SM/J mice carry a number of rare polymorphic alleles and are often matched to other strains for quantitative trait locus analysis. These mice are susceptible to diet-induced obesity and diet-induced atherosclerosis. SM/J mice exhibit a hyperresponsiveness to B cell mitogens. Small in size at birth and through weaning, SM/J mice attain a normal body weight as they age.Read More +
SM/J mice carry a number of rare polymorphic alleles and are often matched to LG/J (Stock No. 000675), A/J (Stock No. 000646) or NZB/BINJ (Stock No. 000684) for quantitative trait locus analysis. These mice are susceptible to diet-induced obesity and diet-induced atherosclerosis. SM/J mice exhibit a hyperresponsiveness to B cell mitogens (Clark et al. 1981, Engel et al. 1981). A point mutation in Neu1 is responsible for a partial deficiency of lysosomal neuraminadase and may explain the altered immune response (Rottier et al. 1998). Small in size at birth and through weaning, SM/J mice attain a normal body weight as they age.
SM/J, created by MacArthur in 1939 from crosses involving 7 inbred strains - among them DBA - followed by inbreeding with selection for small body size, is segregating white-bellied agouti (Aw) vs. nonagouti (a) at the agouti locus.
|Allele Name||mutation 1|
|Allele Synonym(s)||Il3raA/J; Il3ran|
|Gene Symbol and Name||Il3ra, interleukin 3 receptor, alpha chain|
|Strain of Origin||multiple strains|
|General Note||This allele has been identified in A/J, A/WySnJ, A/HeJ, C58/J, RF/J, AKR/J, SM/J, BUB/BnJ, CE/J, and NZB/B1NJ. see J:24918.|
|Molecular Note||Sequence analysis revealed A/J mice lack the sequence corresponding to exon 8, which encodes 10 amino acid residues in the extracellular domain. Aberrant splicing was due to a 5 base pair deletion at the branch point in intron 7.|
|Allele Name||a variant|
|Allele Type||Not Applicable|
|Gene Symbol and Name||Neu1, neuraminidase 1|
|Strain of Origin||SM/J|
|General Note||Low activity determined by the Neu1a allele occurs in the SM/J inbred strain and in wild mice in the area of Ann Arbor, Michigan; all other inbred strains have high activity determined by the Neu1b allele. Heterozygotes have intermediate activity. Neuraminidase removes extra sialic acid residues from these enzymes. The defective neuraminidase of Neu1a> mice, by failing to remove the extra sialic acid, changes their electrophoretic mobility (J:6480). Level of activity of neuraminidase in activated T lymphocytes is also depressed in Neu1a/Neu1a mice (J:7976).|
|Molecular Note||Sequencing of the a allele revealed 5 nucleotide differences compared to the b allele. These changes alter the amino acid residues 11, 15, 17, 19 and 209 of the encoded protein from Gly, Tyr, Ala, Arg and Leu to Arg, Cys, Val, Cys and Ile, respectively. This encoded protein has 85-95% less activity than the protein encoded by the b allele as demonstrated in an in vitro assay. Further studies attributed most of the activity loss to the variation at position 209. Later studies detected 4 silent mutations in the signal peptide sequence and 2 mutations (c.-240C>T and c.-519G>A) in the promoter region. The mutation c.-519G>A creates a novel binding site for Nkx3-1 and Nkx3-2. In vitro assays demonstrated that binding of Nkx3-2 specifically represses promoter driven expression.|
|Allele Type||Spontaneous (Not Specified)|
|Gene Symbol and Name||Gpr84, G protein-coupled receptor 84|
|Strain of Origin||multiple strains|
|Molecular Note||This spontaneously arising frameshift deletion is located in exon 2 at position 103308576 bp (NCBI Build 37) and results in a premature stop codon. The mutation is predicted to result in a truncated protein lacking the transmembrane domains 4-7. The inbred strains BDP/J, DBA/1J, DBA/2J, I/LnJ, FVB/NJ, LG/J, MRL/MpJ, NODShi/LtJ, NOR/LtJ, P/J, PL/J, SKHIN/Sprd, SJL/J, SM/J are homozygous for the deletion. The allele is segregating in the outbred stocks ICR and CD-1.|
|Allele Name||mutation 1|
|Allele Type||Spontaneous (Not Applicable)|
|Gene Symbol and Name||Ogg1, 8-oxoguanine DNA-glycosylase 1|
|Strain of Origin||various|
|Molecular Note||A guanine to adenine change at the fifty-ninth nucleotide in exon 7 resulted in a substitution of the 336th amino acid, arginine, by histidine (R336H) in a putative nuclear localization signal. The mutation led to disruption of the nuclear localization of the enzyme, although the activity remained normal.|
When using the SM/J mouse strain in a publication, please include JAX stock #000687 in your Materials and Methods section.
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