The domain within your query sequence starts at position 18 and ends at position 818; the E-value for the Prominin domain shown below is 3e-288.

LALSLPEAVTDDCGSLGRVEHLAFARVPRTRELAPLVRASGPLNSLYGTVRRFLSVVQLN
PFPAELIKTLLNDPSSVKTDEVVRYEAGYVVCAVIAGLYLLLVPITGLCFCCCRCRQRCG
GRVKTEHKAMACERGTLMIFLLLTTLVLLIGMVCAFATNQHTHSQTGPSVKAVPETLLSL
RGLVSDVPEELRAIAEQFSVPQKQVSKELDGVGENLGNVIHNRLKSTVYPVLASVHSLGQ
ALQVSIDHLRALNTTSVELQEAQRHLEPPVQAHRERLLALLQDSWCHEENCKRVLSQAGA
LQLGADFSQTPPVDDVLHRLKDVPETNFSSMVQEEKATFNNLPLLVQVQAVSVVKDVKKA
LAEQPEGLRMLAQAFPGSEAASRWSQALEGLEQRSRPYLQEVQQYETYRWILGCVLCSAI
LLVVICNLLGLSLGIWGLFAREDPSHSETKGEAGARLLMAGVAFSFLFAVPLILLVFVTF
LVGGNVQTLVCRSWESGELYEFADTPGNLPPSMNLSYLLGLKKNISIVQAYRQCKAGAVL
WKVLQLNDSYDLDKHLDIKQYTHKIQQELQSFQVDLKELDLLSPTARQDLEALQRSGLEK
IHYRGFLVQIQKPVVNTDMWQLAQELEGLAQAQNDSLLRQQLREEARELRSLYQEKVVPQ
ESLVTKLNFSVKTLESLAPSLQVNTSDFLDSVTRLKGELPVQINHILRNATECFLTREMG
YFSQYVTWVRAEVTQRIATCQPFSTALDNGHVILCDMMADPWNAFWFCLGWCTFFLIPSI
IFAVKTSKYFRPIRKRLRVTS

Prominin

Prominin
PFAM accession number:PF05478
Interpro abstract (IPR008795):

The prominins are an emerging family of proteins that, among the multispan membrane proteins, display a novel topology. Mouse and Homo sapiens prominin and (Mus musculus) prominin-like 1 (PROML1) are predicted to contain five membrane spanning domains, with an N-terminal domain exposed to the extracellular space followed by four, alternating small cytoplasmic and large extracellular, loops and a cytoplasmic C-terminal domain [ (PUBMED:11467842) ]. The exact function of prominin is unknown although in humans defects in PROM1, the gene coding for prominin, cause retinal degeneration [ (PUBMED:10587575) ].

GO component:integral component of membrane (GO:0016021)

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