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Carbonic anhydrase 5A, mitochondrial (EC 4.2.1.1) (Carbonate dehydratase VA) (Carbonic anhydrase VA) (CA-VA)

 CAH5A_HUMAN             Reviewed;         305 AA.
P35218; B2RPF2;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
28-FEB-2018, entry version 155.
RecName: Full=Carbonic anhydrase 5A, mitochondrial;
EC=4.2.1.1;
AltName: Full=Carbonate dehydratase VA;
AltName: Full=Carbonic anhydrase VA;
Short=CA-VA;
Flags: Precursor;
Name=CA5A; Synonyms=CA5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Liver;
PubMed=8356065; DOI=10.1073/pnas.90.16.7623;
Nagao Y., Platero J.S., Waheed A., Sly W.S.;
"Human mitochondrial carbonic anhydrase: cDNA cloning, expression,
subcellular localization, and mapping to chromosome 16.";
Proc. Natl. Acad. Sci. U.S.A. 90:7623-7627(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Umbilical cord;
PubMed=7490083; DOI=10.1006/geno.1995.1177;
Nagao Y., Batanian J.R., Clemente M.F., Sly W.S.;
"Genomic organization of the human gene (CA5) and pseudogene for
mitochondrial carbonic anhydrase V and their localization to
chromosomes 16q and 16p.";
Genomics 28:477-484(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
ENZYME REGULATION.
PubMed=16807956; DOI=10.1002/chem.200600159;
Temperini C., Scozzafava A., Vullo D., Supuran C.T.;
"Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA,
VII, and XIV with l- and d-histidine and crystallographic analysis of
their adducts with isoform II: engineering proton-transfer processes
within the active site of an enzyme.";
Chemistry 12:7057-7066(2006).
[6]
ENZYME REGULATION.
PubMed=16686544; DOI=10.1021/jm0603320;
Temperini C., Scozzafava A., Vullo D., Supuran C.T.;
"Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA,
VII, and XIV with L- and D-phenylalanine and crystallographic analysis
of their adducts with isozyme II: stereospecific recognition within
the active site of an enzyme and its consequences for the drug
design.";
J. Med. Chem. 49:3019-3027(2006).
[7]
ENZYME REGULATION.
PubMed=17127057; DOI=10.1016/j.bmcl.2006.11.027;
Temperini C., Innocenti A., Scozzafava A., Mastrolorenzo A.,
Supuran C.T.;
"Carbonic anhydrase activators: L-Adrenaline plugs the active site
entrance of isozyme II, activating better isoforms I, IV, VA, VII, and
XIV.";
Bioorg. Med. Chem. Lett. 17:628-635(2007).
[8]
ENZYME REGULATION.
PubMed=17314045; DOI=10.1016/j.bmcl.2007.01.113;
Temperini C., Innocenti A., Guerri A., Scozzafava A., Rusconi S.,
Supuran C.T.;
"Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-
ray crystal structure of the antiviral drug foscarnet complexed to
human carbonic anhydrase I.";
Bioorg. Med. Chem. Lett. 17:2210-2215(2007).
[9]
ENZYME REGULATION.
PubMed=19186056; DOI=10.1016/j.bmcl.2009.01.038;
Crocetti L., Maresca A., Temperini C., Hall R.A., Scozzafava A.,
Muehlschlegel F.A., Supuran C.T.;
"A thiabendazole sulfonamide shows potent inhibitory activity against
mammalian and nematode alpha-carbonic anhydrases.";
Bioorg. Med. Chem. Lett. 19:1371-1375(2009).
[10]
ENZYME REGULATION.
PubMed=19206230; DOI=10.1021/ja809683v;
Maresca A., Temperini C., Vu H., Pham N.B., Poulsen S.-A.,
Scozzafava A., Quinn R.J., Supuran C.T.;
"Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a
new class of suicide inhibitors.";
J. Am. Chem. Soc. 131:3057-3062(2009).
[11]
BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME REGULATION.
PubMed=18618712; DOI=10.1002/prot.22144;
Di Fiore A., Monti S.M., Hilvo M., Parkkila S., Romano V., Scaloni A.,
Pedone C., Scozzafava A., Supuran C.T., De Simone G.;
"Crystal structure of human carbonic anhydrase XIII and its complex
with the inhibitor acetazolamide.";
Proteins 74:164-175(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
VARIANT CA5AD PRO-233, AND CHARACTERIZATION OF VARIANT CA5AD PRO-233.
PubMed=24530203; DOI=10.1016/j.ajhg.2014.01.006;
van Karnebeek C.D., Sly W.S., Ross C.J., Salvarinova R.,
Yaplito-Lee J., Santra S., Shyr C., Horvath G.A., Eydoux P.,
Lehman A.M., Bernard V., Newlove T., Ukpeh H., Chakrapani A.,
Preece M.A., Ball S., Pitt J., Vallance H.D., Coulter-Mackie M.,
Nguyen H., Zhang L.H., Bhavsar A.P., Sinclair G., Waheed A.,
Wasserman W.W., Stockler-Ipsiroglu S.;
"Mitochondrial carbonic anhydrase VA deficiency resulting from CA5A
alterations presents with hyperammonemia in early childhood.";
Am. J. Hum. Genet. 94:453-461(2014).
-!- FUNCTION: Reversible hydration of carbon dioxide. Low activity.
-!- CATALYTIC ACTIVITY: H(2)CO(3) = CO(2) + H(2)O.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:P23589};
-!- ENZYME REGULATION: Activated by histamine, L-adrenaline, L- and D-
histidine, and L- and D-phenylalanine. Inhibited by coumarins,
sulfonamide derivatives such as acetazolamide and Foscarnet
(phosphonoformate trisodium salt). {ECO:0000269|PubMed:16686544,
ECO:0000269|PubMed:16807956, ECO:0000269|PubMed:17127057,
ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:18618712,
ECO:0000269|PubMed:19186056, ECO:0000269|PubMed:19206230}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=10.0 mM for CO(2) {ECO:0000269|PubMed:18618712};
-!- SUBCELLULAR LOCATION: Mitochondrion.
-!- DISEASE: Hyperammonemia due to carbonic anhydrase VA deficiency
(CA5AD) [MIM:615751]: An autosomal recessive inborn error of
metabolism, clinically characterized by infantile hyperammonemic
encephalopathy. Metabolic abnormalities include hypoglycemia,
hyperlactatemia, metabolic acidosis and respiratory alkalosis.
{ECO:0000269|PubMed:24530203}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L19297; AAA02890.1; -; mRNA.
EMBL; U25134; AAC99806.1; -; Genomic_DNA.
EMBL; S80181; AAB47048.1; -; Genomic_DNA.
EMBL; S80175; AAB47048.1; JOINED; Genomic_DNA.
EMBL; S80176; AAB47048.1; JOINED; Genomic_DNA.
EMBL; S80177; AAB47048.1; JOINED; Genomic_DNA.
EMBL; S80178; AAB47048.1; JOINED; Genomic_DNA.
EMBL; S80240; AAB47048.1; JOINED; Genomic_DNA.
EMBL; S80180; AAB47048.1; JOINED; Genomic_DNA.
EMBL; CH471114; EAW95372.1; -; Genomic_DNA.
EMBL; BC137405; AAI37406.1; -; mRNA.
EMBL; BC137411; AAI37412.1; -; mRNA.
CCDS; CCDS10965.1; -.
PIR; A47745; CRHU5.
RefSeq; NP_001730.1; NM_001739.1.
UniGene; Hs.177446; -.
ProteinModelPortal; P35218; -.
SMR; P35218; -.
BioGrid; 107218; 5.
STRING; 9606.ENSP00000309649; -.
BindingDB; P35218; -.
ChEMBL; CHEMBL4789; -.
DrugBank; DB03385; 4-Methylimidazole.
DrugBank; DB01194; Brinzolamide.
DrugBank; DB08846; Ellagic Acid.
DrugBank; DB00909; Zonisamide.
iPTMnet; P35218; -.
PhosphoSitePlus; P35218; -.
BioMuta; CA5A; -.
DMDM; 461680; -.
MaxQB; P35218; -.
PaxDb; P35218; -.
PeptideAtlas; P35218; -.
PRIDE; P35218; -.
Ensembl; ENST00000309893; ENSP00000309649; ENSG00000174990.
GeneID; 763; -.
KEGG; hsa:763; -.
UCSC; uc002fkn.2; human.
CTD; 763; -.
DisGeNET; 763; -.
EuPathDB; HostDB:ENSG00000174990.4; -.
GeneCards; CA5A; -.
HGNC; HGNC:1377; CA5A.
MalaCards; CA5A; -.
MIM; 114761; gene.
MIM; 615751; phenotype.
neXtProt; NX_P35218; -.
OpenTargets; ENSG00000174990; -.
Orphanet; 401948; Hyperammonemic encephalopathy due to carbonic anhydrase VA deficiency.
PharmGKB; PA25992; -.
eggNOG; KOG0382; Eukaryota.
eggNOG; COG3338; LUCA.
GeneTree; ENSGT00760000118915; -.
HOGENOM; HOG000112637; -.
HOVERGEN; HBG002837; -.
InParanoid; P35218; -.
KO; K01672; -.
OMA; NNFRPPM; -.
OrthoDB; EOG091G0XFM; -.
PhylomeDB; P35218; -.
TreeFam; TF316425; -.
BRENDA; 4.2.1.1; 2681.
Reactome; R-HSA-1475029; Reversible hydration of carbon dioxide.
SABIO-RK; P35218; -.
ChiTaRS; CA5A; human.
GenomeRNAi; 763; -.
PRO; PR:P35218; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000174990; -.
CleanEx; HS_CA5A; -.
Genevisible; P35218; HS.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; TAS:ProtInc.
GO; GO:0004089; F:carbonate dehydratase activity; TAS:Reactome.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0015701; P:bicarbonate transport; TAS:Reactome.
GO; GO:0006730; P:one-carbon metabolic process; IEA:InterPro.
Gene3D; 3.10.200.10; -; 1.
InterPro; IPR001148; Carbonic_anhydrase_a.
InterPro; IPR023561; Carbonic_anhydrase_a-class.
InterPro; IPR018338; Carbonic_anhydrase_a-class_CS.
InterPro; IPR036398; Carbonic_anhydrase_a_sf.
PANTHER; PTHR18952; PTHR18952; 1.
Pfam; PF00194; Carb_anhydrase; 1.
SMART; SM01057; Carb_anhydrase; 1.
SUPFAM; SSF51069; SSF51069; 1.
PROSITE; PS00162; ALPHA_CA_1; 1.
PROSITE; PS51144; ALPHA_CA_2; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disease mutation; Lyase;
Metal-binding; Mitochondrion; Reference proteome; Transit peptide;
Zinc.
TRANSIT 1 38 Mitochondrion.
CHAIN 39 305 Carbonic anhydrase 5A, mitochondrial.
/FTId=PRO_0000004234.
DOMAIN 39 296 Alpha-carbonic anhydrase.
{ECO:0000255|PROSITE-ProRule:PRU01134}.
REGION 235 236 Substrate binding. {ECO:0000250}.
ACT_SITE 164 164 {ECO:0000250|UniProtKB:P00918}.
METAL 130 130 Zinc; catalytic.
{ECO:0000250|UniProtKB:P23589}.
METAL 132 132 Zinc; catalytic.
{ECO:0000250|UniProtKB:P23589}.
METAL 155 155 Zinc; catalytic.
{ECO:0000250|UniProtKB:P23589}.
VARIANT 233 233 S -> P (in CA5AD; reduced enzymatic
activity; dbSNP:rs587777316).
{ECO:0000269|PubMed:24530203}.
/FTId=VAR_071188.
SEQUENCE 305 AA; 34750 MW; C4E998D269AB1FE5 CRC64;
MLGRNTWKTS AFSFLVEQMW APLWSRSMRP GRWCSQRSCA WQTSNNTLHP LWTVPVSVPG
GTRQSPINIQ WRDSVYDPQL KPLRVSYEAA SCLYIWNTGY LFQVEFDDAT EASGISGGPL
ENHYRLKQFH FHWGAVNEGG SEHTVDGHAY PAELHLVHWN SVKYQNYKEA VVGENGLAVI
GVFLKLGAHH QTLQRLVDIL PEIKHKDARA AMRPFDPSTL LPTCWDYWTY AGSLTTPPLT
ESVTWIIQKE PVEVAPSQLS AFRTLLFSAL GEEEKMMVNN YRPLQPLMNR KVWASFQATN
EGTRS


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