SMART: Pfam domain Sorting

The domain within your query sequence starts at position 2 and ends at position 134; the E-value for the Sorting_nexin domain shown below is 1.6e-29.

AAEREPPPLGDVKPTDFEELEDGEDLFTSTVSTLESSPSSPEPASLPAEDISANSNGSKP
VEVVLDDDREDLFAEATEEVSLDSPERELILSSEPSPAVTPVTPTTLIAPRIESKSISAP
VIFDRSRDEIEEE

Sorting_nexin

PFAM accession number:	PF03700
Interpro abstract (IPR005329):	Sorting nexins (SNXs) are hydrophilic molecules that are localized in the cytoplasm and have the potential for membrane association either through their lipid-binding PX domains ( IPR001683 ) or through protein-protein interactions with membrane-associated protein complexes [ (PUBMED:12461558) ]. Indeed, several of the SNXs require several targeting motifs for their appropriate cellular localization. In almost every case studied, mammalian SNXs can be shown to have a role in protein sorting, with the most commonly used experimental model being plasma-membrane receptor endocytosis and sorting through the endosomal pathway. However, it is equally probable that SNXs sort vesicles that are not derived from the plasma membrane, and have a function in the accurate targeting of these vesicles and their cargo. The N-terminal domain appears to be specific to sorting nexins 1 and 2. SNX1 and SNX2 are members of the retromer complex involved in protein sorting within the endocytic pathway [ (PUBMED:17101778) ]. SNX1 is both membrane-associated and cytosolic, where it probably exists as a tetramer in large protein complexes and may hetero-oligomerize with SNX2.
GO process:	intracellular protein transport (GO:0006886)

PFAM accession number:

PF03700

Interpro abstract (IPR005329):

Sorting nexins (SNXs) are hydrophilic molecules that are localized in the cytoplasm and have the potential for membrane association either through their lipid-binding PX domains ( IPR001683 ) or through protein-protein interactions with membrane-associated protein complexes [ (PUBMED:12461558) ]. Indeed, several of the SNXs require several targeting motifs for their appropriate cellular localization. In almost every case studied, mammalian SNXs can be shown to have a role in protein sorting, with the most commonly used experimental model being plasma-membrane receptor endocytosis and sorting through the endosomal pathway. However, it is equally probable that SNXs sort vesicles that are not derived from the plasma membrane, and have a function in the accurate targeting of these vesicles and their cargo.

The N-terminal domain appears to be specific to sorting nexins 1 and 2. SNX1 and SNX2 are members of the retromer complex involved in protein sorting within the endocytic pathway [ (PUBMED:17101778) ]. SNX1 is both membrane-associated and cytosolic, where it probably exists as a tetramer in large protein complexes and may hetero-oligomerize with SNX2.

GO process:

intracellular protein transport (GO:0006886)

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