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P23589 (CAH5A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carbonic anhydrase 5A, mitochondrial

EC=4.2.1.1
Alternative name(s):
Carbonate dehydratase VA
Short name=CA Y
Carbonic anhydrase VA
Short name=CA-VA
Gene names
Name:Ca5a
Synonyms:Ca5, Car5, Car5a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length299 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reversible hydration of carbon dioxide. Low activity.

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Zinc.

Enzyme regulation

Inhibited by acetazolamide By similarity.

Subcellular location

Mitochondrion.

Tissue specificity

Liver.

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7-8. Ref.4

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2929Mitochondrion Ref.2
Chain30 – 299270Carbonic anhydrase 5A, mitochondrial
PRO_0000004235

Regions

Region229 – 2302Substrate binding By similarity

Sites

Active site941 Probable
Active site1581 By similarity
Active site1611 Probable
Metal binding1241Zinc; catalytic
Metal binding1261Zinc; catalytic
Metal binding1491Zinc; catalytic

Amino acid modifications

Modified residue661N6-succinyllysine Ref.5

Natural variations

Natural variant151 – 1533VHW → FM in strain: BIO-HTT.

Experimental info

Mutagenesis941Y → A: Normal activity. Ref.6 Ref.7
Mutagenesis941Y → H: Normal activity. Enhanced proton transfer due to removal of the steric hindrance of F-95; when associated with A-95. Ref.6 Ref.7
Mutagenesis951F → A: Normal activity. Enhanced proton transfer; when associated with H-94 or C-161. Ref.4 Ref.7 Ref.8
Mutagenesis1211K → C: Normal activity. Ref.4
Mutagenesis1611Y → A: Normal activity. Ref.4 Ref.7 Ref.8
Mutagenesis1611Y → C: Normal activity. Enhanced proton transfer; when associated with A-95. Ref.4 Ref.7 Ref.8
Mutagenesis1611Y → H: Normal activity. Ref.4 Ref.7 Ref.8

Secondary structure

............................................. 299
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23589 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 2698CABA00686151

FASTA29934,072
        10         20         30         40         50         60 
MLRRDPRKPL AILRHVGLLC ATGPQRWRFQ HSCAEEHSNC ARHPLWTGPV SSAEGTRQSP 

        70         80         90        100        110        120 
INIQWKDSVY DPQLAPLRVS YDAASCRYLW NTGYFFQVEF DDSCEDSGIS GGPLGNHYRL 

       130        140        150        160        170        180 
KQFHFHWGAT DEWGSEHAVD GHTYPAELHL VHWNSTKYEN YKKASVGENG LAVIGVFLKL 

       190        200        210        220        230        240 
GAHHQALQKL VDVLPEVRHK DTQVAMGPFD PSCLLPACRD YWTYPGSLTT PPLAESVTWI 

       250        260        270        280        290 
VQKTPVEVSP SQLSTFRTLL FSGRGEEEDV MVNNYRPLQP LRDRKLRSSF RLDRTKMRS 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide and derived amino-acid sequence of a cDNA encoding a new mouse carbonic anhydrase."
Amor-Gueret M., Levi-Strauss M.
Nucleic Acids Res. 18:1646-1646(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BIO-HTT.
Tissue: Liver.
[2]"Mitochondrial carbonic anhydrase (isozyme V) in mouse and rat: cDNA cloning, expression, subcellular localization, processing, and tissue distribution."
Nagao Y., Srinivasan M., Platero J.S., Svendrowski M., Waheed A., Sly W.S.
Proc. Natl. Acad. Sci. U.S.A. 91:10330-10334(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 30-41.
Tissue: Liver.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver.
[4]"Introduction of histidine analogs leads to enhanced proton transfer in carbonic anhydrase V."
Earnhardt J.N., Wright S.K., Qian M., Tu C., Laipis P.J., Viola R.E., Silverman D.N.
Arch. Biochem. Biophys. 361:264-270(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF PHE-95; LYS-121 AND TYR-161.
[5]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
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.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"Structure determination of murine mitochondrial carbonic anhydrase V at 2.45-A resolution: implications for catalytic proton transfer and inhibitor design."
Boriack-Sjodin P.A., Heck R.W., Laipis P.J., Silverman D.N., Christianson D.W.
Proc. Natl. Acad. Sci. U.S.A. 92:10949-10953(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 55-299 IN COMPLEX WITH INHIBITORS AND ZINC ION, MUTAGENESIS OF TYR-94.
[7]"Structure-based design of an intramolecular proton transfer site in murine carbonic anhydrase V."
Heck R.W., Boriack-Sjodin P.A., Qian M., Tu C., Christianson D.W., Laipis P.J., Silverman D.N.
Biochemistry 35:11605-11611(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 52-299 IN COMPLEX WITH ZINC ION, MUTAGENESIS OF TYR-94; PHE-95 AND TYR-161.
[8]"Crystal structure of F65A/Y131C-methylimidazole carbonic anhydrase V reveals architectural features of an engineered proton shuttle."
Jude K.M., Wright S.K., Tu C., Silverman D.N., Viola R.E., Christianson D.W.
Biochemistry 41:2485-2491(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 55-299 IN COMPLEX WITH INHIBITORS AND ZINC ION, MUTAGENESIS OF PHE-95 AND TYR-161.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X51971 mRNA. Translation: CAA36233.1.
BC030174 mRNA. Translation: AAH30174.1.
PIRS12579.
RefSeqNP_031634.2. NM_007608.2.
UniGeneMm.116761.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DMXX-ray2.45A/B55-299[»]
1DMYX-ray2.45A/B55-299[»]
1KEQX-ray1.88A/B55-299[»]
1URTX-ray2.80A52-299[»]
ProteinModelPortalP23589.
SMRP23589. Positions 55-290.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP23589. 1 interaction.
MINTMINT-4089763.

Chemistry

BindingDBP23589.

PTM databases

PhosphoSiteP23589.

Proteomic databases

PaxDbP23589.
PRIDEP23589.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000057653; ENSMUSP00000060457; ENSMUSG00000025317.
GeneID12352.
KEGGmmu:12352.
UCSCuc009nsf.2. mouse.

Organism-specific databases

CTD12352.
MGIMGI:101946. Car5a.

Phylogenomic databases

eggNOGCOG3338.
GeneTreeENSGT00750000117305.
HOGENOMHOG000112637.
HOVERGENHBG002837.
InParanoidP23589.
KOK01672.
OMAFFQVEFD.
OrthoDBEOG7WMCK7.
PhylomeDBP23589.
TreeFamTF316425.

Gene expression databases

BgeeP23589.
CleanExMM_CAR5A.
GenevestigatorP23589.

Family and domain databases

Gene3D3.10.200.10. 1 hit.
InterProIPR018437. CA-VB_mt.
IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF25. PTHR18952:SF25. 1 hit.
PfamPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMSSF51069. SSF51069. 1 hit.
PROSITEPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP23589.
NextBio281008.
PROP23589.
SOURCESearch...

Entry information

Entry nameCAH5A_MOUSE
AccessionPrimary (citable) accession number: P23589
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot