Difference between revisions of "Phosphatase Subfamily SAC1"
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[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_Sac|Family Sac]]: [[Phosphatase_Subfamily_SAC1|Subfamily SAC1]] | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_Sac|Family Sac]]: [[Phosphatase_Subfamily_SAC1|Subfamily SAC1]] | ||
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| + | SAC1 is an integral membrane phosphoinositide phosphatase located in endoplasmic reticulum (ER) and golgi apparatus. SAC1 is conserved in eukaryotes. | ||
=== Evolution === | === Evolution === | ||
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=== Domain === | === Domain === | ||
| − | The SAC1 subfamily has | + | The SAC1 subfamily has SAC phosphatase domain. |
| + | |||
| + | Human SAC1 has a C-terminal tail of ~90 amino acid. The C-terminal tail a dual-pass transmembrane region. Human SAC1 also has a KxKxx motif of the last five C-terminal residues which mediates its interaction with COPI complex <cite>Rohde03</cite>. The motif is not strictly conserved, and it is unclear whether the last C-terminal residues of yeast SAC1 interacts with COPI complex. | ||
| + | |||
| + | Human SAC1 has a RLNSTSP motif (145-151) interacting with 14-3-3, which binds to COPII complex and serves as a cytosolic adaptor in mediating SAC1 transport in COPII-coated vesicle <cite>Pahuja15</cite>. The motif within the phosphatase domain is not conserved among SAC1s. An alignment of SAC1s in phosphatome.net shows none of the seven residues are strictly conserved. | ||
=== Function === | === Function === | ||
| − | The members of the SAC1 subfamily are integral membrane phosphoinositide phosphatases that play evolutionary conserved roles in eukaryotic cell physiology <cite>Nemoto00</cite>. It locates in the endoplasmic reticulum (ER) and the Golgi apparatus in yeast and mammals. | + | The members of the SAC1 subfamily are integral membrane phosphoinositide phosphatases that play evolutionary conserved roles in eukaryotic cell physiology <cite>Nemoto00</cite>. It locates in the endoplasmic reticulum (ER) and the Golgi apparatus in yeast <cite>Konrad02</cite> and mammals <cite>Rohde03</cite>. |
| − | SAC1 is best characterized in Saccharomyces cerevisiae <cite>Cleves89, Cai14</cite>. Yeast SAC1 mutants display a wide array of phenotypes including inositol auxotrophy, cold sensitivity, secretory defects, disturbed ATP transport into the ER, or suppression of actin gene mutations. | + | SAC1 is best characterized in Saccharomyces cerevisiae <cite>Cleves89, Cai14</cite>. Yeast SAC1 mutants display a wide array of phenotypes including inositol auxotrophy, cold sensitivity, secretory defects, disturbed ATP transport into the ER, or suppression of actin gene mutations. Sac1p is able to dephosphorylate PtdIns[3]P, PtdIns[4]P, and PtdIns[3,5]P2 in vitro, the role of Sac1p in processes involving PtdIns[4]P has been the primary focus of in vivo studies (see [http://www.yeastgenome.org/locus/S000001695/overview#paragraph SGD]). |
In mammals, it regulates Golgi membrane morphology and mitotic spindle organization <cite>Liu08</cite>. The human SAC1 is widely expressed in different tissues (see [http://www.gtexportal.org/home/gene/SACM1L GTEx]). It interacts with the coatomer I complex via a putative COPI interaction motif (KXKXX) at its C terminus in a manner dependent on its catalytic activity <cite>Rohde03</cite>. | In mammals, it regulates Golgi membrane morphology and mitotic spindle organization <cite>Liu08</cite>. The human SAC1 is widely expressed in different tissues (see [http://www.gtexportal.org/home/gene/SACM1L GTEx]). It interacts with the coatomer I complex via a putative COPI interaction motif (KXKXX) at its C terminus in a manner dependent on its catalytic activity <cite>Rohde03</cite>. | ||
| Line 19: | Line 25: | ||
#Cai14 pmid=25113029 | #Cai14 pmid=25113029 | ||
#Cleves89 pmid=2687291 | #Cleves89 pmid=2687291 | ||
| + | #Konrad02 pmid=11792713 | ||
#Liu08 pmid=18480408 | #Liu08 pmid=18480408 | ||
#Nemoto00 pmid=10887188 | #Nemoto00 pmid=10887188 | ||
| + | #Pahuja15 pmid=26056309 | ||
#Rohde03 pmid=14527956 | #Rohde03 pmid=14527956 | ||
</biblio> | </biblio> | ||
Latest revision as of 22:48, 10 June 2015
Phosphatase Classification: Fold CC1: Superfamily CC1: Family Sac: Subfamily SAC1
SAC1 is an integral membrane phosphoinositide phosphatase located in endoplasmic reticulum (ER) and golgi apparatus. SAC1 is conserved in eukaryotes.
Evolution
The SAC1 subfamily is conserved in eukaryotes. It is present in almost all the 203 eukaryotic genomes in gOrtholog database (internal).
Domain
The SAC1 subfamily has SAC phosphatase domain.
Human SAC1 has a C-terminal tail of ~90 amino acid. The C-terminal tail a dual-pass transmembrane region. Human SAC1 also has a KxKxx motif of the last five C-terminal residues which mediates its interaction with COPI complex [1]. The motif is not strictly conserved, and it is unclear whether the last C-terminal residues of yeast SAC1 interacts with COPI complex.
Human SAC1 has a RLNSTSP motif (145-151) interacting with 14-3-3, which binds to COPII complex and serves as a cytosolic adaptor in mediating SAC1 transport in COPII-coated vesicle [2]. The motif within the phosphatase domain is not conserved among SAC1s. An alignment of SAC1s in phosphatome.net shows none of the seven residues are strictly conserved.
Function
The members of the SAC1 subfamily are integral membrane phosphoinositide phosphatases that play evolutionary conserved roles in eukaryotic cell physiology [3]. It locates in the endoplasmic reticulum (ER) and the Golgi apparatus in yeast [4] and mammals [1].
SAC1 is best characterized in Saccharomyces cerevisiae [5, 6]. Yeast SAC1 mutants display a wide array of phenotypes including inositol auxotrophy, cold sensitivity, secretory defects, disturbed ATP transport into the ER, or suppression of actin gene mutations. Sac1p is able to dephosphorylate PtdIns[3]P, PtdIns[4]P, and PtdIns[3,5]P2 in vitro, the role of Sac1p in processes involving PtdIns[4]P has been the primary focus of in vivo studies (see SGD).
In mammals, it regulates Golgi membrane morphology and mitotic spindle organization [7]. The human SAC1 is widely expressed in different tissues (see GTEx). It interacts with the coatomer I complex via a putative COPI interaction motif (KXKXX) at its C terminus in a manner dependent on its catalytic activity [1].
References
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- Error fetching PMID 26056309:
- Error fetching PMID 10887188:
- Error fetching PMID 11792713:
- Error fetching PMID 2687291:
- Error fetching PMID 25113029:
- Error fetching PMID 18480408:
