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ARS Home » Northeast Area » Beltsville, Maryland (BARC) » Beltsville Agricultural Research Center » Animal Genomics and Improvement Laboratory » Research » Publications at this Location » Publication #303488

Title: The hunt for a functional mutation affecting conformation and calving traits on chromosome 18 in Holstein cattle

Author
item Cole, John
item Hutchison, Jana
item Null, Daniel
item Vanraden, Paul
item Liu, Ge - George
item Schroeder, Steven - Steve
item Smith, Timothy - Tim
item Sonstegard, Tad
item Van Tassell, Curtis - Curt
item Bickhart, Derek

Submitted to: World Congress of Genetics Applied in Livestock Production
Publication Type: Proceedings
Publication Acceptance Date: 4/21/2014
Publication Date: 8/17/2014
Citation: Cole, J.B., Hutchison, J.L., Null, D.J., Van Raden, P.M., Liu, G., Schroeder, S.G., Smith, T.P., Sonstegard, T.S., Van Tassell, C.P., Bickhart, D.M. 2014. The hunt for a functional mutation affecting conformation and calving traits on chromosome 18 in Holstein cattle. World Congress of Genetics Applied in Livestock Production. Vancouver, Canada, Aug. 17–22. 3 pp.

Interpretive Summary:

Technical Abstract: Sequence data from 11 US Holstein bulls were analyzed to identify putative causal mutations associated with calving and conformation traits. The SNP ARS-BFGL-NGS-109285 at 57,589,121 bp (UMD 3.1 assembly) on BTA18 has large effects on 4 measures of body shape and size, 2 measures of dystocia, longevity, and lifetime economic merit. This region includes a human sialic acid Ig-like lectin 6 (Siglec-6) gene. We sequenced a homozygote for the minor allele, 4 carriers, and 3 non-carrier bulls from the same family. Three unrelated carrier bulls also were sequenced. Tandem duplications, insertions, and deletions were detected using custom analysis software that uses paired-end read alignments and split-read mapping. One duplication CNV and two tandem duplication events were detected within the gene. Predicted tandem duplications present in the carrier animals suggest that portions of two exons and a connecting intron within the Ig-like protein domains of Siglec-6 may have been duplicated.