SEI1_YEAST
ID SEI1_YEAST Reviewed; 285 AA.
AC Q06058; D6VZ37;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Seipin {ECO:0000305|PubMed:18250201};
DE AltName: Full=Few lipid droplets protein 1 {ECO:0000303|PubMed:18250201};
GN Name=SEI1 {ECO:0000303|PubMed:21829381};
GN Synonyms=FLD1 {ECO:0000303|PubMed:18250201};
GN OrderedLocusNames=YLR404W {ECO:0000312|SGD:S000004396};
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 INDUCTION.
RX PubMed=12161108; DOI=10.1016/s0143-4160(02)00110-0;
RA Lombardia L.J., Becerra M., Rodriguez-Belmonte E., Hauser N.C.,
RA Cerdan M.E.;
RT "Genome-wide analysis of yeast transcription upon calcium shortage.";
RL Cell Calcium 32:83-91(2002).
RN [4]
RP TOPOLOGY.
RX PubMed=12524434; DOI=10.1074/jbc.m300163200;
RA Kim H., Melen K., von Heijne G.;
RT "Topology models for 37 Saccharomyces cerevisiae membrane proteins based on
RT C-terminal reporter fusions and predictions.";
RL J. Biol. Chem. 278:10208-10213(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 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 [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18093937; DOI=10.1073/pnas.0704154104;
RA Szymanski K.M., Binns D., Bartz R., Grishin N.V., Li W.-P., Agarwal A.K.,
RA Garg A., Anderson R.G.W., Goodman J.M.;
RT "The lipodystrophy protein seipin is found at endoplasmic reticulum lipid
RT droplet junctions and is important for droplet morphology.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:20890-20895(2007).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18250201; DOI=10.1083/jcb.200711136;
RA Fei W., Shui G., Gaeta B., Du X., Kuerschner L., Li P., Brown A.J.,
RA Wenk M.R., Parton R.G., Yang H.;
RT "Fld1p, a functional homologue of human seipin, regulates the size of lipid
RT droplets in yeast.";
RL J. Cell Biol. 180:473-482(2008).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=21829381; DOI=10.1371/journal.pgen.1002201;
RA Fei W., Shui G., Zhang Y., Krahmer N., Ferguson C., Kapterian T.S.,
RA Lin R.C., Dawes I.W., Brown A.J., Li P., Huang X., Parton R.G., Wenk M.R.,
RA Walther T.C., Yang H.;
RT "A role for phosphatidic acid in the formation of 'supersized' lipid
RT droplets.";
RL PLoS Genet. 7:E1002201-E1002201(2011).
RN [10]
RP FUNCTION.
RX PubMed=25540432; DOI=10.1091/mbc.e14-08-1303;
RA Cartwright B.R., Binns D.D., Hilton C.L., Han S., Gao Q., Goodman J.M.;
RT "Seipin performs dissectible functions in promoting lipid droplet
RT biogenesis and regulating droplet morphology.";
RL Mol. Biol. Cell 26:726-739(2015).
CC -!- FUNCTION: Involved in lipid metabolism and lipid droplet (LD)
CC morphology, number, and size (PubMed:18093937, PubMed:18250201).
CC Facilitates initiation of LD formation, and ensures that vectorial
CC budding of LDs from the ER is directed towards the cytoplasm
CC (PubMed:25540432). {ECO:0000269|PubMed:18093937,
CC ECO:0000269|PubMed:18250201, ECO:0000269|PubMed:25540432}.
CC -!- INTERACTION:
CC Q06058; P25587: LDB16; NbExp=7; IntAct=EBI-35851, EBI-21668;
CC Q06058; Q06058: SEI1; NbExp=2; IntAct=EBI-35851, EBI-35851;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18093937, ECO:0000269|PubMed:18250201}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:18093937,
CC ECO:0000269|PubMed:18250201}. Note=Concentrates at endoplasmic
CC reticulum lipid droplet junctions. {ECO:0000269|PubMed:18093937}.
CC -!- INDUCTION: By calcium shortage. {ECO:0000269|PubMed:12161108}.
CC -!- DISRUPTION PHENOTYPE: Produces supersized LDs that are up to 50 times
CC the volume of those in wild-type cells. {ECO:0000269|PubMed:21829381}.
CC -!- MISCELLANEOUS: Present with 846 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the seipin family. {ECO:0000305}.
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DR EMBL; U19729; AAB82342.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09703.1; -; Genomic_DNA.
DR PIR; S55960; S55960.
DR RefSeq; NP_013508.3; NM_001182292.3.
DR PDB; 7RSL; EM; 3.45 A; A/B/C/D/E/F/G/H/I/J=1-285.
DR PDBsum; 7RSL; -.
DR AlphaFoldDB; Q06058; -.
DR SMR; Q06058; -.
DR BioGRID; 31661; 272.
DR ComplexPortal; CPX-3342; Seipin complex.
DR IntAct; Q06058; 6.
DR MINT; Q06058; -.
DR STRING; 4932.YLR404W; -.
DR MaxQB; Q06058; -.
DR PaxDb; Q06058; -.
DR PRIDE; Q06058; -.
DR EnsemblFungi; YLR404W_mRNA; YLR404W; YLR404W.
DR GeneID; 851120; -.
DR KEGG; sce:YLR404W; -.
DR SGD; S000004396; SEI1.
DR VEuPathDB; FungiDB:YLR404W; -.
DR eggNOG; ENOG502S0BA; Eukaryota.
DR HOGENOM; CLU_061225_0_0_1; -.
DR InParanoid; Q06058; -.
DR OMA; KIFHTSR; -.
DR BioCyc; YEAST:G3O-32466-MON; -.
DR PRO; PR:Q06058; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06058; protein.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:ComplexPortal.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0005811; C:lipid droplet; IDA:ComplexPortal.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0140042; P:lipid droplet formation; IMP:SGD.
DR GO; GO:0034389; P:lipid droplet organization; IMP:SGD.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0090155; P:negative regulation of sphingolipid biosynthetic process; IMP:SGD.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IMP:SGD.
DR GO; GO:0008104; P:protein localization; IMP:SGD.
DR GO; GO:1990044; P:protein localization to lipid droplet; IMP:ComplexPortal.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IC:ComplexPortal.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Lipid metabolism; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..285
FT /note="Seipin"
FT /id="PRO_0000247216"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:12524434,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..244
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:12524434,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..285
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:12524434,
FT ECO:0000269|PubMed:16847258"
SQ SEQUENCE 285 AA; 32590 MW; 3966CB0967B7B62B CRC64;
MKINVSRPLQ FLQWSSYIVV AFLIQLLIIL PLSILIYHDF YLRLLPADSS NVVPLNTFNI
LNGVQFGTKF FQSIKSIPVG TDLPQTIDNG LSQLIPMRDN MEYKLDLNLQ LYCQSKTDHL
NLDNLLIDVY RGPGPLLGAP GGSNSKDEKI FHTSRPIVCL ALTDSMSPQE IEQLGPSRLD
VYDEEWLNTI RIEDKISLES SYETISVFLK TEIAQRNLII HPESGIKFRM NFEQGLRNLM
LRKRFLSYII GISIFHCIIC VLFFITGCTA FIFVRKGQEK SKKHS
