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Protein

Carbonic anhydrase 3

Gene

Ca3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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

Zn2+1 Publication

Enzyme regulationi

Inhibited by acetazolamide.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi94Zinc; catalytic1 Publication1
Metal bindingi96Zinc; catalytic1 Publication1
Metal bindingi119Zinc; catalytic1 Publication1
Active sitei127By similarity1

GO - Molecular functioni

  • carbonate dehydratase activity Source: RGD
  • nickel cation binding Source: Ensembl
  • phosphatase activity Source: CACAO
  • zinc ion binding Source: InterPro

GO - Biological processi

  • one-carbon metabolic process Source: InterPro
  • response to ethanol Source: RGD
  • 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.
ReactomeiR-RNO-1475029. 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
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi2241. Ca3.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000774292 – 260Carbonic anhydrase 3Add BLAST259

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei29PhosphoserineCombined sources1
Modified residuei43PhosphoserineCombined sources1
Modified residuei48PhosphoserineCombined sources1
Modified residuei50PhosphoserineCombined sources1
Modified residuei55PhosphoserineCombined sources1
Modified residuei73PhosphothreonineCombined sources1
Modified residuei127PhosphotyrosineCombined sources1
Modified residuei129PhosphothreonineCombined sources1
Modified residuei182S-glutathionyl cysteine1 Publication1
Modified residuei187S-glutathionyl cysteine1 Publication1
Modified residuei216PhosphothreonineCombined sources1
Modified residuei219PhosphoserineCombined sources1

Post-translational modificationi

S-thiolated both by thiol-disulfide exchange with glutathione disulfide and by oxyradical-initiated S-thiolation with reduced glutathione.1 Publication
S-glutathionylated in hepatocytes under oxidative stress.1 Publication

Keywords - PTMi

Acetylation, Disulfide bond, Glutathionylation, Phosphoprotein

Proteomic databases

PaxDbiP14141.
PRIDEiP14141.

PTM databases

iPTMnetiP14141.
PhosphoSitePlusiP14141.

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

BgeeiENSRNOG00000010079.
GenevisibleiP14141. RN.

Interactioni

Protein-protein interaction databases

MINTiMINT-4569746.
STRINGi10116.ENSRNOP00000014177.

Structurei

Secondary structure

1260
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni9 – 11Combined sources3
Helixi13 – 18Combined sources6
Helixi21 – 24Combined sources4
Beta strandi25 – 27Combined sources3
Helixi35 – 37Combined sources3
Beta strandi38 – 40Combined sources3
Beta strandi47 – 50Combined sources4
Helixi53 – 55Combined sources3
Beta strandi56 – 61Combined sources6
Beta strandi66 – 70Combined sources5
Beta strandi73 – 81Combined sources9
Beta strandi88 – 97Combined sources10
Beta strandi106 – 109Combined sources4
Beta strandi115 – 123Combined sources9
Helixi125 – 127Combined sources3
Helixi130 – 133Combined sources4
Beta strandi139 – 151Combined sources13
Helixi154 – 162Combined sources9
Helixi163 – 166Combined sources4
Beta strandi172 – 174Combined sources3
Helixi180 – 183Combined sources4
Beta strandi190 – 195Combined sources6
Beta strandi206 – 213Combined sources8
Beta strandi215 – 217Combined sources3
Helixi219 – 225Combined sources7
Beta strandi229 – 231Combined sources3
Beta strandi255 – 258Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FLJX-ray1.80A2-259[»]
ProteinModelPortaliP14141.
SMRiP14141.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14141.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 259Alpha-carbonic anhydrasePROSITE-ProRule annotationAdd BLAST257

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni64 – 67Involved in proton transferBy similarity4
Regioni198 – 199Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated
Contains 1 alpha-carbonic anhydrase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP14141.
KOiK01672.
OMAiDISHDPS.
OrthoDBiEOG091G0XFM.
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:SF127. PTHR18952:SF127. 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

        10         20         30         40         50
MAKEWGYASH NGPEHWHELY PIAKGDNQSP IELHTKDIRH DPSLQPWSVS
60 70 80 90 100
YDPGSAKTIL NNGKTCRVVF DDTFDRSMLR GGPLSGPYRL RQFHLHWGSS
110 120 130 140 150
DDHGSEHTVD GVKYAAELHL VHWNPKYNTF GEALKQPDGI AVVGIFLKIG
160 170 180 190 200
REKGEFQILL DALDKIKTKG KEAPFNHFDP SCLFPACRDY WTYHGSFTTP
210 220 230 240 250
PCEECIVWLL LKEPMTVSSD QMAKLRSLFA SAENEPPVPL VGNWRPPQPI
260
KGRVVRASFK
Length:260
Mass (Da):29,431
Last modified:January 23, 2007 - v3
Checksum:iC3C7DA7DA8793F18
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti8A → G in AAA40846 (PubMed:2852973).Curated1
Sequence conflicti34H → HI AA sequence (PubMed:1899179).Curated1
Sequence conflicti57K → R AA sequence (PubMed:1899179).Curated1
Sequence conflicti126K → DR AA sequence (PubMed:1899179).Curated1
Sequence conflicti130 – 131FG → SE in AAA40846 (PubMed:2852973).Curated2
Sequence conflicti135K → R AA sequence (PubMed:1899179).Curated1
Sequence conflicti189 – 191DYW → QYP AA sequence (PubMed:1899179).Curated3
Sequence conflicti224 – 225KL → NV in AAA40846 (PubMed:2852973).Curated2
Sequence conflicti225 – 226LR → DE AA sequence (PubMed:1899179).Curated2
Sequence conflicti230A → G AA sequence (PubMed:1899179).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FLJX-ray1.80A2-259[»]
ProteinModelPortaliP14141.
SMRiP14141.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4569746.
STRINGi10116.ENSRNOP00000014177.

PTM databases

iPTMnetiP14141.
PhosphoSitePlusiP14141.

Proteomic databases

PaxDbiP14141.
PRIDEiP14141.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi12350.
RGDi2241. Ca3.

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP14141.
KOiK01672.
OMAiDISHDPS.
OrthoDBiEOG091G0XFM.
PhylomeDBiP14141.
TreeFamiTF316425.

Enzyme and pathway databases

BRENDAi4.2.1.1. 5301.
ReactomeiR-RNO-1475029. Reversible hydration of carbon dioxide.

Miscellaneous databases

EvolutionaryTraceiP14141.
PROiP14141.

Gene expression databases

BgeeiENSRNOG00000010079.
GenevisibleiP14141. RN.

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:SF127. PTHR18952:SF127. 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]
ProtoNetiSearch...

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: November 2, 2016
This is version 158 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.