SpermatogenesisOnline 1.0

Tag Content
SG ID
SG00021429 
UniProt Accession
Theoretical PI
6.71  
Molecular Weight
57318 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Amy2 
Gene Synonyms/Alias
Amy2a 
Protein Name
Pancreatic alpha-amylase 
Protein Synonyms/Alias
PAEC=3.2.1.1 1,4-alpha-D-glucan glucanohydrolase;Flags: Precursor 
Organism
Mus musculus (Mouse) 
NCBI Taxonomy ID
10090 
Chromosome Location
chr:3;113052094-113061755;-1
View in Ensembl genome browser  
Function in Stage
Uncertain 
Function in Cell Type
Uncertain 
Probability (GAS) of Function in Spermatogenesis
0.083692533 
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. We have determined the nucleotide sequence of two different mouse alpha-amylase mRNAs, one found in the pancreas and the other in the salivary gland. The 1577 and 1659 nucleotide mRNAs from pancreas and salivary gland, respectively are the major alpha-amylase species which accumulate in each tissue. Differences in mRNA length are primarily in the 5' noncoding regions. Comparable portions of the mRNAs are 89% homologous. The mRNA sequences predict alpha-amylase precursor proteins of 508 and 511 amino acid residues, accounting for nearly the entire coding capacity of the mRNAs; differences in protein length occur as a result of a nine nucleotide segment present within the translated portion of salivary gland, but not pancreas, mRNA. The lengths and amino acid compositions of the predicted proteins concur with those determined empirically by others. These proteins differ 12% in amino acid sequence, explaining previously observed differences in net charge and antigenic properties. Finally, translation of the salivary gland alpha-amylase mRNA is not initiated at the AUG codon nearest the 5' terminus since that codon is almost immediately followed by the termination triplet UAA. This observation may have implications for the mechanism of translation initiation in eucaroytes. PMID: [6157477] 

2. The number of active Amy-2 genes has been estimated in strain CE/J mice which produce four distinct electrophoretic forms of alpha-amylase in their pancreas. cDNA cloning and DNA sequence analysis discloses five distinct mRNA sequences which differ by approximately 1% of their nucleotides. Two of these mRNAs specify the same protein. Changes in the nucleotide sequences result in amino acid replacements that alter the net charges of the deduced proteins. This has allowed a tentative assignment of individual mRNAs to isozymes detected by electrophoresis. Quantitative Southern blot hybridization using a DNA probe specific for the first exon of Amy-2 reveals the presence of greater than 10 Amy-2 related sequences per haploid CE/J genome. Models which could account for the mouse strain-specific differences with respect to the number of pancreatic alpha-amylase isozymes and their variable but genetically determined quantitative ratios are discussed. PMID: [6098446] 

3. This study describes comprehensive polling of transcription start and termination sites and analysis of previously unidentified full-length complementary DNAs derived from the mouse genome. We identify the 5' and 3' boundaries of 181,047 transcripts with extensive variation in transcripts arising from alternative promoter usage, splicing, and polyadenylation. There are 16,247 new mouse protein-coding transcripts, including 5154 encoding previously unidentified proteins. Genomic mapping of the transcriptome reveals transcriptional forests, with overlapping transcription on both strands, separated by deserts in which few transcripts are observed. The data provide a comprehensive platform for the comparative analysis of mammalian transcriptional regulation in differentiation and development. PMID: [16141072] 

4. 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] 


6. Several members of the Amy-2 alpha-amylase multigene family from the CE/J strain of mouse have been cloned in cosmid vectors. Structural analysis of these recombinants reveals that the cloned Amy-2 copies contain tandem 5' termini. The duplicated 5'-terminal elements, which lie upstream from the Amy-2 cap site, are separated from their Amy-2 homologues by about 8000 bases. The orientation of these 5' orphons is the same as that of Amy-2. Gene titration and cloning experiments suggest that at least four of the approximately 15 Amy-2 copies present in the CE/J genome contain 5' orphon elements. The extent of sequence homology between 5' orphons and their gene homologues has been determined by DNA sequence analysis. All the orphons are identical and contain the entire 185 base-pairs of the first exon, 49 base-pairs of the first intron and more than 400 base-pairs of the Amy-2 5' flanking region. Intron and flanking-region sequences of the orphons differ by about 20% from their Amy-2 counterparts, and the exon by about 8%. The TATA box and the cap site are conserved, while the ATG translation initiation signal is mutated to ATA in the orphon. No transcription initiation has been detected at the orphon cap site using run-off transcription in isolated pancreatic nuclei in vitro. PMID: [2987507] 

7. The regulatory properties of mouse pancreatic amylase genes include exclusive expression in the acinar cells of the pancreas and dependence on insulin and glucocorticoids for maximal expression. We have characterized a murine pancreatic amylase gene, Amy-2.2y, whose promoter sequence is 30% divergent from those of previously sequenced amylase genes. To localize sequences required for tissue-specific and hormone-dependent activation, we established two lines of transgenic mice. The first line contained a single copy of the complete Amy-2.2y gene as well as 9 kilobases of 5'-flanking sequence and 5 kilobases of 3'-flanking sequence. The second line carried a minigene which included 208 base pairs of 5'-flanking sequence and 300 base pairs of 3'-flanking sequence. In both lines the transgene was expressed at high levels exclusively in the pancreas. Both constructs were dependent on insulin and induced by dexamethasone. Thus, the transferred genes contained the sequences required for tissue-specific and hormonally regulated expression. PMID: [2436036] 

8. The two isozymes of pancreatic amylase in mouse strain YBR/Ki are encoded by closely linked genes which are independently regulated. We have isolated these two pancreatic amylase genes, Amy-2.1 and Amy-2.2, from a cosmid library of YBR/Ki genomic DNA and compared the nucleotide sequences of coding regions with the amino acid sequences of the protein isozymes. Transcripts of both genes were also isolated from a pancreatic cDNA library and partially sequenced. The results demonstrate that Amy-2.1 encodes the A1 isozyme of YBR/Ki pancreatic amylase, while Amy- 2.2 encodes the insulin-dependent B1 isozyme. Similarities of restriction maps and nucleotide sequences suggest that Amy-2.1 is closely related to the active Amy-2a gene previously isolated from strain A/J (Schibler, U., Pittet, A.-C., Young, R. A., Hagenbüchle, O., Tosi, M., Gellman, S., and Wellauer, P. K. (1982) J. Mol. Biol. 155, 247-266). Expression of Amy-2.2 may be limited to strain YBR/Ki. The inactive Amy-X gene from A/J (Schibler, U., Pittet, A.-C., Young, R. A., Hagenbüchle, O., Tosi, M., Gellman, S., and Wellauer, P. K. (1982) J. Mol. Biol. 155, 247-266) is apparently a null allele of Amy-2.2. An additional amylase gene from YBR/Ki has been identified as a pancreatic amylase pseudogene which diverged between sixteen and thirty-two million years ago. The pancreatic amylase subfamily in strain YBR/Ki thus consists of two active genes and one pseudogene. The low rate of amylase production in YBR/Ki pancreas, relative to that of other inbred strains, can be accounted for by the lower number of gene copies in this strain. Comparison of pancreatic amylase genes from different inbred strains provides evidence for several duplication and deletion events during the recent evolution of this chromosome region. PMID: [2414282] 


10. The genetic determinants of pancreatic amylase expression in YBR mice differ in two respects from those of other inbred strains. First, there are two nonallelic amylase isozymes present in YBR pancreas, while most mouse strains express a single pancreatic amylase protein. In addition, the in vivo rate of total pancreatic amylase synthesis is 50% of that in other strains. Both these traits are determined by genetic sites in the region of the Amy-2 locus on mouse chromosome 3. To determine the molecular basis for the presence of two isozymes in this strain, we have compared portions of their amino acid sequences. Two differences between isozymes A1 and B1 were identified among the 77 residues compared. This result demonstrates that two distinct amylase genes are expressed in YBR pancreas. PMID: [6180955] 

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Function
 
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Subcellular Location
Secreted, extracellular space. 
Tissue Specificity
 
Gene Ontology
GO IDGO termEvidence
GO:0005615 C:extracellular space ISS:UniProtKB.
GO:0004556 F:alpha-amylase activity ISS:UniProtKB.
GO:0005509 F:calcium ion binding ISS:UniProtKB.
GO:0031404 F:chloride ion binding ISS:UniProtKB.
GO:0016052 P:carbohydrate catabolic process ISS:UniProtKB.
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Interpro
IPR006048;    A-amylase_b_C.
IPR006046;    Alpha_amylase.
IPR015902;    Glyco_hydro_13.
IPR013780;    Glyco_hydro_13_b.
IPR006047;    Glyco_hydro_13_cat_dom.
IPR006589;    Glyco_hydro_13_sub_cat_dom.
IPR013781;    Glyco_hydro_catalytic_dom.
IPR017853;    Glycoside_hydrolase_SF.
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Pfam
PF00128;    Alpha-amylase;    1.
PF02806;    Alpha-amylase_C;    1.
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SMART
SM00642;    Aamy;    1.
SM00632;    Aamy_C;    1.
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PROSITE
PRINTS
PR00110;    ALPHAAMYLASE.;   
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Created Date
18-Oct-2012 
Record Type
GAS predicted 
Sequence Annotation
SIGNAL        1     15
CHAIN        16    508       Pancreatic alpha-amylase.
                             /FTId=PRO_0000001398.
ACT_SITE    209    209       Nucleophile (By similarity).
ACT_SITE    245    245       Proton donor (By similarity).
METAL       115    115       Calcium (By similarity).
METAL       170    170       Calcium; via carbonyl oxygen (By
                             similarity).
METAL       179    179       Calcium (By similarity).
METAL       213    213       Calcium; via carbonyl oxygen (By
                             similarity).
BINDING     207    207       Chloride (By similarity).
BINDING     310    310       Chloride (By similarity).
BINDING     349    349       Chloride (By similarity).
SITE        312    312       Transition state stabilizer (By
                             similarity).
MOD_RES      16     16       Pyrrolidone carboxylic acid.
DISULFID     43    101       By similarity.
DISULFID     85    130       By similarity.
DISULFID    156    172       By similarity.
DISULFID    390    396       By similarity.
DISULFID    462    474       By similarity.
VARIANT      64     64       V -> I (in A1, B(C) and AMY-2.2Y).
VARIANT      66     66       V -> I (in AMY-2.2Y).
VARIANT     120    120       A -> S (in A1, B(A) and B(C)).
VARIANT     161    161       D -> S (in A1, B(A) and B(C); requires 2
                             nucleotide substitutions).
VARIANT     174    174       L -> V (in A1 and B(C)).
VARIANT     175    175       T -> S (in B(A)).
VARIANT     254    254       I -> V (in A1 and B(C)).
VARIANT     270    272       YGA -> FGV (in A1 and B(C)).
VARIANT     298    298       L -> M (in A1, B(A) and B(C)).
VARIANT     322    322       S -> A (in B(A)).
VARIANT     419    419       S -> A (in B1).
VARIANT     450    450       A -> E (in B(C)).
CONFLICT     70     70       S -> T (in Ref. 5; AAA37228).
CONFLICT     85     85       C -> S (in Ref. 5; AAA37228).
CONFLICT    217    217       G -> R (in Ref. 1; CAA24098 and 2;
                             CAA26413/CAA26414/CAA26415).
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Nucleotide Sequence
Length: 1579 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 508 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
UniProt
 Gene Symbol Ref Databases
Other Protein-Protein interaction resources
String database  
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