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P14141 (CAH3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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. A major participant in the liver response to oxidative stress.

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Zinc.

Enzyme regulation

Inhibited by acetazolamide By similarity.

Subcellular location

Cytoplasm.

Tissue specificity

Expressed in liver and muscle. Ref.5

Induction

Repressed by 3,3',4,4',5-pentachlorobiphenyl (PenCB) and 3-methylchlantherene (3MC). Ref.2 Ref.9

Post-translational modification

S-thiolated both by thiol-disulfide exchange with glutathione disulfide and by oxyradical-initiated S-thiolation with reduced glutathione.

S-glutathionylated in hepatocytes under oxidative stress.

Miscellaneous

Expressed at much higher levels in the adipocytes of lean Zucker rats than in obese Zucker rats. Expression is higher is the adipocytes of male Zucker rats than in female Zucker rats.

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_0000077429

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
Modified residue1871S-glutathionyl cysteine

Experimental info

Sequence conflict81A → G in AAA40846. Ref.1
Sequence conflict341H → HI AA sequence Ref.7
Sequence conflict571K → R AA sequence Ref.7
Sequence conflict1261K → DR AA sequence Ref.7
Sequence conflict130 – 1312FG → SE in AAA40846. Ref.1
Sequence conflict1351K → R AA sequence Ref.7
Sequence conflict189 – 1913DYW → QYP AA sequence Ref.7
Sequence conflict224 – 2252KL → NV in AAA40846. Ref.1
Sequence conflict225 – 2262LR → DE AA sequence Ref.7
Sequence conflict2301A → G AA sequence Ref.7

Secondary structure

................................................... 260
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14141 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: C3C7DA7DA8793F18

FASTA26029,431
        10         20         30         40         50         60 
MAKEWGYASH NGPEHWHELY PIAKGDNQSP IELHTKDIRH DPSLQPWSVS YDPGSAKTIL 

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

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

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

       250        260 
VGNWRPPQPI KGRVVRASFK 

« Hide

References

« Hide 'large scale' references
[1]"Characterisation of cDNA clones for rat muscle carbonic anhydrase III."
Kelly C.D., Carter N.D., Jeffery S., Edwards Y.H.
Biosci. Rep. 8:401-406(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Suppression of carbonic anhydrase III in rat liver by a dioxin-related toxic compound, coplanar polychlorinated biphenyl, 3,3',4,4',5-pentachlorobiphenyl."
Ikeda M., Ishii Y., Kato H., Akazawa D., Hatsumura M., Ishida T., Matsusue K., Yamada H., Oguri K.
Arch. Biochem. Biophys. 380:159-164(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
Strain: Wistar.
Tissue: Liver and Soleus muscle.
[3]"Crystal structure of S-glutathiolated carbonic anhydrase III."
Mallis R.J., Poland B.W., Chatterjee T.K., Fisher R.A., Darmawan S., Honzatko R.B., Thomas J.A.
FEBS Lett. 482:237-241(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ZINC ION AND GLUTATHIONE, GLUTATHIONYLATION AT CYS-182 AND CYS-187.
Tissue: Liver.
[4]"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: Prostate.
[5]"Carbonic anhydrase III in obese Zucker rats."
Lynch C.J., Brennan W.A. Jr., Vary T.C., Carter N., Dodgson S.J.
Am. J. Physiol. 264:E621-E630(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-45 AND 120-142, TISSUE SPECIFICITY.
Strain: Zucker.
[6]"Analyses of polypeptides in the liver of a novel mutant (LEC rats) to hereditary hepatitis and hepatoma by two-dimensional gel electrophoresis: identification of P29/6.8 as carbonic anhydrase III and triosephosphate isomerase."
Nagase T., Sugiyama T., Kawata S., Tarui S., Deutsch H.F., Taniguchi N.
Comp. Biochem. Physiol. 99B:193-201(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-33.
Tissue: Liver.
[7]"Identification of an abundant S-thiolated rat liver protein as carbonic anhydrase III; characterization of S-thiolation and dethiolation reactions."
Chai Y.-C., Jung C.-H., Lii C.-K., Ashraf S.S., Hendrich S., Wolf B., Sies H., Thomas J.A.
Arch. Biochem. Biophys. 284:270-278(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-35; 40-57; 68-76; 81-89; 114-135; 189-201 AND 225-239.
Tissue: Liver.
[8]Lubec G., Afjehi-Sadat L.
Submitted (DEC-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 113-125 AND 136-148, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Spinal cord.
[9]"Suppression of carbonic anhydrase III mRNA level by an aryl hydrocarbon receptor ligand in primary cultured hepatocytes of rat."
Ishii Y., Akazawa D., Aoki Y., Yamada H., Oguri K.
Biol. Pharm. Bull. 28:1087-1090(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M22413 mRNA. Translation: AAA40846.1.
AB030829 mRNA. Translation: BAB08111.1.
AB030830 mRNA. Translation: BAB20673.1.
AF037072 mRNA. Translation: AAB92558.1.
BC061980 mRNA. Translation: AAH61980.1.
PIRI52551.
RefSeqNP_062165.2. NM_019292.4.
XP_006232178.1. XM_006232116.1.
UniGeneRn.1647.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FLJX-ray1.80A2-260[»]
ProteinModelPortalP14141.
SMRP14141. Positions 2-260.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4569746.
STRING10116.ENSRNOP00000014177.

Chemistry

BindingDBP14141.

PTM databases

PhosphoSiteP14141.

Proteomic databases

PaxDbP14141.
PRIDEP14141.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000014180; ENSRNOP00000014177; ENSRNOG00000010079.
GeneID54232.
KEGGrno:54232.
UCSCRGD:2241. rat.

Organism-specific databases

CTD12350.
RGD2241. Ca3.

Phylogenomic databases

eggNOGCOG3338.
GeneTreeENSGT00750000117305.
HOGENOMHOG000112637.
HOVERGENHBG002837.
InParanoidP14141.
KOK01672.
OMAEAPFTHF.
OrthoDBEOG7WMCK7.
PhylomeDBP14141.
TreeFamTF316425.

Enzyme and pathway databases

BRENDA4.2.1.1. 5301.

Gene expression databases

GenevestigatorP14141.

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:SF29. PTHR18952:SF29. 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

EvolutionaryTraceP14141.
NextBio610666.
PROP14141.

Entry information

Entry nameCAH3_RAT
AccessionPrimary (citable) accession number: P14141
Secondary accession number(s): O54961, Q9QV77
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 134 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references