The domain within your query sequence starts at position 37 and ends at position 243; the E-value for the Seipin domain shown below is 3.9e-71.

TILLLLWVSVFLYGSFYYSYMPTVSHLSPVHFHYRTDCDSSTASLCSFPVANVSLAKSGR
DRVLMYGQPYRVTLELELPESPVNQDLGMFLVTVSCYTRGGRIISTSSRSVMLHYRSQLL
QVLDTLLFSSLLLFGFAEQKQLLEVELYSDYRENSYVPTTGAIIEIHSKRIQMYGAYLRI
HAHFTGLRYLLYNFPMTCAFVGVASNF

Seipin

Seipin
PFAM accession number:PF06775
Interpro abstract (IPR009617):

Seipin is a cell-autonomous regulator of lipolysis essential for adipocyte differentiation [(PUBMED:22269949)]. Seipin is predicted to contain two transmembrane domains at residues 28-49 and 237-258, in humans, and a third transmembrane domain might be present at residues 155-173. Mutations in the Seipin gene underlie human congenital generalized lipodystrophy [(PUBMED:11479539)]. Seipin may also be implicated in Silver spastic paraplegia syndrome and distal hereditary motor neuropathy type V [(PUBMED:11479539)].

This entry also includes Seipin homologues from fission yeasts and plants. There are three SEIPIN homologues in Arabidopsis thaliana, designated SEIPIN1, SEIPIN2, and SEIPIN3. Similar to their animal homologus, plant and yeast Seipins also play roles in lipid droplet (LD) biogenesis [(PUBMED:26362606)].

GO process:lipid storage (GO:0019915)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Seipin