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Protein

Reticulon-like protein 1

Gene

RTN1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GO - Biological processi

  1. endoplasmic reticulum organization Source: UniProtKB
  2. endoplasmic reticulum tubular network maintenance Source: SGD
  3. endoplasmic reticulum tubular network organization Source: UniProtKB
  4. nuclear pore complex assembly Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-29810-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Reticulon-like protein 1
Gene namesi
Name:RTN1
Ordered Locus Names:YDR233C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDR233c.
SGDiS000002641. RTN1.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5050CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei51 – 7323HelicalSequence AnalysisAdd
BLAST
Topological domaini74 – 14269LumenalSequence AnalysisAdd
BLAST
Transmembranei143 – 16321HelicalSequence AnalysisAdd
BLAST
Topological domaini164 – 295132CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cortical endoplasmic reticulum Source: SGD
  2. endoplasmic reticulum Source: SGD
  3. endoplasmic reticulum tubular network Source: UniProtKB
  4. Golgi apparatus Source: SGD
  5. integral component of cytoplasmic side of endoplasmic reticulum membrane Source: UniProtKB
  6. integral component of endoplasmic reticulum membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 295295Reticulon-like protein 1PRO_0000168168Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei186 – 1861Phosphothreonine2 Publications
Modified residuei219 – 2191Phosphothreonine1 Publication
Modified residuei232 – 2321Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ04947.
PaxDbiQ04947.
PeptideAtlasiQ04947.

Expressioni

Gene expression databases

GenevestigatoriQ04947.

Interactioni

Subunit structurei

Interacts with POM33.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SEY1Q992872EBI-38020,EBI-37523

Protein-protein interaction databases

BioGridi32284. 115 interactions.
DIPiDIP-4090N.
IntActiQ04947. 15 interactions.
MINTiMINT-510849.
STRINGi4932.YDR233C.

Structurei

3D structure databases

ProteinModelPortaliQ04947.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 220201ReticulonPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili265 – 29531Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi9 – 168Poly-Gln

Sequence similaritiesi

Contains 1 reticulon domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG116114.
GeneTreeiENSGT00530000066264.
HOGENOMiHOG000248018.
InParanoidiQ04947.
OMAiGASKFPD.
OrthoDBiEOG7C8GVW.

Family and domain databases

InterProiIPR003388. Reticulon.
[Graphical view]
PANTHERiPTHR10994. PTHR10994. 1 hit.
PfamiPF02453. Reticulon. 1 hit.
[Graphical view]
PROSITEiPS50845. RETICULON. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q04947-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSASAQHSQA QQQQQQKSCN CDLLLWRNPV QTGKYFGGSL LALLILKKVN
60 70 80 90 100
LITFFLKVAY TILFTTGSIE FVSKLFLGQG LITKYGPKEC PNIAGFIKPH
110 120 130 140 150
IDEALKQLPV FQAHIRKTVF AQVPKHTFKT AVALFLLHKF FSWFSIWTIV
160 170 180 190 200
FVADIFTFTL PVIYHSYKHE IDATVAQGVE ISKQKTQEFS QMACEKTKPY
210 220 230 240 250
LDKVESKLGP ISNLVKSKTA PVSSTAGPQT ASTSKLAADV PLEPESKAYT
260 270 280 290
SSAQVMPEVP QHEPSTTQEF NVDELSNELK KSTKNLQNEL EKNNA
Length:295
Mass (Da):32,916
Last modified:November 1, 1996 - v1
Checksum:i245575E65D3C2193
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY164798 mRNA. Translation: AAP47373.1.
Z48612 Genomic DNA. Translation: CAA88512.1.
AY558579 Genomic DNA. Translation: AAS56905.1.
BK006938 Genomic DNA. Translation: DAA12074.1.
PIRiS59439.
RefSeqiNP_010519.3. NM_001180541.3.

Genome annotation databases

EnsemblFungiiYDR233C; YDR233C; YDR233C.
GeneIDi851819.
KEGGisce:YDR233C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY164798 mRNA. Translation: AAP47373.1.
Z48612 Genomic DNA. Translation: CAA88512.1.
AY558579 Genomic DNA. Translation: AAS56905.1.
BK006938 Genomic DNA. Translation: DAA12074.1.
PIRiS59439.
RefSeqiNP_010519.3. NM_001180541.3.

3D structure databases

ProteinModelPortaliQ04947.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32284. 115 interactions.
DIPiDIP-4090N.
IntActiQ04947. 15 interactions.
MINTiMINT-510849.
STRINGi4932.YDR233C.

Proteomic databases

MaxQBiQ04947.
PaxDbiQ04947.
PeptideAtlasiQ04947.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR233C; YDR233C; YDR233C.
GeneIDi851819.
KEGGisce:YDR233C.

Organism-specific databases

CYGDiYDR233c.
SGDiS000002641. RTN1.

Phylogenomic databases

eggNOGiNOG116114.
GeneTreeiENSGT00530000066264.
HOGENOMiHOG000248018.
InParanoidiQ04947.
OMAiGASKFPD.
OrthoDBiEOG7C8GVW.

Enzyme and pathway databases

BioCyciYEAST:G3O-29810-MONOMER.

Miscellaneous databases

NextBioi969686.

Gene expression databases

GenevestigatoriQ04947.

Family and domain databases

InterProiIPR003388. Reticulon.
[Graphical view]
PANTHERiPTHR10994. PTHR10994. 1 hit.
PfamiPF02453. Reticulon. 1 hit.
[Graphical view]
PROSITEiPS50845. RETICULON. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A reticular rhapsody: phylogenic evolution and nomenclature of the RTN/Nogo gene family."
    Oertle T., Klinger M., Stuermer C.A.O., Schwab M.E.
    FASEB J. 17:1238-1247(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Bienvenut W.V., Peters C.
    Submitted (JUN-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 18-27; 219-247 AND 285-295, IDENTIFICATION BY MASS SPECTROMETRY.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-186, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-186; THR-219 AND SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Pom33, a novel transmembrane nucleoporin required for proper nuclear pore complex distribution."
    Chadrin A., Hess B., San Roman M., Gatti X., Lombard B., Loew D., Barral Y., Palancade B., Doye V.
    J. Cell Biol. 189:795-811(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POM33.

Entry informationi

Entry nameiRTN1_YEAST
AccessioniPrimary (citable) accession number: Q04947
Secondary accession number(s): D6VSL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 1, 1996
Last modified: January 7, 2015
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 37105 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.