Component of the U7 snRNP complex that is involved in the histone 3'-end pre-mRNA processing (PubMed:11574479, PubMed:16914750, PubMed:33230297). Increases U7 snRNA levels but not histone 3'-end pre-mRNA processing activity, when overexpressed (PubMed:11574479, PubMed:16914750). Required for cell cycle progression from G1 to S phases (By similarity). Binds specifically to the Sm-binding site of U7 snRNA (PubMed:11574479, PubMed:16914750). Component of the heptameric ring U7 snRNP complex, or U7 Sm protein core complex, at least composed of LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF, SNRPG and U7 snRNA (PubMed:12975319, PubMed:11574479). Formation of the U7 snRNP is an ATP-dependent process mediated by a specialized SMN complex containing at least the Sm protein core complex and additionally, the U7-specific LSM10 and LSM11 proteins (PubMed:11574479). Identified in a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1 (By similarity). Interacts (via the Sm domains) with CLNS1A (By similarity). Interacts with SMN and ZNF473 (PubMed:12975319, PubMed:16714279). Interacts with PRMT5 and WDR77 (By similarity). The C-terminal SM 1 domain is both necessary for the binding to the Sm-binding site of U7 snRNA and U7 snRNP assembly (By similarity). The N-terminal domain is essential for histone pre-mRNA cleavage (By similarity). Amino acids 63-82 are sufficient to interact with ZNF473 (By similarity). The disease is caused by variants affecting the gene represented in this entry. Impaired histone 3'-end pre-mRNA processing caused by disease variants affects chromatin structure, relieving CGAS inhibition by nucleosomes (PubMed:33230297). This activates the cGAS-STING pathway, triggering type-I interferon production and autoinflammation (PubMed:33230297). Belongs to the snRNP Sm proteins family.