CAH5B_MOUSE
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 03-AUG-2022, entry version 156.
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 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].
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: 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.
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; 1.
DR STRING; 10090.ENSMUSP00000033739; -.
DR PhosphoSitePlus; Q9QZA0; -.
DR EPD; Q9QZA0; -.
DR jPOST; Q9QZA0; -.
DR MaxQB; Q9QZA0; -.
DR PaxDb; Q9QZA0; -.
DR PeptideAtlas; Q9QZA0; -.
DR PRIDE; Q9QZA0; -.
DR ProteomicsDB; 273899; -.
DR Antibodypedia; 541; 260 antibodies from 33 providers.
DR DNASU; 56078; -.
DR Ensembl; ENSMUST00000033739; ENSMUSP00000033739; ENSMUSG00000031373.
DR GeneID; 56078; -.
DR KEGG; mmu:56078; -.
DR UCSC; uc009uvb.2; mouse.
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; 1377476at2759; -.
DR PhylomeDB; Q9QZA0; -.
DR TreeFam; TF316425; -.
DR Reactome; R-MMU-1475029; Reversible hydration of carbon dioxide.
DR BioGRID-ORCS; 56078; 2 hits in 73 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 89 other tissues.
DR Genevisible; Q9QZA0; MM.
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: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; IEP:MGI.
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 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
