RTN1_SCHPO
ID RTN1_SCHPO Reviewed; 308 AA.
AC P53694;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Reticulon-like protein 1;
DE AltName: Full=Cell lysis protein cwl1;
GN Name=rtn1; Synonyms=cwl1; ORFNames=SPBC31A8.01c, SPBC651.13c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8873452;
RX DOI=10.1002/(sici)1097-0061(199608)12:10<983::aid-yea2>3.0.co;2-d;
RA Godoy C., Arellano M., Diaz M., Duran A., Perez P.;
RT "Characterization of cwl1+, a gene from Schizosaccharomyces pombe whose
RT overexpression causes cell lysis.";
RL Yeast 12:983-990(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP SUBCELLULAR LOCATION, INTERACTION WITH TTS1 AND YOP1, AND FUNCTION.
RX PubMed=20434336; DOI=10.1016/j.cub.2010.04.017;
RA Zhang D., Vjestica A., Oliferenko S.;
RT "The cortical ER network limits the permissive zone for actomyosin ring
RT assembly.";
RL Curr. Biol. 20:1029-1034(2010).
CC -!- FUNCTION: Required for the correct positioning of the cellular division
CC plane by delimiting the actomyosin ring assembly at the cell equator.
CC Overexpression causes cell lysis. {ECO:0000269|PubMed:20434336}.
CC -!- SUBUNIT: Interacts with TTS1 and YOP1. {ECO:0000269|PubMed:20434336}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:20434336}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:20434336}. Nucleus membrane
CC {ECO:0000269|PubMed:20434336}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:20434336}. Note=Enriched at the cell equator during
CC mitosis.
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DR EMBL; X94445; CAA64219.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB37626.1; -; Genomic_DNA.
DR PIR; S71746; S71746.
DR RefSeq; NP_001018789.2; NM_001021421.3.
DR AlphaFoldDB; P53694; -.
DR BioGRID; 280345; 55.
DR STRING; 4896.SPBC31A8.01c.1; -.
DR iPTMnet; P53694; -.
DR MaxQB; P53694; -.
DR PaxDb; P53694; -.
DR PRIDE; P53694; -.
DR EnsemblFungi; SPBC31A8.01c.1; SPBC31A8.01c.1:pep; SPBC31A8.01c.
DR GeneID; 3361269; -.
DR KEGG; spo:SPBC31A8.01c; -.
DR PomBase; SPBC31A8.01c; rtn1.
DR VEuPathDB; FungiDB:SPBC31A8.01c; -.
DR eggNOG; KOG1792; Eukaryota.
DR HOGENOM; CLU_903618_0_0_1; -.
DR InParanoid; P53694; -.
DR OMA; WINIPRL; -.
DR PhylomeDB; P53694; -.
DR PRO; PR:P53694; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1990809; P:endoplasmic reticulum tubular network membrane organization; IMP:PomBase.
DR InterPro; IPR003388; Reticulon.
DR Pfam; PF02453; Reticulon; 1.
DR PROSITE; PS50845; RETICULON; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Nucleus; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..308
FT /note="Reticulon-like protein 1"
FT /id="PRO_0000079619"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 127..308
FT /note="Reticulon"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00170"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 308 AA; 33659 MW; F6FA92A6E9FF695D CRC64;
MSEQHSLNPF ESGSVTASDV AAAKSGAEDL VNTLTAHTVH PSTELPSATS FPSALPNSEN
PVIQNISSSS SEPHHTSQST PGETSSPVCP VSGAHGGADK KCPALEAGCP FTNTTKQNVD
PEISNALWSV LTWKNTSCSF STLMSILALV YVPSWINLPR LFFRTFRYVF LITSIIEFGG
LFASNGKRGV LSHFRSSYIT CDSKALDRIV NSIVDIFNVM LIQFQRILFA ESPILTFTAS
VAAFIEFFLS GFLSYKSLFV WNVLFAFILP RLYVCNERSI KHLVASLERS GDKLKKQATE
TINTTVNK
