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1O95105_HUMAN*   Trembl (?) | Description Local Annotation Link Reference
General Information
DescriptionOsmosis responsive factor.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005488 binding (IEA)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
This Pfam entry includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by . See: .
  IPR013105:Tetratricopeptide TPR_2
The tetratrico peptide repeat (TPR) is a structural motif present in a wide range of proteins . It mediates proteinprotein interactions and the assembly of multiprotein complexes . The TPR motif consists of 316 tandem-repeats of 34 amino acids residues.lthough individual TPR motifs can be dispersed in the protein sequence. Sequence alignment of the TPR domains reveals a consensus sequence defined by a pattern of small and large amino acids. TPR motifs have been identified in various different organisms.anging from bacteria to humans. Proteins containing TPRs are involved in a variety of biological processes.uch as cell cycle regulation.ranscriptional control.itochondrial and peroxisomal protein transport.eurogenesis and protein folding. The X-ray structure of a domain containing three TPRs from protein phosphatase 5 revealed that TPR adopts a helixturnhelix arrangement.ith adjacent TPR motifs packing in a parallel fashion.esulting in a spiral of repeating anti-parallel alpha-helices . The two helices are denoted helix A and helix B. The packing angle between helix A and helix B is ~24° within a single TPR and generates a right-handed superhelical shape. Helix A interacts with helix B and with helix A of the next TPR. Two protein surfaces are generated: the inner concave surface is contributed to mainly by residue on helices A.nd the other surface presents residues from both helices A and B.
  IPR001440:Tetratricopeptide TPR_1
This domain consists of a multi-helical fold comprised of two curved layers of alpha helices arranged in a regular right-handed the repeats that make up this structure are arranged about a common axis . These superhelical structures present an extensive solvent-accessible surface that is well suited to binding large substrates such as proteins and nucleic acids. This topology has been found with a number of repeats and domains.ncluding the tetratricopeptide repeat (TPR) (found in kinesin light chains.NAP regulatory proteins.lathrin heavy chains and bacterial aspartyl-phosphate phosphatases).nd the pentatricopeptide repeat (PPR) (RNA-processing proteins). The TRP is likely to be an ancient repeat.ince it is found in eukaryotes.acteria and archaea.hereas the PPR repeat is found predominantly in higher plants. The superhelix formed from these repeats can bind ligands at a number of different regions.nd has the ability to acquire multiple functional roles .
  IPR011990:Tetratricopeptide-like helical
SequencesProtein: O95105_HUMAN (262 aa)
mRNA: NM_012382
Local Annotation
Synapse Ontology
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 675 residues, 40750335-40752357Exon2: 46 residues, 40764203-40764335Exon3: 29 residues, 40766120-40766202Exon4: 76 residues, 40782656-40782878Exon5: 30 residues, 40791682-40791767Exon6: 2 residues, -Jump to O95105_HUMAN  
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Loci Cluster (Details)Loci: 4711 40795238-40834233 ~-39K 28748(PRKAA1)(-)Loci: 4710 40750335-40791767 ~-41K 28747(-)Link out to UCSC