SMART: Pfam domain DUF747

The domain within your query sequence starts at position 152 and ends at position 456; the E-value for the DUF747 domain shown below is 8.9e-112.

LQPAQVCDILKGVILVICYFMMHYVDYSMMYHLIRGQSVIKLYIIYNMLEVADRLFSSFG
QDILDALYWTATEPKERKRAHIGVIPHFFMAVLYVFLHAILIMVQATTLNVAFNSHNKSL
LTIMMSNNFVEIKGSVFKKFEKNNLFQMSNSDIKERFTNYVLLLIVCLRNMEQFSWNPDH
LWVLFPDVCMVIASEIAVDIVKHAFITKFNDITADVYSEYRASLAFDLVSSRQKNAYTDY
SDSVARRMGFIPLPLAVLLIRVVTSSIKVQGILSYACVILFYFGLISLKILNSIVLLGKS
CQYVK

DUF747

PFAM accession number:	PF05346
Interpro abstract (IPR008010):	This family of membrane proteins is conserved in eukaryotes. It includes Tapt1 (transmembrane anterior posterior transformation 1) and homologues. Analysis of mouse Tapt1 has shown it to be involved in patterning of the vertebrate axial skeleton [ (PUBMED:17151244) ]. Its cellular function is not known, but defective Tapt1 disrupts Golgi morphology and trafficking, and normal primary cilium formation [ (PUBMED:26365339) ]. The homologues in yeast, endoplasmic reticulum membrane protein 65, and Arabidopsis, POD1, seem to be involved in protein folding in the endoplasmic reticulum [ (PUBMED:19325107) (PUBMED:21954464) ].

PFAM accession number:

PF05346

Interpro abstract (IPR008010):

This family of membrane proteins is conserved in eukaryotes. It includes Tapt1 (transmembrane anterior posterior transformation 1) and homologues. Analysis of mouse Tapt1 has shown it to be involved in patterning of the vertebrate axial skeleton [ (PUBMED:17151244) ]. Its cellular function is not known, but defective Tapt1 disrupts Golgi morphology and trafficking, and normal primary cilium formation [ (PUBMED:26365339) ].

The homologues in yeast, endoplasmic reticulum membrane protein 65, and Arabidopsis, POD1, seem to be involved in protein folding in the endoplasmic reticulum [ (PUBMED:19325107) (PUBMED:21954464) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry DUF747