CAH4_RABIT
ID CAH4_RABIT Reviewed; 308 AA.
AC P48283;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
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 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 STRAIN=New Zealand white; TISSUE=Kidney cortex;
RX PubMed=9140058; DOI=10.1152/ajprenal.1997.272.4.f551;
RA Winkler C.A., Kittelberger A.M., Schwartz G.J.;
RT "Expression of carbonic anhydrase IV mRNA in rabbit kidney: stimulation by
RT metabolic acidosis.";
RL Am. J. Physiol. 272:F551-F560(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Kidney cortex;
RA Tamai S.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH SLC4A4.
RX PubMed=14567693; DOI=10.1021/bi0353124;
RA Alvarez B.V., Loiselle F.B., Supuran C.T., Schwartz G.J., Casey J.R.;
RT "Direct extracellular interaction between carbonic anhydrase IV and the
RT human NBC1 sodium/bicarbonate co-transporter.";
RL Biochemistry 42:12321-12329(2003).
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:0000269|PubMed:14567693}.
CC -!- INTERACTION:
CC P48283; Q9Y6R1-1: SLC4A4; Xeno; NbExp=2; IntAct=EBI-6859264, EBI-6859278;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L48928; AAC37337.1; -; mRNA.
DR EMBL; U58871; AAB09467.1; -; mRNA.
DR RefSeq; NP_001075841.1; NM_001082372.1.
DR AlphaFoldDB; P48283; -.
DR SMR; P48283; -.
DR IntAct; P48283; 1.
DR STRING; 9986.ENSOCUP00000008104; -.
DR GeneID; 100009226; -.
DR KEGG; ocu:100009226; -.
DR CTD; 762; -.
DR eggNOG; KOG0382; Eukaryota.
DR InParanoid; P48283; -.
DR OrthoDB; 1377476at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0031225; C:anchored 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 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 1: Evidence at protein 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:0000255"
FT CHAIN 19..280
FT /note="Carbonic anhydrase 4"
FT /id="PRO_0000004230"
FT PROPEP 281..308
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P22748"
FT /id="PRO_0000004231"
FT DOMAIN 21..281
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT ACT_SITE 86
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q64444"
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 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q64444"
FT BINDING 221..222
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT LIPID 280
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000250|UniProtKB:P22748"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 24..34
FT /evidence="ECO:0000250|UniProtKB:Q64444"
FT DISULFID 44..225
FT /evidence="ECO:0000250|UniProtKB:Q64444"
SQ SEQUENCE 308 AA; 34394 MW; CDB29AED9D8CDEBC CRC64;
MQLLFALLAL GALRPLAGEE LHWCYEIQAS NYSCLGPDKW QEDCQKSRQS PINIVTTKAE
VDHSLGRFHF SGYDQREARL VENNGHSVMV SLGDEISISG GGLPARYRAT QLHLHWSQEL
DRGSEHSLDG ERSAMEMHIV HQKETGTSGN EVQDSDDSIA VLAFLVEAGP TMNEGFQPLV
TALSAISIPG TNTTMAPSSL WDLLPAEEEL RHYFRYMGSL TTPACSETVV WTVFQEPIRL
HRDQILEFSS KLYYDQERKM NMKDNVRPLQ RLGDRSVFKS QAAGQLLPLP LPTLLVPTLA
CVMAGLLR
