RTN1/YDR233C Summary Help

Standard Name RTN1 1
Systematic Name YDR233C
Feature Type ORF, Verified
Description Reticulon protein; stabilizes membrane curvature; involved in nuclear pore assembly and maintenance of tubular ER morphology; mutant overexpressing RTN1 shows increase in tubular ER; interacts with exocyst subunit Sec6p, Yip3p, and Sbh1p; more abundant than Rtn2p; member of the RTNLA subfamily; mutants have reduced phosphatidylserine transfer between the ER and mitochondria; RTN1 has a paralog, RTN2, that arose from the whole genome duplication (1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12)
Name Description ReTiculoN-like 1
Chromosomal Location
ChrIV:930357 to 929470 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology Annotations All RTN1 GO evidence and references
  View Computational GO annotations for RTN1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Regulators 8 genes
Resources
Classical genetics
null
Large-scale survey
null
overexpression
Resources
169 total interaction(s) for 114 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 33
  • Affinity Capture-RNA: 5
  • Affinity Capture-Western: 14
  • Co-purification: 1
  • PCA: 2
  • Two-hybrid: 2

Genetic Interactions
  • Dosage Growth Defect: 6
  • Negative Genetic: 51
  • Phenotypic Enhancement: 10
  • Phenotypic Suppression: 8
  • Positive Genetic: 16
  • Synthetic Growth Defect: 9
  • Synthetic Lethality: 11
  • Synthetic Rescue: 1

Resources
Expression Summary
histogram
Resources
Length (a.a.) 295
Molecular Weight (Da) 32,916
Isoelectric Point (pI) 9.64
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrIV:930357 to 929470 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..888 930357..929470 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000002641
References cited on this page View Complete Literature Guide for RTN1
1) Oertle T, et al.  (2003) A reticular rhapsody: phylogenic evolution and nomenclature of the RTN/Nogo gene family. FASEB J 17(10):1238-47
2) Geng J, et al.  (2005) Saccharomyces cerevisiae Rab-GDI displacement factor ortholog Yip3p forms distinct complexes with the Ypt1 Rab GTPase and the reticulon Rtn1p. Eukaryot Cell 4(7):1166-74
3) Byrne KP and Wolfe KH  (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
4) Voeltz GK, et al.  (2006) A class of membrane proteins shaping the tubular endoplasmic reticulum. Cell 124(3):573-86
5) de Craene JO, et al.  (2006) Rtn1p is involved in structuring the cortical endoplasmic reticulum. Mol Biol Cell 17(7):3009-20
6) Feng D, et al.  (2007) The transmembrane domain is sufficient for Sbh1p function, its association with the Sec61 complex, and interaction with Rtn1p. J Biol Chem 282(42):30618-28
7) Hu J, et al.  (2008) Membrane proteins of the endoplasmic reticulum induce high-curvature tubules. Science 319(5867):1247-50
8) Shibata Y, et al.  (2008) The reticulon and dp1/yop1p proteins form immobile oligomers in the tubular endoplasmic reticulum. J Biol Chem 283(27):18892-904
9) Dawson TR, et al.  (2009) ER membrane-bending proteins are necessary for de novo nuclear pore formation. J Cell Biol 184(5):659-75
10) Hu J, et al.  (2009) A class of dynamin-like GTPases involved in the generation of the tubular ER network. Cell 138(3):549-61
11) West M, et al.  (2011) A 3D analysis of yeast ER structure reveals how ER domains are organized by membrane curvature. J Cell Biol 193(2):333-46
12) Voss C, et al.  (2012) ER-shaping proteins facilitate lipid exchange between the ER and mitochondria in S. cerevisiae. J Cell Sci 125(Pt 20):4791-9