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Protein

Carbonic anhydrase 3

Gene

Ca3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Reversible hydration of carbon dioxide.

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zn2+By similarity

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 – 1271By similarity

GO - Molecular functioni

  • carbonate dehydratase activity Source: UniProtKB-EC
  • nickel cation binding Source: MGI
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi4.2.1.1. 3474.
ReactomeiREACT_327358. 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
Synonyms:Car3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:88270. Car3.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 260259Carbonic anhydrase 3PRO_0000077427Add
BLAST

Amino acid modifications

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

Post-translational modificationi

S-glutathionylated in hepatocytes under oxidative stress.By similarity

Keywords - PTMi

Acetylation, Glutathionylation

Proteomic databases

MaxQBiP16015.
PaxDbiP16015.
PRIDEiP16015.

2D gel databases

SWISS-2DPAGEP16015.

PTM databases

PhosphoSiteiP16015.

Expressioni

Tissue specificityi

Expressed at lower levels in adipose tissue from animals that were either genetically obese or had experimentally induced obesity.1 Publication

Gene expression databases

BgeeiP16015.
CleanExiMM_CAR3.
GenevisibleiP16015. MM.

Interactioni

Protein-protein interaction databases

BioGridi198484. 1 interaction.
IntActiP16015. 4 interactions.
MINTiMINT-1869657.
STRINGi10090.ENSMUSP00000029076.

Structurei

3D structure databases

ProteinModelPortaliP16015.
SMRiP16015. Positions 2-260.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni64 – 674Involved in proton transferBy similarity
Regioni198 – 1992Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated

Phylogenomic databases

eggNOGiCOG3338.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP16015.
KOiK01672.
OMAiEAPFTHF.
OrthoDBiEOG7WMCK7.
PhylomeDBiP16015.
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.

P16015-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKEWGYASH NGPDHWHELY PIAKGDNQSP IELHTKDIKH DPSLQPWSAS
60 70 80 90 100
YDPGSAKTIL NNGKTCRVVF DDTYDRSMLR GGPLSGPYRL RQFHLHWGSS
110 120 130 140 150
DDHGSEHTVD GVKYAAELHL VHWNPKYNTF GEALKQPDGI AVVGIFLKIG
160 170 180 190 200
REKGEFQILL DALDKIKTKG KEAPFTHFDP SCLFPACRDY WTYHGSFTTP
210 220 230 240 250
PCEECIVWLL LKEPMTVSSD QMAKLRSLFS SAENEPPVPL VGNWRPPQPV
260
KGRVVRASFK
Length:260
Mass (Da):29,366
Last modified:January 23, 2007 - v3
Checksum:iF4E9FE69A3C324BB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91S → R in AAA37355 (PubMed:2496681).Curated
Sequence conflicti86 – 861G → R in AAA37355 (PubMed:2496681).Curated
Sequence conflicti126 – 1261K → R in AAA37355 (PubMed:2496681).Curated
Sequence conflicti146 – 1461F → L in AAA37355 (PubMed:2496681).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27796 mRNA. Translation: AAA37355.1.
AF294988
, AF294983, AF294984, AF294985, AF294986, AF294987 Genomic DNA. Translation: AAG22029.1.
BC011129 mRNA. Translation: AAH11129.1.
CCDSiCCDS17250.1.
PIRiA43641.
RefSeqiNP_031632.2. NM_007606.3.
UniGeneiMm.300.

Genome annotation databases

EnsembliENSMUST00000029076; ENSMUSP00000029076; ENSMUSG00000027559.
GeneIDi12350.
KEGGimmu:12350.
UCSCiuc008oqs.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27796 mRNA. Translation: AAA37355.1.
AF294988
, AF294983, AF294984, AF294985, AF294986, AF294987 Genomic DNA. Translation: AAG22029.1.
BC011129 mRNA. Translation: AAH11129.1.
CCDSiCCDS17250.1.
PIRiA43641.
RefSeqiNP_031632.2. NM_007606.3.
UniGeneiMm.300.

3D structure databases

ProteinModelPortaliP16015.
SMRiP16015. Positions 2-260.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198484. 1 interaction.
IntActiP16015. 4 interactions.
MINTiMINT-1869657.
STRINGi10090.ENSMUSP00000029076.

PTM databases

PhosphoSiteiP16015.

2D gel databases

SWISS-2DPAGEP16015.

Proteomic databases

MaxQBiP16015.
PaxDbiP16015.
PRIDEiP16015.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029076; ENSMUSP00000029076; ENSMUSG00000027559.
GeneIDi12350.
KEGGimmu:12350.
UCSCiuc008oqs.1. mouse.

Organism-specific databases

CTDi12350.
MGIiMGI:88270. Car3.

Phylogenomic databases

eggNOGiCOG3338.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP16015.
KOiK01672.
OMAiEAPFTHF.
OrthoDBiEOG7WMCK7.
PhylomeDBiP16015.
TreeFamiTF316425.

Enzyme and pathway databases

BRENDAi4.2.1.1. 3474.
ReactomeiREACT_327358. Reversible hydration of carbon dioxide.

Miscellaneous databases

NextBioi281000.
PROiP16015.
SOURCEiSearch...

Gene expression databases

BgeeiP16015.
CleanExiMM_CAR3.
GenevisibleiP16015. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: PROTEIN SEQUENCE OF 79-96, TISSUE SPECIFICITY.

Entry informationi

Entry nameiCAH3_MOUSE
AccessioniPrimary (citable) accession number: P16015
Secondary accession number(s): Q9ERN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.