ID CAH5B_RAT Reviewed; 317 AA.
AC Q66HG6;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 127.
DE RecName: Full=Carbonic anhydrase 5B, mitochondrial;
DE EC=4.2.1.1 {ECO:0000250|UniProtKB:Q9QZA0};
DE AltName: Full=Carbonate dehydratase VB;
DE AltName: Full=Carbonic anhydrase VB;
DE Short=CA-VB;
DE Flags: Precursor;
GN Name=Ca5b; Synonyms=Car5b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Mitochondrial carbonic anhydrase that catalyzes the
CC reversible conversion of carbon dioxide to bicarbonate/HCO3.
CC {ECO:0000250|UniProtKB:Q9QZA0}.
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:Q9QZA0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10749;
CC Evidence={ECO:0000250|UniProtKB:Q9QZA0};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10750;
CC Evidence={ECO:0000250|UniProtKB:Q9QZA0};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P23589};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9QZA0}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; BC081872; AAH81872.1; -; mRNA.
DR RefSeq; NP_001005551.1; NM_001005551.2.
DR RefSeq; XP_006256921.1; XM_006256859.3.
DR AlphaFoldDB; Q66HG6; -.
DR SMR; Q66HG6; -.
DR STRING; 10116.ENSRNOP00000043235; -.
DR iPTMnet; Q66HG6; -.
DR PhosphoSitePlus; Q66HG6; -.
DR PaxDb; 10116-ENSRNOP00000043235; -.
DR Ensembl; ENSRNOT00000047354.5; ENSRNOP00000043235.3; ENSRNOG00000029330.5.
DR GeneID; 302669; -.
DR KEGG; rno:302669; -.
DR UCSC; RGD:1549783; rat.
DR AGR; RGD:1549783; -.
DR CTD; 56078; -.
DR RGD; 1549783; Ca5b.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000156978; -.
DR HOGENOM; CLU_039326_2_1_1; -.
DR InParanoid; Q66HG6; -.
DR OMA; GESNDWG; -.
DR OrthoDB; 49814at2759; -.
DR PhylomeDB; Q66HG6; -.
DR TreeFam; TF316425; -.
DR Reactome; R-RNO-1475029; Reversible hydration of carbon dioxide.
DR PRO; PR:Q66HG6; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000029330; Expressed in adult mammalian kidney and 18 other cell types or tissues.
DR Genevisible; Q66HG6; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0004089; F:carbonate dehydratase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 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; CARBONIC ANHYDRASE; 1.
DR PANTHER; PTHR18952:SF25; CARBONIC ANHYDRASE 5B, MITOCHONDRIAL; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR PROSITE; PS00162; ALPHA_CA_1; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 2: Evidence at transcript level;
KW Lyase; Metal-binding; Mitochondrion; Reference proteome; Transit peptide;
KW Zinc.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 34..317
FT /note="Carbonic anhydrase 5B, mitochondrial"
FT /id="PRO_0000041944"
FT DOMAIN 37..296
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 235..236
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00918"
SQ SEQUENCE 317 AA; 36598 MW; E8DF65463368618B CRC64;
MTVMSHLRVS LQVSSCTLLW RRFRVPRLVP LRSCSLYTCT YRTRNRALPP LWENLDLVPA
GDRQSPINIR WRDSVYDPGL KPLTISYDPA TCLHIWNNGY SFLVEFEDTT DKSVIEGGPL
EHNYRLKQFH FHWGAIDAWG SEHTVDSKCY PAELHLVHWN AVKFESFEDA ALEENGLAVI
GVFLKLGKHH KELQKLVDTL PSIKHKDTLV KFGSFDPSCL MPTCPDYWTY SGSLTTPPLS
ESVTWIIKKQ PVEVDHDQLE QFRTLLFTSE GEKEKRMVDN FRPLQPLMNR TVRSSFRHDY
VLNIQVKPEP TASEVSP
//
