P23589 (CAH5A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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)

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. Source: MGI one-carbon metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrion Inferred from direct assay Ref.2. Source: MGI
Molecular function	carbonate dehydratase activity Inferred from direct assay. 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

29

Mitochondrion Ref.2

Chain

30 – 299

270

Carbonic anhydrase 5A, mitochondrial

PRO_0000004235

Regions

Region

229 – 230

2

Substrate binding By similarity

Sites

Active site

94

1

Probable

Active site

158

1

By similarity

Active site

161

1

Probable

Metal binding

124

1

Zinc; catalytic

Metal binding

126

1

Zinc; catalytic

Metal binding

149

1

Zinc; catalytic

Natural variations

Natural variant

151 – 153

3

VHW → FM in strain: BIO-HTT.

Experimental info

Mutagenesis

94

1

Y → A: Normal activity. Ref.5 Ref.6

Mutagenesis

94

1

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

95

1

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

Mutagenesis

121

1

K → C: Normal activity. Ref.4

Mutagenesis

161

1

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

Mutagenesis

161

1

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

Mutagenesis

161

1

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

Secondary structure

1

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299

Helix Strand Turn

Details...

Helix

65 – 67

3

Beta strand

68 – 70

3

Beta strand

75 – 80

6

Helix

83 – 85

3

Beta strand

86 – 91

6

Beta strand

93 – 100

8

Beta strand

107 – 112

6

Beta strand

118 – 127

10

Beta strand

136 – 139

4

Beta strand

145 – 153

9

Turn

155 – 157

3

Helix

161 – 164

4

Beta strand

171 – 182

12

Helix

185 – 191

7

Helix

192 – 196

5

Beta strand

203 – 205

3

Helix

211 – 214

4

Beta strand

221 – 226

6

Beta strand

237 – 244

8

Beta strand

246 – 248

3

Helix

250 – 256

7

Beta strand

260 – 262

3

Beta strand

264 – 266

3

Beta strand

286 – 288

3

Sequences

	Sequence		Length	Mass (Da)
	P23589 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: 2698CABA00686151	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

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: 2109313] [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: 7937950] [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: 15489334] [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: 9882455] [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: 7479916] [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: 8794740] [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: 11851394] [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 26-291.

ModBase

Search...

Proteomic databases

PRIDE

P23589.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000057653; ENSMUSP00000060457; ENSMUSG00000025317.

GeneID

12352.

KEGG

mmu:12352.

UCSC

uc009nsf.1. mouse.

Organism-specific databases

CTD

12352.

MGI

MGI:101946. Car5a.

Phylogenomic databases

eggNOG

roNOG11543.

GeneTree

ENSGT00560000076828.

HOGENOM

HBG717384.

HOVERGEN

HBG002837.

InParanoid

P23589.

OMA

SYDAASC.

OrthoDB

EOG4FR0RX.

PhylomeDB

P23589.

Gene expression databases

ArrayExpress

P23589.

Bgee

P23589.

CleanEx

MM_CAR5A.

Genevestigator

P23589.

GermOnline

ENSMUSG00000025317. Mus musculus.

Family and domain databases

InterPro

IPR001148. a_carbonic_anhydrase.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018437. Carbonic_anhydrase_CA5_mt.
[Graphical view]

Gene3D

G3DSA:3.10.200.10. Euk_COanhd. 1 hit.

KO

K01672.

PANTHER

PTHR18952:SF25. Carbonic_anhydrase_CA5_mt. 1 hit.
PTHR18952. Euk_COanhd. 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.

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:	January 25, 2012
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program