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   03-AUG-2022, entry version 118.
DE   RecName: Full=Carbonic anhydrase 5B, mitochondrial;
DE            EC=4.2.1.1;
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: Reversible hydration of carbon dioxide.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
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; 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; Q66HG6; -.
DR   PRIDE; Q66HG6; -.
DR   Ensembl; ENSRNOT00000047354; ENSRNOP00000043235; ENSRNOG00000029330.
DR   GeneID; 302669; -.
DR   KEGG; rno:302669; -.
DR   UCSC; RGD:1549783; rat.
DR   CTD; 11238; -.
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; 1377476at2759; -.
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 tissues.
DR   Genevisible; Q66HG6; RN.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR   GO; GO:0004089; F:carbonate dehydratase activity; ISO:RGD.
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   GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR   Gene3D; 3.10.200.10; -; 1.
DR   InterPro; IPR018437; CA-VB_mt.
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   PANTHER; PTHR18952:SF25; PTHR18952:SF25; 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   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