Summary: Glucosidase II beta subunit-like protein
Glucosidase II beta subunit-like protein Provide feedback
The sequences found in this family are similar to a region found in the beta-subunit of glucosidase II (P14314), which is also known as protein kinase C substrate 80K-H (PRKCSH). The enzyme catalyses the sequential removal of two alpha-1,3-linked glucose residues in the second step of N-linked oligosaccharide processing . The beta subunit is required for the solubility and stability of the heterodimeric enzyme, and is involved in retaining the enzyme within the endoplasmic reticulum . Mutations in the gene coding for PRKCSH have been found to be involved in the development of autosomal dominant polycystic liver disease (ADPLD), but the precise role the protein has in the pathogenesis of this disease is unknown . This family also includes an ER sensor for misfolded glycoproteins and is therefore likely to be a generic sugar binding domain.
Pelletier MF, Marcil A, Sevigny G, Jakob CA, Tessier DC, Chevet E, Menard R, Bergeron JJ, Thomas DY; , Glycobiology 2000;10:815-827.: The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo. PUBMED:10929008 EPMC:10929008
Li A, Davila S, Furu L, Qian Q, Tian X, Kamath PS, King BF, Torres VE, Somlo S; , Am J Hum Genet 2003;72:691-703.: Mutations in PRKCSH cause isolated autosomal dominant polycystic liver disease. PUBMED:12529853 EPMC:12529853
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR012913
The sequences found in this family are similar to a region found in the beta-subunit of glucosidase II (SWISSPROT), which is also known as protein kinase C substrate 80K-H (PRKCSH). The enzyme catalyses the sequential removal of two alpha-1,3-linked glucose residues in the second step of N-linked oligosaccharide processing [PUBMED:10929008]. The beta subunit is required for the solubility and stability of the heterodimeric enzyme, and is involved in retaining the enzyme within the endoplasmic reticulum [PUBMED:10929008]. Mutations in the gene coding for PRKCSH have been found to be involved in the development of autosomal dominant polycystic liver disease (ADPLD), but the precise role the protein has in the pathogenesis of this disease is unknown [PUBMED:12529853].
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We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_9407 (release 14.0)|
|Number in seed:||104|
|Number in full:||586|
|Average length of the domain:||84.40 aa|
|Average identity of full alignment:||27 %|
|Average coverage of the sequence by the domain:||19.03 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||8|
|Download:||download the raw HMM for this family|
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There are 3 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the PRKCSH domain has been found. There are 2 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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