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

 CAH5A_MOUSE             Reviewed;         299 AA.
P23589;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 2.
28-FEB-2018, entry version 161.
RecName: Full=Carbonic anhydrase 5A, mitochondrial;
EC=4.2.1.1;
AltName: Full=Carbonate dehydratase VA;
Short=CA Y;
AltName: Full=Carbonic anhydrase VA;
Short=CA-VA;
Flags: Precursor;
Name=Ca5a; Synonyms=Ca5, Car5, Car5a;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BIO-HTT; TISSUE=Liver;
PubMed=2109313; DOI=10.1093/nar/18.6.1646;
Amor-Gueret M., Levi-Strauss M.;
"Nucleotide and derived amino-acid sequence of a cDNA encoding a new
mouse carbonic anhydrase.";
Nucleic Acids Res. 18:1646-1646(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 30-41.
TISSUE=Liver;
PubMed=7937950; DOI=10.1073/pnas.91.22.10330;
Nagao Y., Srinivasan M., Platero J.S., Svendrowski M., Waheed A.,
Sly W.S.;
"Mitochondrial carbonic anhydrase (isozyme V) in mouse and rat: cDNA
cloning, expression, subcellular localization, processing, and tissue
distribution.";
Proc. Natl. Acad. Sci. U.S.A. 91:10330-10334(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Liver;
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).
[4]
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF PHE-95; LYS-121 AND
TYR-161.
PubMed=9882455; DOI=10.1006/abbi.1998.0984;
Earnhardt J.N., Wright S.K., Qian M., Tu C., Laipis P.J., Viola R.E.,
Silverman D.N.;
"Introduction of histidine analogs leads to enhanced proton transfer
in carbonic anhydrase V.";
Arch. Biochem. Biophys. 361:264-270(1999).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-66, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[7]
X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 55-299 IN COMPLEX WITH
INHIBITORS AND ZINC ION, AND MUTAGENESIS OF TYR-94.
PubMed=7479916; DOI=10.1073/pnas.92.24.10949;
Boriack-Sjodin P.A., Heck R.W., Laipis P.J., Silverman D.N.,
Christianson D.W.;
"Structure determination of murine mitochondrial carbonic anhydrase V
at 2.45-A resolution: implications for catalytic proton transfer and
inhibitor design.";
Proc. Natl. Acad. Sci. U.S.A. 92:10949-10953(1995).
[8]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 52-299 IN COMPLEX WITH ZINC
ION, AND MUTAGENESIS OF TYR-94; PHE-95 AND TYR-161.
PubMed=8794740; DOI=10.1021/bi9608018;
Heck R.W., Boriack-Sjodin P.A., Qian M., Tu C., Christianson D.W.,
Laipis P.J., Silverman D.N.;
"Structure-based design of an intramolecular proton transfer site in
murine carbonic anhydrase V.";
Biochemistry 35:11605-11611(1996).
[9]
X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 55-299 IN COMPLEX WITH
INHIBITORS AND ZINC ION, AND MUTAGENESIS OF PHE-95 AND TYR-161.
PubMed=11851394; DOI=10.1021/bi015808q;
Jude K.M., Wright S.K., Tu C., Silverman D.N., Viola R.E.,
Christianson D.W.;
"Crystal structure of F65A/Y131C-methylimidazole carbonic anhydrase V
reveals architectural features of an engineered proton shuttle.";
Biochemistry 41:2485-2491(2002).
-!- 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:0000269|PubMed:11851394,
ECO:0000269|PubMed:7479916, ECO:0000269|PubMed:8794740};
-!- ENZYME REGULATION: Inhibited by acetazolamide. {ECO:0000250}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 7-8. {ECO:0000269|PubMed:9882455};
-!- SUBCELLULAR LOCATION: Mitochondrion.
-!- TISSUE SPECIFICITY: Liver.
-!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X51971; CAA36233.1; -; mRNA.
EMBL; BC030174; AAH30174.1; -; mRNA.
CCDS; CCDS22731.1; -.
PIR; S12579; S12579.
RefSeq; NP_031634.2; NM_007608.2.
UniGene; Mm.116761; -.
PDB; 1DMX; X-ray; 2.45 A; A/B=53-299.
PDB; 1DMY; X-ray; 2.45 A; A/B=53-299.
PDB; 1KEQ; X-ray; 1.88 A; A/B=53-299.
PDB; 1URT; X-ray; 2.80 A; A=52-299.
PDBsum; 1DMX; -.
PDBsum; 1DMY; -.
PDBsum; 1KEQ; -.
PDBsum; 1URT; -.
ProteinModelPortal; P23589; -.
SMR; P23589; -.
IntAct; P23589; 1.
MINT; P23589; -.
BindingDB; P23589; -.
iPTMnet; P23589; -.
PhosphoSitePlus; P23589; -.
MaxQB; P23589; -.
PaxDb; P23589; -.
PeptideAtlas; P23589; -.
PRIDE; P23589; -.
Ensembl; ENSMUST00000057653; ENSMUSP00000060457; ENSMUSG00000025317.
GeneID; 12352; -.
KEGG; mmu:12352; -.
UCSC; uc009nsf.2; mouse.
CTD; 12352; -.
MGI; MGI:101946; Car5a.
eggNOG; KOG0382; Eukaryota.
eggNOG; COG3338; LUCA.
GeneTree; ENSGT00760000118915; -.
HOGENOM; HOG000112637; -.
HOVERGEN; HBG002837; -.
InParanoid; P23589; -.
KO; K01672; -.
OMA; NNFRPPM; -.
OrthoDB; EOG091G0XFM; -.
PhylomeDB; P23589; -.
TreeFam; TF316425; -.
Reactome; R-MMU-1475029; Reversible hydration of carbon dioxide.
EvolutionaryTrace; P23589; -.
PRO; PR:P23589; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000025317; -.
CleanEx; MM_CAR5A; -.
Genevisible; P23589; MM.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0004089; F:carbonate dehydratase activity; IDA:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006094; P:gluconeogenesis; TAS:MGI.
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;
3D-structure; Complete proteome; Direct protein sequencing; Lyase;
Metal-binding; Mitochondrion; Reference proteome; Transit peptide;
Zinc.
TRANSIT 1 29 Mitochondrion.
{ECO:0000269|PubMed:7937950}.
CHAIN 30 299 Carbonic anhydrase 5A, mitochondrial.
/FTId=PRO_0000004235.
DOMAIN 30 290 Alpha-carbonic anhydrase.
{ECO:0000255|PROSITE-ProRule:PRU01134}.
REGION 229 230 Substrate binding.
{ECO:0000250|UniProtKB:P00918}.
ACT_SITE 94 94 {ECO:0000305}.
ACT_SITE 158 158 {ECO:0000250|UniProtKB:P00918}.
ACT_SITE 161 161 {ECO:0000305}.
METAL 124 124 Zinc; catalytic.
{ECO:0000269|PubMed:11851394,
ECO:0000269|PubMed:7479916,
ECO:0000269|PubMed:8794740}.
METAL 126 126 Zinc; catalytic.
{ECO:0000269|PubMed:11851394,
ECO:0000269|PubMed:7479916,
ECO:0000269|PubMed:8794740}.
METAL 149 149 Zinc; catalytic.
{ECO:0000269|PubMed:11851394,
ECO:0000269|PubMed:7479916,
ECO:0000269|PubMed:8794740}.
MOD_RES 66 66 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
VARIANT 151 153 VHW -> FM (in strain: BIO-HTT).
MUTAGEN 94 94 Y->A: Normal activity.
{ECO:0000269|PubMed:7479916,
ECO:0000269|PubMed:8794740}.
MUTAGEN 94 94 Y->H: Normal activity. Enhanced proton
transfer due to removal of the steric
hindrance of F-95; when associated with
A-95. {ECO:0000269|PubMed:7479916,
ECO:0000269|PubMed:8794740}.
MUTAGEN 95 95 F->A: Normal activity. Enhanced proton
transfer; when associated with H-94 or C-
161. {ECO:0000269|PubMed:11851394,
ECO:0000269|PubMed:8794740,
ECO:0000269|PubMed:9882455}.
MUTAGEN 121 121 K->C: Normal activity.
{ECO:0000269|PubMed:9882455}.
MUTAGEN 161 161 Y->A: Normal activity.
{ECO:0000269|PubMed:11851394,
ECO:0000269|PubMed:8794740,
ECO:0000269|PubMed:9882455}.
MUTAGEN 161 161 Y->C: Normal activity. Enhanced proton
transfer; when associated with A-95.
{ECO:0000269|PubMed:11851394,
ECO:0000269|PubMed:8794740,
ECO:0000269|PubMed:9882455}.
MUTAGEN 161 161 Y->H: Normal activity.
{ECO:0000269|PubMed:11851394,
ECO:0000269|PubMed:8794740,
ECO:0000269|PubMed:9882455}.
HELIX 65 67 {ECO:0000244|PDB:1KEQ}.
STRAND 68 70 {ECO:0000244|PDB:1KEQ}.
STRAND 75 80 {ECO:0000244|PDB:1KEQ}.
HELIX 83 85 {ECO:0000244|PDB:1KEQ}.
STRAND 86 91 {ECO:0000244|PDB:1KEQ}.
STRAND 93 100 {ECO:0000244|PDB:1KEQ}.
STRAND 104 112 {ECO:0000244|PDB:1KEQ}.
STRAND 118 127 {ECO:0000244|PDB:1KEQ}.
STRAND 136 139 {ECO:0000244|PDB:1KEQ}.
STRAND 145 154 {ECO:0000244|PDB:1KEQ}.
TURN 155 157 {ECO:0000244|PDB:1KEQ}.
HELIX 161 164 {ECO:0000244|PDB:1KEQ}.
STRAND 171 182 {ECO:0000244|PDB:1KEQ}.
HELIX 185 191 {ECO:0000244|PDB:1KEQ}.
HELIX 192 196 {ECO:0000244|PDB:1KEQ}.
STRAND 203 205 {ECO:0000244|PDB:1KEQ}.
HELIX 211 214 {ECO:0000244|PDB:1KEQ}.
STRAND 221 226 {ECO:0000244|PDB:1KEQ}.
STRAND 237 244 {ECO:0000244|PDB:1KEQ}.
STRAND 246 248 {ECO:0000244|PDB:1KEQ}.
HELIX 250 256 {ECO:0000244|PDB:1KEQ}.
STRAND 260 262 {ECO:0000244|PDB:1KEQ}.
STRAND 264 266 {ECO:0000244|PDB:1DMX}.
STRAND 286 290 {ECO:0000244|PDB:1KEQ}.
SEQUENCE 299 AA; 34072 MW; 2698CABA00686151 CRC64;
MLRRDPRKPL AILRHVGLLC ATGPQRWRFQ HSCAEEHSNC ARHPLWTGPV SSAEGTRQSP
INIQWKDSVY DPQLAPLRVS YDAASCRYLW NTGYFFQVEF DDSCEDSGIS GGPLGNHYRL
KQFHFHWGAT DEWGSEHAVD GHTYPAELHL VHWNSTKYEN YKKASVGENG LAVIGVFLKL
GAHHQALQKL VDVLPEVRHK DTQVAMGPFD PSCLLPACRD YWTYPGSLTT PPLAESVTWI
VQKTPVEVSP SQLSTFRTLL FSGRGEEEDV MVNNYRPLQP LRDRKLRSSF RLDRTKMRS


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