RTN1/YDR233C Protein Information Help

Standard Name Rtn1p 1
Systematic Name Ydr233cp
ORF Classification 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, 10, 11, 12, 2, 3, 4, 5, 6, 7, 8, 9)
Name Description ReTiculoN-like 1
Experimental Data
Molecules/cell 37100 13
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 295
Molecular Weight (Da) 32,916
Isoelectric Point (pI) 9.64

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Rtn1p (InterPro)
Transmembrane Domains There are 2 total predicted transmembrane domains (TMHMM)
Physical Interactions There are 52 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI000006C2BF | Q04947
MIPS: YDR233C
NCBI: 32331691 | 398366209 | 45271048 | 728688 | 74644878 | NP_010519.3
GenBank/EMBL/DDBJ: DAA12074.1 | AY164798 | AY558579 | Z48612
Amino Acid Sequence (or in FASTA format)
       1  MSASAQHSQA QQQQQQKSCN CDLLLWRNPV QTGKYFGGSL LALLILKKVN
      51  LITFFLKVAY TILFTTGSIE FVSKLFLGQG LITKYGPKEC PNIAGFIKPH
     101  IDEALKQLPV FQAHIRKTVF AQVPKHTFKT AVALFLLHKF FSWFSIWTIV
     151  FVADIFTFTL PVIYHSYKHE IDATVAQGVE ISKQKTQEFS QMACEKTKPY
     201  LDKVESKLGP ISNLVKSKTA PVSSTAGPQT ASTSKLAADV PLEPESKAYT
     251  SSAQVMPEVP QHEPSTTQEF NVDELSNELK KSTKNLQNEL EKNNA*    

external links for Rtn1p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily Organelle DB
Ashbya (AGD) BOND GPMdb (Mass Spec.) YPL+
Aspergillus (AspGD) BioPIXIE MIPS YeastGFP
Candida (CGD) CYC2008 (complexes) Pfam domains YeastRC Public Image Repository
Candida (CandidaDB) Complexome YeastRC Structure Prediction (Seattle)
YGOB DIP

YOGY GeneMANIA


YeastRC Mass Spec (Seattle)

References cited on this page View Complete Literature Guide for Rtn1p
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
13) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41