Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P23589 (CAH5A_MOUSE)

Last modified January 19, 2010. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Carbonic anhydrase 5A, mitochondrial
    EC=4.2.1.1
Alternative name(s):
    Carbonic anhydrase VA
      Short name=CA-VA
    Carbonate dehydratase VA
      Short name=CA Y
Gene names
Name: Ca5a
Synonyms: Ca5, Car5, Car5a
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Hide | Top

Protein attributes

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

Hide | Top

General annotation (Comments)

Function

Reversible hydration of carbon dioxide.

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Zinc.

Subcellular location

Mitochondrion.

Tissue specificity

Liver.

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

Hide | Top

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processgluconeogenesis

Traceable author statement. Source: MGI

one-carbon metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrion Ref.2

Inferred from direct assay. Source: MGI

   Molecular functioncarbonate dehydratase activity

Inferred from direct assay. Source: MGI

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Sites

Metal binding1241Zinc; catalytic By similarity
Metal binding1261Zinc; catalytic By similarity
Metal binding1491Zinc; catalytic By similarity

Natural variations

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

Secondary structure

1 .............................................. 299
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P23589-1 [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

Hide | Top

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: 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]"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).
[5]"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: X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS).
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X51971 mRNA. Translation: CAA36233.1.
BC030174 mRNA. Translation: AAH30174.1.
IPIIPI00133663.
PIRS12579.
RefSeqNP_031634.2.
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[»]
SMRP23589. Positions 27-290.
ModBaseSearch...

Protein-protein interaction databases

STRINGP23589.

Proteomic databases

PRIDEP23589.

Genome annotation databases

EnsemblENSMUST00000057653; ENSMUSP00000060457; ENSMUSG00000025317; Mus musculus. [Genome view]
GeneID12352.
KEGGmmu:12352.
UCSCuc009nsf.1. mouse.

Organism-specific databases

CTD12352.
MGIMGI:101946. Car5a.

Phylogenomic databases

eggNOGroNOG11543.
HOGENOMHBG717384.
HOVERGENP23589.
InParanoidP23589.
OMASYDAASC.
OrthoDBEOG9GJ27G.
PhylomeDBP23589.

Enzyme and pathway databases

BRENDA4.2.1.1. 244.

Gene expression databases

ArrayExpressP23589.
BgeeP23589.
CleanExMM_CAR5A.
GenevestigatorP23589.
GermOnlineENSMUSG00000025317. Mus musculus.

Family and domain databases

InterProIPR001148. Carbonic_anhydrase_a-class_cat.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018437. Carbonic_anhydrase_CA5_mt.
[Graphical view]
Gene3DG3DSA:3.10.200.10. Euk_COanhd. 1 hit.
PANTHERPTHR18952:SF25. Carbonic_anhydrase_CA5_mt. 1 hit.
PTHR18952. Euk_COanhd. 1 hit.
PfamPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
PROSITEPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

BindingDBP23589.
NextBio281008.
SOURCESearch...

Hide | Top

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: January 19, 2010
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

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 and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents