Carbonic anhydrase 5A, mitochondrial precursor

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P23589 (CAH5A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 128. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	299 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	gluconeogenesis Traceable author statement PubMed 7929150. Source: MGI one-carbon metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	mitochondrion Inferred from direct assay PubMed 10677517 PubMed 14651853 PubMed 18614015 Ref.2. Source: MGI
Molecular_function	carbonate dehydratase activity Inferred from direct assay PubMed 10677517 PubMed 7929150. Source: MGI zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 29

Mitochondrion Ref.2

Chain

30 – 299

270

Carbonic anhydrase 5A, mitochondrial

PRO_0000004235

Regions

Region

229 – 230

Substrate binding By similarity

Sites

Active site

Probable

Active site

158

By similarity

Active site

161

Probable

Metal binding

124

Zinc; catalytic

Metal binding

126

Zinc; catalytic

Metal binding

149

Zinc; catalytic

Natural variations

Natural variant

151 – 153

VHW → FM in strain: BIO-HTT.

Experimental info

Mutagenesis

Y → A: Normal activity. Ref.5 Ref.6

Mutagenesis

Y → H: Normal activity. Enhanced proton transfer due to removal of the steric hindrance of F-95; when associated with A-95. Ref.5 Ref.6

Mutagenesis

F → A: Normal activity. Enhanced proton transfer; when associated with H-94 or C-161. Ref.4 Ref.6 Ref.7

Mutagenesis

121

K → C: Normal activity. Ref.4

Mutagenesis

161

Y → A: Normal activity. Ref.4 Ref.6 Ref.7

Mutagenesis

161

Y → C: Normal activity. Enhanced proton transfer; when associated with A-95. Ref.4 Ref.6 Ref.7

Mutagenesis

161

Y → H: Normal activity. Ref.4 Ref.6 Ref.7

Secondary structure

299

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P23589 [UniParc].

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

FASTA

299

34,072

        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' referencesShow '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]	"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.
[6]	"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.
[7]	"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.

IPI

IPI00133663.

PIR

S12579.

RefSeq

NP_031634.2. NM_007608.2.

UniGene

Mm.116761.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DMX	X-ray	2.45	A/B	55-299	[»]
1DMY	X-ray	2.45	A/B	55-299	[»]
1KEQ	X-ray	1.88	A/B	55-299	[»]
1URT	X-ray	2.80	A	52-299	[»]

ProteinModelPortal

P23589.

SMR

P23589. Positions 55-290.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-4089763.

PTM databases

PhosphoSite

P23589.

Proteomic databases

PaxDb

P23589.

PRIDE

P23589.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000057653; ENSMUSP00000060457; ENSMUSG00000025317.

GeneID

12352.

KEGG

mmu:12352.

UCSC

uc009nsf.2. mouse.

Organism-specific databases

CTD

12352.

MGI

MGI:101946. Car5a.

Phylogenomic databases

eggNOG

COG3338.

GeneTree

ENSGT00560000076828.

HOGENOM

HOG000112637.

HOVERGEN

HBG002837.

InParanoid

P23589.

K01672.

OMA

FDDSTEG.

OrthoDB

EOG4FR0RX.

Gene expression databases

Bgee

P23589.

CleanEx

MM_CAR5A.

Genevestigator

P23589.

GermOnline

ENSMUSG00000025317. Mus musculus.

Family and domain databases

Gene3D

3.10.200.10. 1 hit.

InterPro

IPR018437. CA-V_mt.
IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]

PANTHER

PTHR18952. PTHR18952. 1 hit.
PTHR18952:SF25. PTHR18952:SF25. 1 hit.

Pfam

PF00194. Carb_anhydrase. 1 hit.
[Graphical view]

SMART

SM01057. Carb_anhydrase. 1 hit.
[Graphical view]

SUPFAM

SSF51069. Euk_COanhd. 1 hit.

PROSITE

PS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P23589.

ChEMBL

CHEMBL2330.

EvolutionaryTrace

P23589.

NextBio

281008.

SOURCE

Search...

Entry information

Entry name

CAH5A_MOUSE

Accession

Primary (citable) accession number: P23589

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1995
Last modified:	May 29, 2013
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents