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P16015 (CAH3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 3

EC=4.2.1.1
Alternative name(s):
Carbonate dehydratase III
Carbonic anhydrase III
Short name=CA-III
Gene names
Name:Ca3
Synonyms:Car3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length260 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.

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Zinc By similarity.

Enzyme regulation

Inhibited by acetazolamide By similarity.

Subcellular location

Cytoplasm.

Tissue specificity

Expressed at lower levels in adipose tissue from animals that were either genetically obese or had experimentally induced obesity. Ref.4

Post-translational modification

S-glutathionylated in hepatocytes under oxidative stress By similarity.

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 260259Carbonic anhydrase 3
PRO_0000077427

Regions

Region64 – 674Involved in proton transfer By similarity
Region198 – 1992Substrate binding By similarity

Sites

Active site1271 By similarity
Metal binding941Zinc; catalytic
Metal binding961Zinc; catalytic
Metal binding1191Zinc; catalytic

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1821S-glutathionyl cysteine By similarity
Modified residue1871S-glutathionyl cysteine By similarity

Experimental info

Sequence conflict91S → R in AAA37355. Ref.1
Sequence conflict861G → R in AAA37355. Ref.1
Sequence conflict1261K → R in AAA37355. Ref.1
Sequence conflict1461F → L in AAA37355. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P16015 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F4E9FE69A3C324BB

FASTA26029,366
        10         20         30         40         50         60 
MAKEWGYASH NGPDHWHELY PIAKGDNQSP IELHTKDIKH DPSLQPWSAS YDPGSAKTIL 

        70         80         90        100        110        120 
NNGKTCRVVF DDTYDRSMLR GGPLSGPYRL RQFHLHWGSS DDHGSEHTVD GVKYAAELHL 

       130        140        150        160        170        180 
VHWNPKYNTF GEALKQPDGI AVVGIFLKIG REKGEFQILL DALDKIKTKG KEAPFTHFDP 

       190        200        210        220        230        240 
SCLFPACRDY WTYHGSFTTP PCEECIVWLL LKEPMTVSSD QMAKLRSLFS SAENEPPVPL 

       250        260 
VGNWRPPQPV KGRVVRASFK 

« Hide

References

« Hide 'large scale' references
[1]"Mouse carbonic anhydrase III: nucleotide sequence and expression studies."
Tweedie S., Edwards Y.
Biochem. Genet. 27:17-30(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Nucleotide sequence and structure of the mouse carbonic anhydrase III gene."
Kim G., Lee T.-H., Wynshaw-Boris A., Levine R.L.
Gene 265:37-44(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/SvJ.
[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].
Tissue: Liver.
[4]"Expression of CA III in rodent models of obesity."
Stanton L.W., Ponte P.A., Coleman R.T., Snyder M.A.
Mol. Endocrinol. 5:860-866(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 79-96, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M27796 mRNA. Translation: AAA37355.1.
AF294988 expand/collapse EMBL AC list , AF294983, AF294984, AF294985, AF294986, AF294987 Genomic DNA. Translation: AAG22029.1.
BC011129 mRNA. Translation: AAH11129.1.
CCDSCCDS17250.1.
PIRA43641.
RefSeqNP_031632.2. NM_007606.3.
UniGeneMm.300.

3D structure databases

ProteinModelPortalP16015.
SMRP16015. Positions 2-260.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198484. 1 interaction.
IntActP16015. 4 interactions.
MINTMINT-1869657.
STRING10090.ENSMUSP00000029076.

PTM databases

PhosphoSiteP16015.

2D gel databases

SWISS-2DPAGEP16015.

Proteomic databases

MaxQBP16015.
PaxDbP16015.
PRIDEP16015.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029076; ENSMUSP00000029076; ENSMUSG00000027559.
GeneID12350.
KEGGmmu:12350.
UCSCuc008oqs.1. mouse.

Organism-specific databases

CTD12350.
MGIMGI:88270. Car3.

Phylogenomic databases

eggNOGCOG3338.
GeneTreeENSGT00750000117305.
HOGENOMHOG000112637.
HOVERGENHBG002837.
InParanoidP16015.
KOK01672.
OMAEAPFTHF.
OrthoDBEOG7WMCK7.
PhylomeDBP16015.
TreeFamTF316425.

Gene expression databases

BgeeP16015.
CleanExMM_CAR3.
GenevestigatorP16015.

Family and domain databases

Gene3D3.10.200.10. 1 hit.
InterProIPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018441. Carbonic_anhydrase_CA3.
[Graphical view]
PANTHERPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF96. PTHR18952:SF96. 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

ChiTaRSCA3. mouse.
NextBio281000.
PROP16015.
SOURCESearch...

Entry information

Entry nameCAH3_MOUSE
AccessionPrimary (citable) accession number: P16015
Secondary accession number(s): Q9ERN8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 117 of the entry and version 3 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

MGD cross-references

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