LDS2_YEAST
ID LDS2_YEAST Reviewed; 356 AA.
AC Q08218; D6W220;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Outer spore wall protein LDS2 {ECO:0000305|PubMed:23966878};
DE AltName: Full=Lipid droplets in sporulation protein 2 {ECO:0000303|PubMed:23966878};
GN Name=LDS2 {ECO:0000303|PubMed:23966878};
GN OrderedLocusNames=YOL047C {ECO:0000312|SGD:S000005407};
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 REVISION OF GENE MODEL.
RX PubMed=10734188; DOI=10.1093/nar/28.8.1700;
RA Davis C.A., Grate L., Spingola M., Ares M. Jr.;
RT "Test of intron predictions reveals novel splice sites, alternatively
RT spliced mRNAs and new introns in meiotically regulated genes of yeast.";
RL Nucleic Acids Res. 28:1700-1706(2000).
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 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 [6]
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).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=24390141; DOI=10.1128/ec.00333-13;
RA Lam C., Santore E., Lavoie E., Needleman L., Fiacco N., Kim C.,
RA Neiman A.M.;
RT "A visual screen of protein localization during sporulation identifies new
RT components of prospore membrane-associated complexes in budding yeast.";
RL Eukaryot. Cell 13:383-391(2014).
CC -!- FUNCTION: Involved in spore wall assembly.
CC {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, ECO:0000269|PubMed:23966878,
CC ECO:0000269|PubMed:24390141}. Spore wall {ECO:0000269|PubMed:23966878}.
CC Note=Localizes to the ascal side of growing prospore membranes in mid-
CC meiosis II and to the spore wall in post-meiotic cells. Localizes to a
CC specific subset of lipid droplets associated with the exterior surface
CC of the spore throughout spore wall formation.
CC {ECO:0000269|PubMed:23966878, ECO:0000269|PubMed:24390141}.
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 -!- MISCELLANEOUS: Present with 155 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the LDS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA99052.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z74789; CAA99052.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BK006948; DAA10736.1; -; Genomic_DNA.
DR PIR; S66732; S66732.
DR RefSeq; NP_014595.2; NM_001183301.1.
DR AlphaFoldDB; Q08218; -.
DR BioGRID; 34356; 95.
DR STRING; 4932.YOL047C; -.
DR TCDB; 2.A.121.2.5; the sulfate transporter (cysz) family.
DR PaxDb; Q08218; -.
DR PRIDE; Q08218; -.
DR EnsemblFungi; YOL047C_mRNA; YOL047C; YOL047C.
DR GeneID; 854110; -.
DR KEGG; sce:YOL047C; -.
DR SGD; S000005407; LDS2.
DR VEuPathDB; FungiDB:YOL047C; -.
DR HOGENOM; CLU_066715_0_0_1; -.
DR InParanoid; Q08218; -.
DR OMA; CHEVRRD; -.
DR BioCyc; YEAST:G3O-33460-MON; -.
DR PRO; PR:Q08218; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08218; protein.
DR GO; GO:0005619; C:ascospore wall; IDA:SGD.
DR GO; GO:0005633; C:ascus lipid droplet; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA: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; IGI:SGD.
PE 1: Evidence at protein level;
KW Lipid droplet; Membrane; Reference proteome; Sporulation; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..356
FT /note="Outer spore wall protein LDS2"
FT /id="PRO_0000235923"
FT TOPO_DOM 1..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P31379"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..115
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P31379"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P31379"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..294
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P31379"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..356
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P31379"
FT REGION 322..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..338
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 356 AA; 40878 MW; B4D2F6425E8B7539 CRC64;
MSTRPQPDWY YHRHPYASTP LAEGEEPQLL PIQDQGNHKK SKIWMAYKAP IVRWYKNAML
VKDNFWKDLE SSHQIIWYPY KGISESVGNS DYLHLFFLIF GYYLLNLLLI VAFTSILAWS
LLVCIYLPFL GLFALPLAYM QTILISTTLC NSMVKGTDFV LFTRIYGVTF ARKGLTELSE
ACETISFTPF VYRRSHRLGG LFSKRFYLVS LPQFFIFFFW YIFIAFMFLL LLLVPIVGPI
TINMLPFSPG MGFYYFEPYF VDVLHLDSRK LSKVYYKGFA KWLLYSISSG LLESIPILGG
LFIGTNAVGA SLWIVKEIKD RDQPAVPPSP PAEPEEPTVG SYAPPIQQSI AHINPP
