LEM3_YEAST
ID LEM3_YEAST Reviewed; 414 AA.
AC P42838; D6W0M3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Alkylphosphocholine resistance protein LEM3;
DE AltName: Full=Brefeldin-A sensitivity protein 3;
DE AltName: Full=Ro-sensitive 3;
GN Name=LEM3; Synonyms=BRE3, ROS3; OrderedLocusNames=YNL323W; ORFNames=N0333;
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=S288c / FY1676;
RX PubMed=7645347; DOI=10.1002/yea.320110606;
RA Maftahi M., Nicaud J.-M., Levesque H., Gaillardin C.;
RT "Sequencing analysis of a 15.4 kb fragment of yeast chromosome XIV
RT identifies the RPD3, PAS8 and KRE1 loci, five new open reading frames.";
RL Yeast 11:567-572(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
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 [4]
RP CHARACTERIZATION.
RX PubMed=12133835; DOI=10.1074/jbc.m205564200;
RA Kato U., Emoto K., Fredriksson C., Nakamura H., Ohta A., Kobayashi T.,
RA Murakami-Murofushi K., Kobayashi T., Umeda M.;
RT "A novel membrane protein, Ros3p, is required for phospholipid
RT translocation across the plasma membrane in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 277:37855-37862(2002).
RN [5]
RP CHARACTERIZATION.
RX PubMed=12842877; DOI=10.1074/jbc.m305263200;
RA Hanson P.K., Malone L., Birchmore J.L., Nichols J.W.;
RT "Lem3p is essential for the uptake and potency of alkylphosphocholine
RT drugs, edelfosine and miltefosine.";
RL J. Biol. Chem. 278:36041-36050(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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Involved in the asymmetrical organization of
CC phosphatidylethanolamine in the plasma membrane.
CC -!- SUBUNIT: Monomer.
CC -!- INTERACTION:
CC P42838; P32660: DNF1; NbExp=8; IntAct=EBI-28396, EBI-3121;
CC P42838; Q12675: DNF2; NbExp=2; IntAct=EBI-28396, EBI-3114;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: Present with 2460 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CDC50/LEM3 family. {ECO:0000305}.
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DR EMBL; Z46259; CAA86374.1; -; Genomic_DNA.
DR EMBL; Z71599; CAA96254.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10239.1; -; Genomic_DNA.
DR PIR; S55865; S55865.
DR RefSeq; NP_014076.1; NM_001183161.1.
DR PDB; 7DRX; EM; 2.90 A; B=1-414.
DR PDB; 7DSI; EM; 3.21 A; B=1-414.
DR PDB; 7F7F; EM; 3.81 A; B=1-414.
DR PDB; 7KY5; EM; 3.98 A; B=1-414.
DR PDB; 7KY7; EM; 3.08 A; B=1-414.
DR PDB; 7KY8; EM; 3.85 A; B=1-414.
DR PDB; 7KY9; EM; 4.05 A; B=1-414.
DR PDB; 7KYA; EM; 3.50 A; B=1-414.
DR PDB; 7KYB; EM; 3.20 A; B=1-414.
DR PDB; 7KYC; EM; 2.80 A; B=1-414.
DR PDB; 7WHV; EM; 2.80 A; B=1-414.
DR PDB; 7WHW; EM; 3.10 A; B=1-414.
DR PDBsum; 7DRX; -.
DR PDBsum; 7DSI; -.
DR PDBsum; 7F7F; -.
DR PDBsum; 7KY5; -.
DR PDBsum; 7KY7; -.
DR PDBsum; 7KY8; -.
DR PDBsum; 7KY9; -.
DR PDBsum; 7KYA; -.
DR PDBsum; 7KYB; -.
DR PDBsum; 7KYC; -.
DR PDBsum; 7WHV; -.
DR PDBsum; 7WHW; -.
DR AlphaFoldDB; P42838; -.
DR SMR; P42838; -.
DR BioGRID; 35517; 251.
DR ComplexPortal; CPX-1021; DNF1-LEM3 P4-ATPase complex.
DR ComplexPortal; CPX-1022; DNF2-LEM3 P4-ATPase complex.
DR DIP; DIP-4598N; -.
DR IntAct; P42838; 17.
DR MINT; P42838; -.
DR STRING; 4932.YNL323W; -.
DR TCDB; 8.A.27.1.1; the cdc50 p-type atpase lipid flippase subunit (cdc50) family.
DR iPTMnet; P42838; -.
DR MaxQB; P42838; -.
DR PaxDb; P42838; -.
DR PRIDE; P42838; -.
DR EnsemblFungi; YNL323W_mRNA; YNL323W; YNL323W.
DR GeneID; 855393; -.
DR KEGG; sce:YNL323W; -.
DR SGD; S000005267; LEM3.
DR VEuPathDB; FungiDB:YNL323W; -.
DR eggNOG; KOG2952; Eukaryota.
DR GeneTree; ENSGT00390000004660; -.
DR HOGENOM; CLU_025025_0_1_1; -.
DR InParanoid; P42838; -.
DR OMA; TARPPYW; -.
DR BioCyc; YEAST:G3O-33308-MON; -.
DR PRO; PR:P42838; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P42838; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; IPI:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0140331; P:aminophospholipid translocation; IEA:GOC.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IMP:SGD.
DR GO; GO:0045332; P:phospholipid translocation; IMP:SGD.
DR GO; GO:0044088; P:regulation of vacuole organization; IGI:SGD.
DR InterPro; IPR005045; CDC50/LEM3_fam.
DR PANTHER; PTHR10926; PTHR10926; 1.
DR Pfam; PF03381; CDC50; 1.
DR PIRSF; PIRSF015840; DUF284_TM_euk; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..414
FT /note="Alkylphosphocholine resistance protein LEM3"
FT /id="PRO_0000207671"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 20..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT HELIX 37..43
FT /evidence="ECO:0007829|PDB:7KYC"
FT TURN 57..61
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 72..98
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:7KYC"
FT TURN 108..113
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 157..167
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 173..181
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 205..209
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 245..251
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 267..271
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:7KYC"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:7KYC"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:7KYC"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 309..314
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 319..332
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 337..345
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 356..362
FT /evidence="ECO:0007829|PDB:7KYC"
FT STRAND 366..369
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 373..399
FT /evidence="ECO:0007829|PDB:7KYC"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:7KY7"
FT HELIX 410..413
FT /evidence="ECO:0007829|PDB:7KYC"
SQ SEQUENCE 414 AA; 47438 MW; 55BDA1F32251B4E6 CRC64;
MVNFDLGQVG EVFRRKDKGA IVSGDNPEEE EDVDASEFEE DEVKPVRTKN RRPKEDAFTQ
QRLAAINPVL TPRTVLPLYL LIAVVFVIVG GCILAQNSKV DEVTIYYQDC MTNATSSWSD
IPSEHWQFVF HKYKTYNTAP QWRFVDDESD DFTKQRGTCQ IRFTTPSDMK NNVYLNYVLE
KFAANHRRYV LSFSEDQIRG EDASYETVHD ATGINCKPLS KNADGKIYYP CGLIANSMFN
DTFPLQLTNV GDTSNNYSLT NKGINWESDK KRYKKTKYNY TQIAPPPYWE KMYPDGYNET
NIPDIQDWEE FQNWMRPGAF DKITKLIRIN KNDTLPAGEY QLDIGLHWPV LEFNGKKGIY
LTHGSHLGGR NPFLGIVYLI GGCICAAMAL ILLTFWLFGG RKIADASSLS WNMK
