LDS1_YEAST
ID LDS1_YEAST Reviewed; 325 AA.
AC P31379; D6VPK0;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Outer spore wall protein LDS1 {ECO:0000305|PubMed:23966878};
DE AltName: Full=Lipid droplets in sporulation protein 1 {ECO:0000303|PubMed:23966878};
GN Name=LDS1 {ECO:0000303|PubMed:23966878};
GN OrderedLocusNames=YAL018C {ECO:0000312|SGD:S000000016}; ORFNames=YAL003;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=1561836; DOI=10.1002/yea.320080208;
RA Clark M.W., Zhong W.-W., Keng T., Storms R.K., Barton A.B., Kaback D.B.,
RA Bussey H.;
RT "Identification of a Saccharomyces cerevisiae homolog of the SNF2
RT transcriptional regulator in the DNA sequence of an 8.6 kb region in the
RT LTE1-CYS1 interval on the left arm of chromosome I.";
RL Yeast 8:133-145(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8458570; DOI=10.1139/g93-005;
RA Ouellette B.F.F., Clark M.W., Keng T., Storms R.K., Zhong W.-W., Zeng B.,
RA Fortin N., Delaney S., Barton A.B., Kaback D.B., Bussey H.;
RT "Sequencing of chromosome I from Saccharomyces cerevisiae: analysis of a 32
RT kb region between the LTE1 and SPO7 genes.";
RL Genome 36:32-42(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [4]
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 [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, 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:24390141}. 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, 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 -!- SIMILARITY: Belongs to the LDS family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L05146; AAC04939.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06970.1; -; Genomic_DNA.
DR PIR; S36731; S36731.
DR RefSeq; NP_009384.1; NM_001178163.1.
DR AlphaFoldDB; P31379; -.
DR BioGRID; 31748; 65.
DR DIP; DIP-2881N; -.
DR IntAct; P31379; 8.
DR MINT; P31379; -.
DR STRING; 4932.YAL018C; -.
DR TCDB; 2.A.121.2.1; the sulfate transporter (cysz) family.
DR PaxDb; P31379; -.
DR PRIDE; P31379; -.
DR EnsemblFungi; YAL018C_mRNA; YAL018C; YAL018C.
DR GeneID; 851215; -.
DR KEGG; sce:YAL018C; -.
DR SGD; S000000016; LDS1.
DR VEuPathDB; FungiDB:YAL018C; -.
DR eggNOG; ENOG502QTNH; Eukaryota.
DR HOGENOM; CLU_062645_2_1_1; -.
DR InParanoid; P31379; -.
DR OMA; YWATITP; -.
DR BioCyc; YEAST:G3O-28830-MON; -.
DR PRO; PR:P31379; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P31379; 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; IGI:SGD.
PE 1: Evidence at protein level;
KW Lipid droplet; Membrane; Reference proteome; Sporulation; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..325
FT /note="Outer spore wall protein LDS1"
FT /id="PRO_0000202413"
FT TOPO_DOM 1..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..118
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..263
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
SQ SEQUENCE 325 AA; 37050 MW; 1C67C7CCA8B0BAA4 CRC64;
MSFTGSLALA GIGGLVYKFG GGQSYEKLPY VNIPFNQYLD KVYKKHFSKV MSRTRYVLMN
FFKDAFTGGA FMYPFKGFLE FNTNKSSYST TMLGILSSYL IMFALVSFVY WATITPMYTA
FLIVLGPIGL FIAIFHSFLQ ANVFTLLFMR LSHFNNHLVE VCLEKNGLEE NLSEVKPIKY
YAPINSIYFW AYYFPFKLVK YMLGLSVLFV LLVISFFPLI GPILFHILIS PFITQIYFTK
VLRLQNFDNI QRRENIYLHA GQYASFGFLA GLIESVPILA GFAISTNTIG SVLFNLDHPM
VPENLVETQA EIEAAPQDIN QQPNQ
