ID   LMO1_YEAST              Reviewed;         665 AA.
AC   Q07799; D6VXZ5; E9PAG4;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=ELMO family protein LMO1 {ECO:0000303|PubMed:25598154};
GN   Name=LMO1 {ECO:0000303|PubMed:25598154}; OrderedLocusNames=YLL007C;
GN   ORFNames=L1353;
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 90840 / EAY235 / FY23;
RX   PubMed=8810043;
RX   DOI=10.1002/(sici)1097-0061(19960615)12:7<693::aid-yea956>3.0.co;2-g;
RA   Miosga T., Zimmermann F.K.;
RT   "Sequence analysis of the CEN12 region of Saccharomyces cerevisiae on a
RT   43.7 kb fragment of chromosome XII including an open reading frame
RT   homologous to the human cystic fibrosis transmembrane conductance regulator
RT   protein CFTR.";
RL   Yeast 12:693-708(1996).
RN   [2]
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   [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   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   INTERACTION WITH DCK1, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP   FUNCTION.
RX   PubMed=25598154; DOI=10.1111/mmi.12937;
RA   Schmitz H.P., Jendretzki A., Wittland J., Wiechert J., Heinisch J.J.;
RT   "Identification of Dck1 and Lmo1 as upstream regulators of the small GTPase
RT   Rho5 in Saccharomyces cerevisiae.";
RL   Mol. Microbiol. 96:306-324(2015).
CC   -!- FUNCTION: Forms a transiant heterodimeric complex with DCK1, that acts
CC       as a guanine nucleotide exchange factor (GEF) for the small GTPase RHO5
CC       (PubMed:25598154). DCK1, LMO1 and RHO5 relocate to mitochondria upon
CC       oxidative stress and trigger cell death (PubMed:25598154). The
CC       DCK1/LMO1/RHO5 signaling module mediates mitochondrial turnover under
CC       nitrogen starvation conditions via mitophagy (PubMed:25598154). The
CC       DCK1/LMO1/RHO5 signaling module also plays a role in cell wall
CC       integrity signaling (PubMed:25598154). {ECO:0000269|PubMed:25598154}.
CC   -!- SUBUNIT: Forms an active heterodimer with DCK1.
CC       {ECO:0000269|PubMed:25598154}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC       Mitochondrion {ECO:0000269|PubMed:25598154}. Note=Quickly relocates to
CC       mitochondria under oxidative stress. {ECO:0000269|PubMed:25598154}.
CC   -!- DISRUPTION PHENOTYPE: Leads to hyper-resistance to cell wall stress
CC       agents such as calcofluor white and Congo red.
CC       {ECO:0000269|PubMed:25598154}.
CC   -!- MISCELLANEOUS: Present with 486 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; X91488; CAA62762.1; -; Genomic_DNA.
DR   EMBL; Z73111; CAA97450.1; -; Genomic_DNA.
DR   EMBL; Z73112; CAA97451.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09311.1; -; Genomic_DNA.
DR   PIR; S64749; S64749.
DR   RefSeq; NP_013094.1; NM_001181827.1.
DR   AlphaFoldDB; Q07799; -.
DR   BioGRID; 31244; 89.
DR   IntAct; Q07799; 5.
DR   MINT; Q07799; -.
DR   STRING; 4932.YLL007C; -.
DR   iPTMnet; Q07799; -.
DR   MaxQB; Q07799; -.
DR   PaxDb; Q07799; -.
DR   PRIDE; Q07799; -.
DR   EnsemblFungi; YLL007C_mRNA; YLL007C; YLL007C.
DR   GeneID; 850653; -.
DR   KEGG; sce:YLL007C; -.
DR   SGD; S000003930; YLL007C.
DR   VEuPathDB; FungiDB:YLL007C; -.
DR   eggNOG; ENOG502R0G6; Eukaryota.
DR   HOGENOM; CLU_425916_0_0_1; -.
DR   InParanoid; Q07799; -.
DR   OMA; ICHISRE; -.
DR   BioCyc; YEAST:G3O-32112-MON; -.
DR   PRO; PR:Q07799; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q07799; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IMP:SGD.
DR   GO; GO:0048870; P:cell motility; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IMP:SGD.
DR   InterPro; IPR001849; PH_domain.
DR   Pfam; PF16457; PH_12; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Mitochondrion; Reference proteome.
FT   CHAIN           1..665
FT                   /note="ELMO family protein LMO1"
FT                   /id="PRO_0000247098"
SQ   SEQUENCE   665 AA;  76622 MW;  8BA33E7EB0EA191A CRC64;
     MKHNRQMPDE SLENIKVLLN PKLGKPVKSL TSAQSKACYH TLISNKNLNK TSDEYEKLLA
     NYILLCDEKY LCKTVIPDSR FWAILCDNCQ KLRSETLVAN LIRIFNVALK CQDSNKNEVI
     VSICHISREN SQLIGILLQL LSQRPIHIPL FTDTILCITL FLKCSLTLCE TSLSHAVEFV
     PRILILLFQY NFPASMSELL YIEDLQPLIL EEFVPLKQRL INFLSSVSID DYSCSLKADL
     LTAIKDNSVF QKGLEMEMGD LPSINLLNAY DTFTFLNSPN GSFKRLYTEQ LLFGENDFPL
     YEAIFKLSDQ FRRLFNLSGK KENQYSDSER DLKLQIATAV LNRQTCFYKT LELFLRFWIE
     SLAKSQSDLV SLLNLAIITL KYVCLSSSDL EAAIQTKSLL KTQVVALDSM RYKFARTLQL
     DSIKKEQYRT WSSSIASFDT MLSGQVRDYV RHQRLLQLQK GTWVYAENPL NPEAGTPKVY
     FLIVSDNHAN LLAREFETQT NDLPYLFDNK ILTSPGSEAL ANGRTKVVVL KHITSFKSIE
     LTTPSRRTSS NVYIKLDEAN VYTGVELKDR NDRTVLKFYL DTEEGRYIWL DGLKLISPFQ
     HEDISEDTKE QIDTLFDLRK NVQMINLNVR QDIIVPPPEP SDEDEDEEFY NLETLKKVTQ
     NFYFD