
DR PANTHER; PTHR18952; PTHR18952; 1.
DR PANTHER; PTHR18952:SF95; PTHR18952:SF95; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; SSF51069; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Lyase; Membrane; Metal-binding; Reference proteome; Signal; Zinc.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..284
FT /note="Carbonic anhydrase 4"
FT /id="PRO_0000004224"
FT PROPEP 285..312
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P22748"
FT /id="PRO_0000004225"
FT DOMAIN 21..285
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT ACT_SITE 88
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q64444"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q64444"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q64444"
FT BINDING 225..226
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT LIPID 284
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000250|UniProtKB:P22748"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 24..36
FT /evidence="ECO:0000250|UniProtKB:Q64444"
FT DISULFID 46..229
FT /evidence="ECO:0000250|UniProtKB:Q64444"
SQ SEQUENCE 312 AA; 35151 MW; BAEA320C09426351 CRC64;
MRLLLALLVL AAAPPQARAA SHWCYQIQVK PSNYTCLEPD EWEGSCQNNR QSPVNIVTAK
TQLDPNLGRF SFSGYNMKHQ WVVQNNGHTV MVLLENKPSI AGGGLSTRYQ ATQLHLHWSR
AMDRGSEHSF DGERFAMEMH IVHEKEKGLS GNASQNQFAE DEIAVLAFMV EDGSKNVNFQ
PLVEALSDIP RPNMNTTMKE GVSLFDLLPE EESLRHYFRY LGSLTTPTCD EKVVWTVFQK
PIQLHRDQIL AFSQKLFYDD QQKVNMTDNV RPVQSLGQRQ VFRSGAPGLL LAQPLPTLLA
PVLACLTVGF LR
