RRT8_YEAST
ID RRT8_YEAST Reviewed; 342 AA.
AC Q08219; D6W219; Q870H5;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Outer spore wall protein RRT8 {ECO:0000305|PubMed:23966878};
DE AltName: Full=Regulator of rDNA transcription protein 8 {ECO:0000303|PubMed:19270272};
GN Name=RRT8 {ECO:0000303|PubMed:19270272};
GN OrderedLocusNames=YOL048C {ECO:0000312|SGD:S000005408};
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=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-310.
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA Gates K., Gaffney T.D., Philippsen P.;
RT "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT comparison to the genome of a related fungus: Ashbya gossypii.";
RL Genome Biol. 4:R45.1-R45.13(2003).
RN [4]
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 [5]
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 [6]
RP FUNCTION.
RX PubMed=19270272; DOI=10.1534/genetics.108.100313;
RA Hontz R.D., Niederer R.O., Johnson J.M., Smith J.S.;
RT "Genetic identification of factors that modulate ribosomal DNA
RT transcription in Saccharomyces cerevisiae.";
RL Genetics 182:105-119(2009).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=23966878; DOI=10.1371/journal.pgen.1003700;
RA Lin C.P., Kim C., Smith S.O., Neiman A.M.;
RT "A highly redundant gene network controls assembly of the outer spore wall
RT in S. cerevisiae.";
RL PLoS Genet. 9:E1003700-E1003700(2013).
CC -!- FUNCTION: Involved in spore wall assembly (PubMed:23966878). May be
CC involved in the modulation of rDNA transcription (PubMed:19270272).
CC {ECO:0000269|PubMed:19270272, ECO:0000269|PubMed:23966878}.
CC -!- SUBCELLULAR LOCATION: Prospore membrane {ECO:0000269|PubMed:23966878};
CC Multi-pass membrane protein {ECO:0000255}. Lipid droplet
CC {ECO:0000269|PubMed:14562095}. Spore wall
CC {ECO:0000269|PubMed:23966878}. Note=Localizes to the ascal side of
CC growing prospore membranes in mid-meiosis II and to the spore wall in
CC post-meiotic cells. Localizes to a specific subset of lipid droplets
CC associated with the exterior surface of the spore throughout spore wall
CC formation. {ECO:0000269|PubMed:23966878}.
CC -!- DISRUPTION PHENOTYPE: A combined deletion of the LDS proteins RRT8,
CC LDS1 and LDS2 fails to incorporate dityrosine and another yet
CC uncharacterized component in the outer spore wall.
CC {ECO:0000269|PubMed:23966878}.
CC -!- SIMILARITY: Belongs to the LDS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA99053.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z74790; CAA99053.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY245791; AAP04341.1; -; mRNA.
DR EMBL; BK006948; DAA10735.1; -; Genomic_DNA.
DR PIR; S66733; S66733.
DR RefSeq; NP_014594.2; NM_001183302.1.
DR AlphaFoldDB; Q08219; -.
DR BioGRID; 34355; 41.
DR DIP; DIP-49894N; -.
DR IntAct; Q08219; 1.
DR STRING; 4932.YOL048C; -.
DR TCDB; 2.A.121.2.2; the sulfate transporter (cysz) family.
DR MaxQB; Q08219; -.
DR PaxDb; Q08219; -.
DR PRIDE; Q08219; -.
DR EnsemblFungi; YOL048C_mRNA; YOL048C; YOL048C.
DR GeneID; 854109; -.
DR KEGG; sce:YOL048C; -.
DR SGD; S000005408; RRT8.
DR VEuPathDB; FungiDB:YOL048C; -.
DR eggNOG; ENOG502QVX4; Eukaryota.
DR HOGENOM; CLU_062645_2_0_1; -.
DR InParanoid; Q08219; -.
DR OMA; YLYPFKG; -.
DR BioCyc; YEAST:G3O-33461-MON; -.
DR PRO; PR:Q08219; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08219; protein.
DR GO; GO:0005619; C:ascospore wall; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; HDA:SGD.
DR GO; GO:0005628; C:prospore membrane; IDA:SGD.
DR GO; GO:0030476; P:ascospore wall assembly; IMP:SGD.
PE 1: Evidence at protein level;
KW Lipid droplet; Membrane; Reference proteome; Sporulation; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..342
FT /note="Outer spore wall protein RRT8"
FT /id="PRO_0000203488"
FT TOPO_DOM 1..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..299
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..342
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT CONFLICT 138
FT /note="T -> A (in Ref. 3; AAP04341)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 342 AA; 39600 MW; E35FCAD9CEC59A58 CRC64;
MKAGIELISH SQASHATYAN SMTLAEKGPQ RLKRQFKEHS SSKESNVSRW LKIFIRQFDI
WFPETIPTMK VRYELLRKNF IKEIFNSRAF IYPFLGFYEV LTNPVYWKHI LLFAVCYALI
FVTIAGLFYV TLVPLLVTWA ILLLGPLGVI LVHIQWILQT NVLTAFVCRT LVLTHITNQI
FDISLVLQDQ DEFLNEVKVL PKPQKPHRKI DEPDAVRNFN TIKGSRIFKI PRLLFRMFFK
VSNFTSLTLL SLIPIVGPIL ANQLMAPKRT FTYLQRYFLL KGFSKKQAKD FQYEHYASFI
CFGMSAGLLE LIPFFTIVTI SSNTVGAAKW CTSLLKGERK KE
