SpermatogenesisOnline 1.0

Tag Content
SG ID
SG00008654 
UniProt Accession
Theoretical PI
6.97  
Molecular Weight
29366 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Ca3 
Gene Synonyms/Alias
Car3 
Protein Name
Carbonic anhydrase 3 
Protein Synonyms/Alias
EC=4.2.1.1 Carbonate dehydratase III; Carbonic anhydrase III;CA-III 
Organism
Mus musculus (Mouse) 
NCBI Taxonomy ID
10090 
Chromosome Location
chr:3;14863538-14872351;1
View in Ensembl genome browser  
Function in Stage
Uncertain 
Function in Cell Type
Uncertain 
Probability (GAS) of Function in Spermatogenesis
0.101528731 
The probability was calculated by GAS algorithm, ranging from 0 to 1. The closer it is to 1, the more possibly it functions in spermatogenesis.
Description
Temporarily unavailable 
Abstract of related literatures
1. A cDNA for the mouse carbonic anhydrase, CAIII, has been isolated from a lambda gt11 expression library. The cloned cDNA contains all of the coding region (777 bp) and both 5' untranslated (86-bp) and 3' untranslated (217-bp) sequences. The coding sequence shows 87% homology at the nucleotide level and 91% homology, when amino acid residues are compared, with human CAIII. Protein and mRNA analyses show that CAIII is present at low levels in cultured myoblasts and is abundant in adult skeletal muscle and in liver. The marked sex-related differences in CAIII distribution, described for rat liver, are not seen in the mouse. Restriction fragment length polymorphisms using TaqI and PstI are described which distinguish between Mus spretus and Mus musculus domesticus. PMID: [2496681] 

2. At least 14 distinct isozymes of carbonic anhydrase have been identified in mammals. These enzymes catalyze the hydration of carbon dioxide and are essential for regulation of cellular pH and carbon dioxide transport. Carbonic anhydrase III is highly expressed in certain tissues, including muscle and fat where it constitutes up to 25% of the soluble protein. We cloned a cDNA encoding mouse carbonic anhydrase III. This cDNA contains 1653 bp, consisting of 79 bp in the 5' UTR, a 780 bp open reading frame, and 794 bp of the 3' UTR, including two potential polyadenylation signals. Fluorescent in situ hybridization confirmed the existence of a single copy of the gene on chromosome 3. We then isolated the genomic DNA for mouse carbonic anhydrase III and analyzed its structure. The gene consists of seven exons and six introns which span 10.5 kb. The 5' flanking region of the genomic DNA is notable for a pyrimidine rich region consisting of two dinucleotide repeats containing 23 and 20 TC pairs separated by the same 15 bp spacer. PMID: [11255005] 

3. The National Institutes of Health's Mammalian Gene Collection (MGC) project was designed to generate and sequence a publicly accessible cDNA resource containing a complete open reading frame (ORF) for every human and mouse gene. The project initially used a random strategy to select clones from a large number of cDNA libraries from diverse tissues. Candidate clones were chosen based on 5'-EST sequences, and then fully sequenced to high accuracy and analyzed by algorithms developed for this project. Currently, more than 11,000 human and 10,000 mouse genes are represented in MGC by at least one clone with a full ORF. The random selection approach is now reaching a saturation point, and a transition to protocols targeted at the missing transcripts is now required to complete the mouse and human collections. Comparison of the sequence of the MGC clones to reference genome sequences reveals that most cDNA clones are of very high sequence quality, although it is likely that some cDNAs may carry missense variants as a consequence of experimental artifact, such as PCR, cloning, or reverse transcriptase errors. Recently, a rat cDNA component was added to the project, and ongoing frog (Xenopus) and zebrafish (Danio) cDNA projects were expanded to take advantage of the high-throughput MGC pipeline. PMID: [15489334] 

4. To achieve a better understanding of the biochemical basis of obesity, we have undertaken comparative analyses of adipose tissue of lean and obese mice. By two-dimensional gel analysis, carbonic anhydrase-III (CA III) has been identified as a major constituent of murine adipose tissue. Quantitative comparisons of CA III protein and mRNA levels indicate that this enzyme is expressed at lower levels in adipose tissue from animals that were either genetically obese or had experimentally induced obesity compared to levels in the corresponding lean controls. This decrease in CA III expression was unique to adipose tissue, since other CA III-containing organs and tissues did not show a change when lean and obese animals were compared. Additionally, levels of CA III in adipose tissue from obese animals responded to acute changes in energy balance of the animal. These results are discussed in light of possible metabolic roles for CA III. PMID: [1922100] 

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Function
Reversible hydration of carbon dioxide. 
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Subcellular Location
Cytoplasm. 
Tissue Specificity
Expressed at lower levels in adipose tissuefrom animals that were either genetically obese or hadexperimentally induced obesity. 
Gene Ontology
GO IDGO termEvidence
GO:0005737 C:cytoplasm IEA:UniProtKB-SubCell.
GO:0004089 F:carbonate dehydratase activity IEA:EC.
GO:0016151 F:nickel cation binding IDA:MGI.
GO:0008270 F:zinc ion binding IEA:InterPro.
GO:0006730 P:one-carbon metabolic process IEA:InterPro.
GO:0006979 P:response to oxidative stress IEA:Compara.
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Interpro
IPR001148;    Carbonic_anhydrase_a.
IPR023561;    Carbonic_anhydrase_a-class.
IPR018338;    Carbonic_anhydrase_a-class_CS.
IPR018441;    Carbonic_anhydrase_CA3.
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Pfam
PF00194;    Carb_anhydrase;    1.
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SMART
SM01057;    Carb_anhydrase;    1.
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PROSITE
PS00162;    ALPHA_CA_1;    1.
PS51144;    ALPHA_CA_2;    1.
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PRINTS
Created Date
18-Oct-2012 
Record Type
GAS predicted 
Sequence Annotation
INIT_MET      1      1       Removed (By similarity).
CHAIN         2    260       Carbonic anhydrase 3.
                             /FTId=PRO_0000077427.
REGION       64     67       Involved in proton transfer (By
                             similarity).
REGION      198    199       Substrate binding (By similarity).
ACT_SITE    127    127       By similarity.
METAL        94     94       Zinc; catalytic.
METAL        96     96       Zinc; catalytic.
METAL       119    119       Zinc; catalytic.
MOD_RES     182    182       S-glutathionyl cysteine (By similarity).
MOD_RES     187    187       S-glutathionyl cysteine (By similarity).
CONFLICT      9      9       S -> R (in Ref. 1; AAA37355).
CONFLICT     86     86       G -> R (in Ref. 1; AAA37355).
CONFLICT    126    126       K -> R (in Ref. 1; AAA37355).
CONFLICT    146    146       F -> L (in Ref. 1; AAA37355).
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Nucleotide Sequence
Length: 1067 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 260 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
UniProt
 Gene Symbol Ref Databases
EnamIntAct 
Other Protein-Protein interaction resources
String database  
View Microarray data
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