SMART: Pfam domain Syja

The domain within your query sequence starts at position 100 and ends at position 381; the E-value for the Syja_N domain shown below is 4.2e-71.

YGLLGVLRLNLGDTMLHYLVLVTGCMSVGKIQESEVFRVTSTEFISLRVDASDEDRISEV
RKVLNSGNFYFAWSASGVSLDLSLNAHRSMQEHTTDNRFFWNQSLHLHLKHYGVNCDDWL
LRLMCGGVEIRTIYAAHKQAKACLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVIYL
DDCVSSFIQIRGSVPLFWEQPGLQVGSHRVRMSRGFEANAPAFDRHFRTLKDLYGKQIVV
NLLGSKEGEHMLSKAFQSHLKASEHASDIHMVSFDYHQMVKG

Syja_N

PFAM accession number:	PF02383
Interpro abstract (IPR002013):	The Sac domain is a region of homology between the N terminus of synaptojanin and the otherwise unrelated yeast protein Sac1p. The Sac domain is approximately 400 residues in length, and proteins containing this domain show approximately 35% identity with other Sac domains throughout this region. The Sac domain exhibits phosphatidylinositol polyphosphate phosphatase activity and can hydrolyse phosphate from any of the three positions of inositol that may be phosphorylated (3-, 4- and 5). However, adjacent phosphates are resistant to hydrolysis. Sac domains cannot hydrolyse phosphate from phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2), or PtdIns(3,4)P2, or PtdIns(3,4,5)P3, but can hydrolyse PtdIns(3,5)P2 [ (PUBMED:11413010) ]. The Sac domain consists of seven highly conserved motifs which appear to define the catalytic and regulatory regions of the phosphatase. The sixth conserved region contains a highly conserved C-x(5)-R-[TS] motif, thought to be the catalytic motif of many metal-independent protein and inositide polyphosphate phosphatases. Interestingly, the Inp51p Sac domain in which the cysteine, arginine and threonine/serine residues within the C-x(5)-R-[TS] motif are absent, does not exhibit any phosphatase activity [ (PUBMED:11413010) ]. Two classes of Sac domain proteins have been identified in mammals as well as lower eukaryotes [ (PUBMED:11413010) ]. The first comprises proteins, which, in addition to an N-terminal phosphatase Sac domain, have all the domains associated with type II phosphatidylinositol phosphate 5-phosphatases: Mammalian synaptojanins, type II phosphatidylinositol phosphate 5- phosphatases. Yeast INP51, a 108kDa membrane protein. It is involved in endocytosis and regulation of the actin cytoskeleton under conditions of normal vegetative growth. Although the Sac phosphatase domain of INP51 may be catalytically inactive, the domain may retain other functions. Yeast INP52, a 133kDa membrane protein. It is involved in endocytosis and regulation of the actin cytoskeleton under conditions of normal vegetative growth. Yeast INP53, a 124kDa membrane protein. It appears to have a role in intra-Golgi and Golgi-to-endosomal trafficking. The other class of Sac-containing phosphatases consists of proteins with an N-terminal Sac phosphatase domain and no other recognizable domains: Yeast Sac1p, a 67kDa membrane protein found in the endoplasmic reticulum (ER) and Golgi. It regulates the actin cytoskeleton and phospholipid metabolism. Yeast FIG4, a 101kDa protein encoded by a pheromone regulated or induced gene. FIG4 might function to regulate effector molecules of the actin cytoskeleton during mating.
GO function:	phosphoric ester hydrolase activity (GO:0042578)

PFAM accession number:

PF02383

Interpro abstract (IPR002013):

The Sac domain is a region of homology between the N terminus of synaptojanin and the otherwise unrelated yeast protein Sac1p. The Sac domain is approximately 400 residues in length, and proteins containing this domain show approximately 35% identity with other Sac domains throughout this region. The Sac domain exhibits phosphatidylinositol polyphosphate phosphatase activity and can hydrolyse phosphate from any of the three positions of inositol that may be phosphorylated (3-, 4- and 5). However, adjacent phosphates are resistant to hydrolysis. Sac domains cannot hydrolyse phosphate from phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2), or PtdIns(3,4)P2, or PtdIns(3,4,5)P3, but can hydrolyse PtdIns(3,5)P2 [ (PUBMED:11413010) ].

The Sac domain consists of seven highly conserved motifs which appear to define the catalytic and regulatory regions of the phosphatase. The sixth conserved region contains a highly conserved C-x(5)-R-[TS] motif, thought to be the catalytic motif of many metal-independent protein and inositide polyphosphate phosphatases. Interestingly, the Inp51p Sac domain in which the cysteine, arginine and threonine/serine residues within the C-x(5)-R-[TS] motif are absent, does not exhibit any phosphatase activity [ (PUBMED:11413010) ].

Two classes of Sac domain proteins have been identified in mammals as well as lower eukaryotes [ (PUBMED:11413010) ]. The first comprises proteins, which, in addition to an N-terminal phosphatase Sac domain, have all the domains associated with type II phosphatidylinositol phosphate 5-phosphatases:

Mammalian synaptojanins, type II phosphatidylinositol phosphate 5- phosphatases.
Yeast INP51, a 108kDa membrane protein. It is involved in endocytosis and regulation of the actin cytoskeleton under conditions of normal vegetative growth. Although the Sac phosphatase domain of INP51 may be catalytically inactive, the domain may retain other functions.
Yeast INP52, a 133kDa membrane protein. It is involved in endocytosis and regulation of the actin cytoskeleton under conditions of normal vegetative growth.
Yeast INP53, a 124kDa membrane protein. It appears to have a role in intra-Golgi and Golgi-to-endosomal trafficking.

The other class of Sac-containing phosphatases consists of proteins with an N-terminal Sac phosphatase domain and no other recognizable domains:

Yeast Sac1p, a 67kDa membrane protein found in the endoplasmic reticulum (ER) and Golgi. It regulates the actin cytoskeleton and phospholipid metabolism.
Yeast FIG4, a 101kDa protein encoded by a pheromone regulated or induced gene. FIG4 might function to regulate effector molecules of the actin cytoskeleton during mating.

GO function:

phosphoric ester hydrolase activity (GO:0042578)

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