ID   CAH5B_MOUSE             Reviewed;         317 AA.
AC   Q9QZA0; Q8C3J9; Q8K014;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   09-MAY-2003, sequence version 2.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=Carbonic anhydrase 5B, mitochondrial;
DE            EC=4.2.1.1 {ECO:0000269|PubMed:10677517};
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Kidney;
RX   PubMed=10677517; DOI=10.1073/pnas.97.4.1677;
RA   Shah G.N., Hewett-Emmett D., Grubb J.H., Migas M.C., Fleming R.E.,
RA   Waheed A., Sly W.S.;
RT   "Mitochondrial carbonic anhydrase CA VB: differences in tissue distribution
RT   and pattern of evolution from those of CA VA suggest distinct physiological
RT   roles.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:1677-1682(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
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).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Mitochondrial carbonic anhydrase that catalyzes the
CC       reversible conversion of carbon dioxide to bicarbonate/HCO3.
CC       {ECO:0000269|PubMed:10677517}.
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:0000269|PubMed:10677517};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10749;
CC         Evidence={ECO:0000305|PubMed:10677517};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10750;
CC         Evidence={ECO:0000305|PubMed:10677517};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P23589};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10677517}.
CC   -!- TISSUE SPECIFICITY: Expressed in the heart, liver, lung, kidney,
CC       testis, and skeletal muscle (at protein level).
CC       {ECO:0000269|PubMed:10677517}.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000305}.
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DR   EMBL; AF192978; AAF08291.1; -; mRNA.
DR   EMBL; AK085670; BAC39501.1; -; mRNA.
DR   EMBL; BC034413; AAH34413.1; -; mRNA.
DR   CCDS; CCDS30515.1; -.
DR   RefSeq; NP_851832.2; NM_181315.4.
DR   AlphaFoldDB; Q9QZA0; -.
DR   SMR; Q9QZA0; -.
DR   BioGRID; 207805; 2.
DR   STRING; 10090.ENSMUSP00000033739; -.
DR   PhosphoSitePlus; Q9QZA0; -.
DR   SwissPalm; Q9QZA0; -.
DR   EPD; Q9QZA0; -.
DR   jPOST; Q9QZA0; -.
DR   MaxQB; Q9QZA0; -.
DR   PaxDb; 10090-ENSMUSP00000033739; -.
DR   PeptideAtlas; Q9QZA0; -.
DR   ProteomicsDB; 273899; -.
DR   Antibodypedia; 541; 284 antibodies from 33 providers.
DR   DNASU; 56078; -.
DR   Ensembl; ENSMUST00000033739.5; ENSMUSP00000033739.5; ENSMUSG00000031373.5.
DR   GeneID; 56078; -.
DR   KEGG; mmu:56078; -.
DR   UCSC; uc009uvb.2; mouse.
DR   AGR; MGI:1926249; -.
DR   CTD; 56078; -.
DR   MGI; MGI:1926249; Car5b.
DR   VEuPathDB; HostDB:ENSMUSG00000031373; -.
DR   eggNOG; KOG0382; Eukaryota.
DR   GeneTree; ENSGT00940000156978; -.
DR   HOGENOM; CLU_039326_2_1_1; -.
DR   InParanoid; Q9QZA0; -.
DR   OMA; GESNDWG; -.
DR   OrthoDB; 49814at2759; -.
DR   PhylomeDB; Q9QZA0; -.
DR   TreeFam; TF316425; -.
DR   Reactome; R-MMU-1475029; Reversible hydration of carbon dioxide.
DR   BioGRID-ORCS; 56078; 2 hits in 78 CRISPR screens.
DR   ChiTaRS; Car5b; mouse.
DR   PRO; PR:Q9QZA0; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q9QZA0; Protein.
DR   Bgee; ENSMUSG00000031373; Expressed in white adipose tissue and 90 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IDA:MGI.
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; IEP:MGI.
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.
DR   Genevisible; Q9QZA0; MM.
PE   1: Evidence at protein 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_0000004238"
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"
FT   CONFLICT        269
FT                   /note="S -> F (in Ref. 2; BAC39501)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        308
FT                   /note="P -> A (in Ref. 1; AAF08291)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   317 AA;  36623 MW;  719016A75305BFD3 CRC64;
     MAVMNHLRVI LQVSSSTLPW RRCWVPRLVP RRSCSLYTCT YRTRNRALPP LWENLDLVPA
     GDRQSPINIR WRDSVYDPGL KPLTISYDPA TCLHIWNNGY SFLVEFEDST DKSVVEGGPL
     EHNYRLKQFH FHWGAIDAWG SEHTVDSKCY PAELHLVHWN AVKFESFEDA ALEENGLAVI
     GVFLKLGKHH KELQKLVDTL PSIKHKDTLV EFGSFDPSCL MPTCPDYWTY SGSLTTPPLS
     ESVTWIIKKQ PVEVDRDQLE QFRTLLFTSE GEKEKRMVDN FRPLQPLMNR TVRSSFRHDY
     VLNIQVKPKP TASEVTP
//