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RTN1_YEAST
ID   RTN1_YEAST              Reviewed;         295 AA.
AC   Q04947; D6VSL4;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 164.
DE   RecName: Full=Reticulon-like protein 1;
GN   Name=RTN1; OrderedLocusNames=YDR233C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12832288; DOI=10.1096/fj.02-1166hyp;
RA   Oertle T., Klinger M., Stuermer C.A.O., Schwab M.E.;
RT   "A reticular rhapsody: phylogenic evolution and nomenclature of the
RT   RTN/Nogo gene family.";
RL   FASEB J. 17:1238-1247(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   PROTEIN SEQUENCE OF 18-27; 219-247 AND 285-295, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RA   Bienvenut W.V., Peters C.;
RL   Submitted (JUN-2005) to UniProtKB.
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-186, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-186; THR-219 AND SER-232, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [11]
RP   INTERACTION WITH POM33.
RX   PubMed=20498018; DOI=10.1083/jcb.200910043;
RA   Chadrin A., Hess B., San Roman M., Gatti X., Lombard B., Loew D.,
RA   Barral Y., Palancade B., Doye V.;
RT   "Pom33, a novel transmembrane nucleoporin required for proper nuclear pore
RT   complex distribution.";
RL   J. Cell Biol. 189:795-811(2010).
CC   -!- SUBUNIT: Interacts with POM33. {ECO:0000269|PubMed:20498018}.
CC   -!- INTERACTION:
CC       Q04947; Q99287: SEY1; NbExp=3; IntAct=EBI-38020, EBI-37523;
CC       Q04947; P03588: ORF1a; Xeno; NbExp=4; IntAct=EBI-38020, EBI-15874242;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 37105 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
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DR   EMBL; AY164798; AAP47373.1; -; mRNA.
DR   EMBL; Z48612; CAA88512.1; -; Genomic_DNA.
DR   EMBL; AY558579; AAS56905.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12074.1; -; Genomic_DNA.
DR   PIR; S59439; S59439.
DR   RefSeq; NP_010519.3; NM_001180541.3.
DR   AlphaFoldDB; Q04947; -.
DR   BioGRID; 32284; 204.
DR   DIP; DIP-4090N; -.
DR   IntAct; Q04947; 28.
DR   MINT; Q04947; -.
DR   STRING; 4932.YDR233C; -.
DR   TCDB; 8.A.102.1.4; the reticulon (reticulon) family.
DR   CarbonylDB; Q04947; -.
DR   iPTMnet; Q04947; -.
DR   MaxQB; Q04947; -.
DR   PaxDb; Q04947; -.
DR   PRIDE; Q04947; -.
DR   TopDownProteomics; Q04947; -.
DR   EnsemblFungi; YDR233C_mRNA; YDR233C; YDR233C.
DR   GeneID; 851819; -.
DR   KEGG; sce:YDR233C; -.
DR   SGD; S000002641; RTN1.
DR   VEuPathDB; FungiDB:YDR233C; -.
DR   eggNOG; KOG1792; Eukaryota.
DR   GeneTree; ENSGT00940000176429; -.
DR   HOGENOM; CLU_050576_0_0_1; -.
DR   InParanoid; Q04947; -.
DR   OMA; TGLMKQY; -.
DR   BioCyc; YEAST:G3O-29810-MON; -.
DR   PRO; PR:Q04947; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q04947; protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR   GO; GO:0071782; C:endoplasmic reticulum tubular network; IDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR   GO; GO:0071458; C:integral component of cytoplasmic side of endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0048309; P:endoplasmic reticulum inheritance; IGI:SGD.
DR   GO; GO:0007029; P:endoplasmic reticulum organization; IGI:UniProtKB.
DR   GO; GO:0071788; P:endoplasmic reticulum tubular network maintenance; IGI:SGD.
DR   GO; GO:0071786; P:endoplasmic reticulum tubular network organization; IMP:UniProtKB.
DR   GO; GO:0032581; P:ER-dependent peroxisome organization; IGI:SGD.
DR   GO; GO:0051292; P:nuclear pore complex assembly; IGI:SGD.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IGI:SGD.
DR   InterPro; IPR003388; Reticulon.
DR   Pfam; PF02453; Reticulon; 1.
DR   PROSITE; PS50845; RETICULON; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Direct protein sequencing; Endoplasmic reticulum; Membrane;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..295
FT                   /note="Reticulon-like protein 1"
FT                   /id="PRO_0000168168"
FT   TOPO_DOM        1..50
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        51..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        74..142
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        143..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        164..295
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          20..220
FT                   /note="Reticulon"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00170"
FT   REGION          219..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          265..295
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        219..236
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..273
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         186
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         219
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         232
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   295 AA;  32916 MW;  245575E65D3C2193 CRC64;
     MSASAQHSQA QQQQQQKSCN CDLLLWRNPV QTGKYFGGSL LALLILKKVN LITFFLKVAY
     TILFTTGSIE FVSKLFLGQG LITKYGPKEC PNIAGFIKPH IDEALKQLPV FQAHIRKTVF
     AQVPKHTFKT AVALFLLHKF FSWFSIWTIV FVADIFTFTL PVIYHSYKHE IDATVAQGVE
     ISKQKTQEFS QMACEKTKPY LDKVESKLGP ISNLVKSKTA PVSSTAGPQT ASTSKLAADV
     PLEPESKAYT SSAQVMPEVP QHEPSTTQEF NVDELSNELK KSTKNLQNEL EKNNA
 
 
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