CAH5B_HUMAN
ID CAH5B_HUMAN Reviewed; 317 AA.
AC Q9Y2D0; A8K4T5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 168.
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;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC TISSUE=Pancreas;
RX PubMed=10409679; DOI=10.1074/jbc.274.30.21228;
RA Fujikawa-Adachi K., Nishimori I., Taguchi T., Onishi S.;
RT "Human mitochondrial carbonic anhydrase VB: cDNA cloning, mRNA expression,
RT subcellular localization, and mapping to chromosome X.";
RL J. Biol. Chem. 274:21228-21233(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood;
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 [5]
RP ACTIVITY REGULATION.
RX PubMed=17705204; DOI=10.1002/anie.200701189;
RA Koehler K., Hillebrecht A., Schulze Wischeler J., Innocenti A., Heine A.,
RA Supuran C.T., Klebe G.;
RT "Saccharin inhibits carbonic anhydrases: possible explanation for its
RT unpleasant metallic aftertaste.";
RL Angew. Chem. Int. Ed. Engl. 46:7697-7699(2007).
RN [6]
RP ACTIVITY REGULATION.
RX PubMed=17314045; DOI=10.1016/j.bmcl.2007.01.113;
RA Temperini C., Innocenti A., Guerri A., Scozzafava A., Rusconi S.,
RA Supuran C.T.;
RT "Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-ray
RT crystal structure of the antiviral drug foscarnet complexed to human
RT carbonic anhydrase I.";
RL Bioorg. Med. Chem. Lett. 17:2210-2215(2007).
RN [7]
RP ACTIVITY REGULATION.
RX PubMed=19186056; DOI=10.1016/j.bmcl.2009.01.038;
RA Crocetti L., Maresca A., Temperini C., Hall R.A., Scozzafava A.,
RA Muehlschlegel F.A., Supuran C.T.;
RT "A thiabendazole sulfonamide shows potent inhibitory activity against
RT mammalian and nematode alpha-carbonic anhydrases.";
RL Bioorg. Med. Chem. Lett. 19:1371-1375(2009).
RN [8]
RP ACTIVITY REGULATION.
RX PubMed=19206230; DOI=10.1021/ja809683v;
RA Maresca A., Temperini C., Vu H., Pham N.B., Poulsen S.-A., Scozzafava A.,
RA Quinn R.J., Supuran C.T.;
RT "Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new
RT class of suicide inhibitors.";
RL J. Am. Chem. Soc. 131:3057-3062(2009).
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 -!- ACTIVITY REGULATION: Inhibited by coumarins, sulfonamide derivatives
CC such as acetazolamide (AZA), saccharin and Foscarnet (phosphonoformate
CC trisodium salt). {ECO:0000269|PubMed:17314045,
CC ECO:0000269|PubMed:17705204, ECO:0000269|PubMed:19186056,
CC ECO:0000269|PubMed:19206230}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- TISSUE SPECIFICITY: Strongest expression in heart, pancreas, kidney,
CC placenta, lung, and skeletal muscle. Not expressed in liver.
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; AB021660; BAA76671.1; -; mRNA.
DR EMBL; AK291050; BAF83739.1; -; mRNA.
DR EMBL; CH471074; EAW98897.1; -; Genomic_DNA.
DR EMBL; BC028142; AAH28142.1; -; mRNA.
DR CCDS; CCDS14171.1; -.
DR RefSeq; NP_009151.1; NM_007220.3.
DR RefSeq; XP_005274499.1; XM_005274442.4.
DR AlphaFoldDB; Q9Y2D0; -.
DR SMR; Q9Y2D0; -.
DR BioGRID; 116403; 5.
DR IntAct; Q9Y2D0; 1.
DR STRING; 9606.ENSP00000314099; -.
DR BindingDB; Q9Y2D0; -.
DR ChEMBL; CHEMBL3969; -.
DR DrugBank; DB00562; Benzthiazide.
DR DrugBank; DB00606; Cyclothiazide.
DR DrugBank; DB08846; Ellagic acid.
DR DrugBank; DB00909; Zonisamide.
DR DrugCentral; Q9Y2D0; -.
DR GlyGen; Q9Y2D0; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q9Y2D0; -.
DR PhosphoSitePlus; Q9Y2D0; -.
DR BioMuta; CA5B; -.
DR DMDM; 8928041; -.
DR EPD; Q9Y2D0; -.
DR jPOST; Q9Y2D0; -.
DR MassIVE; Q9Y2D0; -.
DR PaxDb; Q9Y2D0; -.
DR PeptideAtlas; Q9Y2D0; -.
DR PRIDE; Q9Y2D0; -.
DR ProteomicsDB; 85732; -.
DR Antibodypedia; 541; 260 antibodies from 33 providers.
DR DNASU; 11238; -.
DR Ensembl; ENST00000318636.8; ENSP00000314099.3; ENSG00000169239.13.
DR Ensembl; ENST00000454127.2; ENSP00000417021.2; ENSG00000169239.13.
DR GeneID; 11238; -.
DR KEGG; hsa:11238; -.
DR MANE-Select; ENST00000318636.8; ENSP00000314099.3; NM_007220.4; NP_009151.1.
DR UCSC; uc004cxe.4; human.
DR CTD; 11238; -.
DR GeneCards; CA5B; -.
DR HGNC; HGNC:1378; CA5B.
DR HPA; ENSG00000169239; Low tissue specificity.
DR MIM; 300230; gene.
DR neXtProt; NX_Q9Y2D0; -.
DR OpenTargets; ENSG00000169239; -.
DR PharmGKB; PA25993; -.
DR VEuPathDB; HostDB:ENSG00000169239; -.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000156978; -.
DR HOGENOM; CLU_039326_2_1_1; -.
DR InParanoid; Q9Y2D0; -.
DR OMA; GESNDWG; -.
DR OrthoDB; 1377476at2759; -.
DR PhylomeDB; Q9Y2D0; -.
DR TreeFam; TF316425; -.
DR BRENDA; 4.2.1.1; 2681.
DR PathwayCommons; Q9Y2D0; -.
DR Reactome; R-HSA-1475029; Reversible hydration of carbon dioxide.
DR SignaLink; Q9Y2D0; -.
DR BioGRID-ORCS; 11238; 15 hits in 712 CRISPR screens.
DR ChiTaRS; CA5B; human.
DR GeneWiki; CA5B; -.
DR GenomeRNAi; 11238; -.
DR Pharos; Q9Y2D0; Tclin.
DR PRO; PR:Q9Y2D0; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9Y2D0; protein.
DR Bgee; ENSG00000169239; Expressed in calcaneal tendon and 113 other tissues.
DR ExpressionAtlas; Q9Y2D0; baseline and differential.
DR Genevisible; Q9Y2D0; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0004089; F:carbonate dehydratase activity; IBA:GO_Central.
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; IEA:Ensembl.
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 CHAIN 34..317
FT /note="Carbonic anhydrase 5B, mitochondrial"
FT /id="PRO_0000004237"
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; 36434 MW; 7CA11920EFF2588A CRC64;
MVVMNSLRVI LQASPGKLLW RKFQIPRFMP ARPCSLYTCT YKTRNRALHP LWESVDLVPG
GDRQSPINIR WRDSVYDPGL KPLTISYDPA TCLHVWNNGY SFLVEFEDST DKSVIKGGPL
EHNYRLKQFH FHWGAIDAWG SEHTVDSKCF PAELHLVHWN AVRFENFEDA ALEENGLAVI
GVFLKLGKHH KELQKLVDTL PSIKHKDALV EFGSFDPSCL MPTCPDYWTY SGSLTTPPLS
ESVTWIIKKQ PVEVDHDQLE QFRTLLFTSE GEKEKRMVDN FRPLQPLMNR TVRSSFRHDY
VLNVQAKPKP ATSQATP
