ROT1_YEAST
ID ROT1_YEAST Reviewed; 256 AA.
AC Q03691; D6W025;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Protein ROT1;
DE AltName: Full=Reversal of TOR2 lethality protein 1;
DE Flags: Precursor;
GN Name=ROT1; OrderedLocusNames=YMR200W; ORFNames=YM8325.01;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
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 [3]
RP FUNCTION.
RX PubMed=9038344; DOI=10.1016/s0092-8674(00)81893-0;
RA Schmidt A., Bickle M., Beck T., Hall M.N.;
RT "The yeast phosphatidylinositol kinase homolog TOR2 activates RHO1 and RHO2
RT via the exchange factor ROM2.";
RL Cell 88:531-542(1997).
RN [4]
RP FUNCTION.
RX PubMed=9545237; DOI=10.1093/emboj/17.8.2235;
RA Bickle M., Delley P.-A., Schmidt A., Hall M.N.;
RT "Cell wall integrity modulates RHO1 activity via the exchange factor
RT ROM2.";
RL EMBO J. 17:2235-2245(1998).
RN [5]
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 [6]
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 [7]
RP FUNCTION.
RX PubMed=15470097; DOI=10.1099/mic.0.27292-0;
RA Machi K., Azuma M., Igarashi K., Matsumoto T., Fukuda H., Kondo A.,
RA Ooshima H.;
RT "Rot1p of Saccharomyces cerevisiae is a putative membrane protein required
RT for normal levels of the cell wall 1,6-beta-glucan.";
RL Microbiology 150:3163-3173(2004).
RN [8]
RP FUNCTION.
RX PubMed=16874095; DOI=10.4161/auto.3089;
RA Takeuchi M., Kimata Y., Kohno K.;
RT "Causal links between protein folding in the ER and events along the
RT secretory pathway.";
RL Autophagy 2:323-324(2006).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16567426; DOI=10.1093/jb/mvj063;
RA Takeuchi M., Kimata Y., Hirata A., Oka M., Kohno K.;
RT "Saccharomyces cerevisiae Rot1p is an ER-localized membrane protein that
RT may function with BiP/Kar2p in protein folding.";
RL J. Biochem. 139:597-605(2006).
RN [10]
RP FUNCTION.
RX PubMed=17606994; DOI=10.1242/jcs.002758;
RA Juanes M.A., Queralt E., Bano M.C., Igual J.C.;
RT "Rot1 plays an antagonistic role to Clb2 in actin cytoskeleton dynamics
RT throughout the cell cycle.";
RL J. Cell Sci. 120:2390-2401(2007).
RN [11]
RP FUNCTION.
RX PubMed=17397129; DOI=10.1002/yea.1479;
RA Orlowski J., Machula K., Janik A., Zdebska E., Palamarczyk G.;
RT "Dissecting the role of dolichol in cell wall assembly in the yeast mutants
RT impaired in early glycosylation reactions.";
RL Yeast 24:239-252(2007).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND GLYCOSYLATION.
RX PubMed=17914748; DOI=10.1002/yea.1549;
RA Angeles Juanes M., Carlos Igual J., Carmen Bano M.;
RT "Membrane topology and post-translational modification of the Saccharomyces
RT cerevisiae essential protein Rot1.";
RL Yeast 25:93-106(2008).
CC -!- FUNCTION: Required for normal levels of the cell wall 1,6-beta-glucan.
CC Involved in a protein folding machinery chaperoning proteins acting in
CC various physiological processes including cell wall synthesis and lysis
CC of autophagic bodies. Controls actin cytoskeleton polarization to the
CC mother-bud neck and CLB2 protein stability.
CC {ECO:0000269|PubMed:15470097, ECO:0000269|PubMed:16567426,
CC ECO:0000269|PubMed:16874095, ECO:0000269|PubMed:17397129,
CC ECO:0000269|PubMed:17606994, ECO:0000269|PubMed:17914748,
CC ECO:0000269|PubMed:9038344, ECO:0000269|PubMed:9545237}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:14562095, ECO:0000305|PubMed:16567426,
CC ECO:0000305|PubMed:17914748}; Single-pass type I membrane protein
CC {ECO:0000305|PubMed:14562095, ECO:0000305|PubMed:16567426,
CC ECO:0000305|PubMed:17914748}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17914748}.
CC -!- MISCELLANEOUS: Present with 2360 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ROT1 family. {ECO:0000305}.
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DR EMBL; Z48755; CAA88641.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10099.1; -; Genomic_DNA.
DR PIR; S59441; S59441.
DR RefSeq; NP_013927.1; NM_001182707.1.
DR AlphaFoldDB; Q03691; -.
DR BioGRID; 35378; 300.
DR DIP; DIP-2676N; -.
DR IntAct; Q03691; 1.
DR MINT; Q03691; -.
DR STRING; 4932.YMR200W; -.
DR iPTMnet; Q03691; -.
DR PaxDb; Q03691; -.
DR PRIDE; Q03691; -.
DR EnsemblFungi; YMR200W_mRNA; YMR200W; YMR200W.
DR GeneID; 855240; -.
DR KEGG; sce:YMR200W; -.
DR SGD; S000004813; ROT1.
DR VEuPathDB; FungiDB:YMR200W; -.
DR eggNOG; ENOG502QQTG; Eukaryota.
DR HOGENOM; CLU_071622_0_0_1; -.
DR InParanoid; Q03691; -.
DR OMA; PMHPMYL; -.
DR BioCyc; YEAST:G3O-32887-MON; -.
DR PRO; PR:Q03691; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03691; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
DR GO; GO:0006458; P:'de novo' protein folding; IMP:SGD.
DR GO; GO:0007118; P:budding cell apical bud growth; IMP:SGD.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:SGD.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IMP:SGD.
DR GO; GO:0006457; P:protein folding; IGI:SGD.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; IGI:SGD.
DR GO; GO:0006487; P:protein N-linked glycosylation; IGI:SGD.
DR GO; GO:0035269; P:protein O-linked mannosylation; IGI:SGD.
DR InterPro; IPR019623; Rot1.
DR PANTHER; PTHR28090; PTHR28090; 1.
DR Pfam; PF10681; Rot1; 1.
DR PIRSF; PIRSF017290; ROT1_prd; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..256
FT /note="Protein ROT1"
FT /id="PRO_0000203327"
FT TOPO_DOM 25..235
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 186..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17914748"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17914748"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17914748"
SQ SEQUENCE 256 AA; 28908 MW; 58C71DF16296B23C CRC64;
MWSKKFTLKK LILGGYLFAQ KVYCEDESNS IYGTWSSKSN QVFTGPGFYD PVDELLIEPS
LPGLSYSFTE DGWYEEATYQ VSGNPRNPTC PMASLIYQHG TYNISENGTL VLNPIEVDGR
QLFSDPCNDD GVSTYSRYNQ TETFKEYAVG IDPYHGIYTL QLYQYDGTPM QPLYLAYRPP
MMLPTETLNP TSSATSTDDP SSNKKRSLRS LVRRSLENRH KTNAIKRQNT SFLTSNAIWY
ISAGMLGVGS LLFLAF
