P14141 (CAH3_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	260 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. 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Lyase
PTM	Acetylation Disulfide bond Glutathionylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	one-carbon metabolic process Inferred from electronic annotation. Source: InterPro response to oxidative stress Inferred from mutant phenotype Ref.2. Source: RGD
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	carbonate dehydratase activity Traceable author statement Ref.2. Source: RGD nickel cation binding Inferred from electronic annotation. Source: Compara 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

Initiator methionine

1

1

Removed

Chain

2 – 260

259

Carbonic anhydrase 3

PRO_0000077429

Regions

Region

64 – 67

4

Involved in proton transfer By similarity

Region

198 – 199

2

Substrate binding By similarity

Sites

Active site

127

1

By similarity

Metal binding

94

1

Zinc; catalytic

Metal binding

96

1

Zinc; catalytic

Metal binding

119

1

Zinc; catalytic

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Modified residue

182

1

S-glutathionyl cysteine

Modified residue

187

1

S-glutathionyl cysteine

Experimental info

Sequence conflict

8

1

A → G in AAA40846. Ref.1

Sequence conflict

34

1

H → HI AA sequence Ref.7

Sequence conflict

57

1

K → R AA sequence Ref.7

Sequence conflict

126

1

K → DR AA sequence Ref.7

Sequence conflict

130 – 131

2

FG → SE in AAA40846. Ref.1

Sequence conflict

135

1

K → R AA sequence Ref.7

Sequence conflict

189 – 191

3

DYW → QYP AA sequence Ref.7

Sequence conflict

224 – 225

2

KL → NV in AAA40846. Ref.1

Sequence conflict

225 – 226

2

LR → DE AA sequence Ref.7

Sequence conflict

230

1

A → G AA sequence Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

260

Helix Strand Turn

Details...

Turn

9 – 11

3

Helix

13 – 18

6

Helix

21 – 24

4

Beta strand

25 – 27

3

Helix

35 – 37

3

Beta strand

38 – 40

3

Beta strand

47 – 50

4

Helix

53 – 55

3

Beta strand

56 – 61

6

Beta strand

66 – 70

5

Beta strand

73 – 81

9

Beta strand

88 – 97

10

Beta strand

106 – 109

4

Beta strand

115 – 123

9

Helix

125 – 127

3

Helix

130 – 133

4

Beta strand

139 – 151

13

Helix

154 – 162

9

Helix

163 – 166

4

Beta strand

172 – 174

3

Helix

180 – 183

4

Beta strand

190 – 195

6

Beta strand

206 – 213

8

Beta strand

215 – 217

3

Helix

219 – 225

7

Beta strand

229 – 231

3

Beta strand

255 – 258

4

Sequences

	Sequence		Length	Mass (Da)
	P14141 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: C3C7DA7DA8793F18	FASTA	260	29,431
	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

References

	« Hide 'large scale' referencesShow '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, S-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, 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.

IPI

IPI00230788.

PIR

I52551.

RefSeq

NP_062165.2. NM_019292.4.

UniGene

Rn.1647.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FLJ	X-ray	1.80	A	2-260	[»]

ProteinModelPortal

P14141.

SMR

P14141. Positions 2-260.

ModBase

Search...

Protein-protein interaction databases

STRING

10116.ENSRNOP00000014177.

PTM databases

PhosphoSite

P14141.

Proteomic databases

PaxDb

P14141.

PRIDE

P14141.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000014180; ENSRNOP00000014177; ENSRNOG00000010079.

GeneID

54232.

KEGG

rno:54232.

UCSC

RGD:2241. rat.

Organism-specific databases

CTD

12350.

RGD

2241. Ca3.

Phylogenomic databases

eggNOG

COG3338.

GeneTree

ENSGT00560000076828.

HOGENOM

HOG000112637.

HOVERGEN

HBG002837.

InParanoid

P14141.

KO

K01672.

OMA

CEECIVW.

OrthoDB

EOG4001JV.

Enzyme and pathway databases

BRENDA

4.2.1.1. 5301.

Gene expression databases

Genevestigator

P14141.

GermOnline

ENSRNOG00000010079. Rattus norvegicus.

Family and domain databases

Gene3D

3.10.200.10. 1 hit.

InterPro

IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018441. Carbonic_anhydrase_CA3.
[Graphical view]

PANTHER

PTHR18952. PTHR18952. 1 hit.
PTHR18952:SF29. PTHR18952:SF29. 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

P14141.

ChEMBL

CHEMBL4997.

EvolutionaryTrace

P14141.

NextBio

610666.

Entry information

Entry name

CAH3_RAT

Accession

Primary (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 3, 2013
This is version 124 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program