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P14141

- CAH3_RAT

UniProt

P14141 - CAH3_RAT

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Protein

Carbonic anhydrase 3

Gene
Ca3
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Reversible hydration of carbon dioxide. A major participant in the liver response to oxidative stress.

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zinc.

Enzyme regulationi

Inhibited by acetazolamide By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi94 – 941Zinc; catalytic
Metal bindingi96 – 961Zinc; catalytic
Metal bindingi119 – 1191Zinc; catalytic
Active sitei127 – 1271 By similarity

GO - Molecular functioni

  1. carbonate dehydratase activity Source: RGD
  2. nickel cation binding Source: Ensembl
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. one-carbon metabolic process Source: InterPro
  2. response to ethanol Source: RGD
  3. response to oxidative stress Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi4.2.1.1. 5301.
ReactomeiREACT_199186. Reversible hydration of carbon dioxide.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase 3 (EC:4.2.1.1)
Alternative name(s):
Carbonate dehydratase III
Carbonic anhydrase III
Short name:
CA-III
Gene namesi
Name:Ca3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 2

Organism-specific databases

RGDi2241. Ca3.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 260259Carbonic anhydrase 3PRO_0000077429Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei182 – 1821S-glutathionyl cysteine
Modified residuei187 – 1871S-glutathionyl cysteine

Post-translational modificationi

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.

Keywords - PTMi

Acetylation, Disulfide bond, Glutathionylation

Proteomic databases

PaxDbiP14141.
PRIDEiP14141.

PTM databases

PhosphoSiteiP14141.

Expressioni

Tissue specificityi

Expressed in liver and muscle.1 Publication

Inductioni

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

Gene expression databases

GenevestigatoriP14141.

Interactioni

Protein-protein interaction databases

MINTiMINT-4569746.
STRINGi10116.ENSRNOP00000014177.

Structurei

Secondary structure

1
260
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni9 – 113
Helixi13 – 186
Helixi21 – 244
Beta strandi25 – 273
Helixi35 – 373
Beta strandi38 – 403
Beta strandi47 – 504
Helixi53 – 553
Beta strandi56 – 616
Beta strandi66 – 705
Beta strandi73 – 819
Beta strandi88 – 9710
Beta strandi106 – 1094
Beta strandi115 – 1239
Helixi125 – 1273
Helixi130 – 1334
Beta strandi139 – 15113
Helixi154 – 1629
Helixi163 – 1664
Beta strandi172 – 1743
Helixi180 – 1834
Beta strandi190 – 1956
Beta strandi206 – 2138
Beta strandi215 – 2173
Helixi219 – 2257
Beta strandi229 – 2313
Beta strandi255 – 2584

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FLJX-ray1.80A2-259[»]
ProteinModelPortaliP14141.
SMRiP14141. Positions 2-260.

Miscellaneous databases

EvolutionaryTraceiP14141.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni64 – 674Involved in proton transfer By similarity
Regioni198 – 1992Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3338.
GeneTreeiENSGT00750000117305.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP14141.
KOiK01672.
OMAiEAPFTHF.
OrthoDBiEOG7WMCK7.
PhylomeDBiP14141.
TreeFamiTF316425.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018441. Carbonic_anhydrase_CA3.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF96. PTHR18952:SF96. 1 hit.
PfamiPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTiSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMiSSF51069. SSF51069. 1 hit.
PROSITEiPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14141-1 [UniParc]FASTAAdd to Basket

« Hide

MAKEWGYASH NGPEHWHELY PIAKGDNQSP IELHTKDIRH DPSLQPWSVS    50
YDPGSAKTIL NNGKTCRVVF DDTFDRSMLR GGPLSGPYRL RQFHLHWGSS 100
DDHGSEHTVD GVKYAAELHL VHWNPKYNTF GEALKQPDGI AVVGIFLKIG 150
REKGEFQILL DALDKIKTKG KEAPFNHFDP SCLFPACRDY WTYHGSFTTP 200
PCEECIVWLL LKEPMTVSSD QMAKLRSLFA SAENEPPVPL VGNWRPPQPI 250
KGRVVRASFK 260
Length:260
Mass (Da):29,431
Last modified:January 23, 2007 - v3
Checksum:iC3C7DA7DA8793F18
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81A → G in AAA40846. 1 Publication
Sequence conflicti34 – 341H → HI AA sequence 1 Publication
Sequence conflicti57 – 571K → R AA sequence 1 Publication
Sequence conflicti126 – 1261K → DR AA sequence 1 Publication
Sequence conflicti130 – 1312FG → SE in AAA40846. 1 Publication
Sequence conflicti135 – 1351K → R AA sequence 1 Publication
Sequence conflicti189 – 1913DYW → QYP AA sequence 1 Publication
Sequence conflicti224 – 2252KL → NV in AAA40846. 1 Publication
Sequence conflicti225 – 2262LR → DE AA sequence 1 Publication
Sequence conflicti230 – 2301A → G AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiI52551.
RefSeqiNP_062165.2. NM_019292.4.
XP_006232178.1. XM_006232116.1.
UniGeneiRn.1647.

Genome annotation databases

EnsembliENSRNOT00000014180; ENSRNOP00000014177; ENSRNOG00000010079.
GeneIDi54232.
KEGGirno:54232.
UCSCiRGD:2241. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi I52551.
RefSeqi NP_062165.2. NM_019292.4.
XP_006232178.1. XM_006232116.1.
UniGenei Rn.1647.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FLJ X-ray 1.80 A 2-259 [» ]
ProteinModelPortali P14141.
SMRi P14141. Positions 2-260.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-4569746.
STRINGi 10116.ENSRNOP00000014177.

Chemistry

BindingDBi P14141.

PTM databases

PhosphoSitei P14141.

Proteomic databases

PaxDbi P14141.
PRIDEi P14141.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000014180 ; ENSRNOP00000014177 ; ENSRNOG00000010079 .
GeneIDi 54232.
KEGGi rno:54232.
UCSCi RGD:2241. rat.

Organism-specific databases

CTDi 12350.
RGDi 2241. Ca3.

Phylogenomic databases

eggNOGi COG3338.
GeneTreei ENSGT00750000117305.
HOGENOMi HOG000112637.
HOVERGENi HBG002837.
InParanoidi P14141.
KOi K01672.
OMAi EAPFTHF.
OrthoDBi EOG7WMCK7.
PhylomeDBi P14141.
TreeFami TF316425.

Enzyme and pathway databases

BRENDAi 4.2.1.1. 5301.
Reactomei REACT_199186. Reversible hydration of carbon dioxide.

Miscellaneous databases

EvolutionaryTracei P14141.
NextBioi 610666.
PROi P14141.

Gene expression databases

Genevestigatori P14141.

Family and domain databases

Gene3Di 3.10.200.10. 1 hit.
InterProi IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018441. Carbonic_anhydrase_CA3.
[Graphical view ]
PANTHERi PTHR18952. PTHR18952. 1 hit.
PTHR18952:SF96. PTHR18952:SF96. 1 hit.
Pfami PF00194. Carb_anhydrase. 1 hit.
[Graphical view ]
SMARTi SM01057. Carb_anhydrase. 1 hit.
[Graphical view ]
SUPFAMi SSF51069. SSF51069. 1 hit.
PROSITEi PS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiCAH3_RAT
AccessioniPrimary (citable) accession number: P14141
Secondary accession number(s): O54961, Q9QV77
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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