LAM6_YEAST
ID LAM6_YEAST Reviewed; 693 AA.
AC Q08001; D6VY73;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Membrane-anchored lipid-binding protein LAM6 {ECO:0000303|PubMed:26001273};
DE AltName: Full=Lipid transfer at contact site protein 1 {ECO:0000303|PubMed:25987606};
DE AltName: Full=Lipid transfer protein anchored at membrane contact sites 1 {ECO:0000303|PubMed:26001273};
GN Name=LAM6 {ECO:0000303|PubMed:26001273};
GN Synonyms=LTC1 {ECO:0000303|PubMed:25987606};
GN OrderedLocusNames=YLR072W {ECO:0000312|SGD:S000004062};
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 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594 AND SER-597, AND
RP IDENTIFICATION BY 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-343 AND SER-591, AND
RP IDENTIFICATION BY 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-343; SER-591; THR-593;
RP SER-594 AND SER-597, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=26119743; DOI=10.1016/j.celrep.2015.06.022;
RA Elbaz-Alon Y., Eisenberg-Bord M., Shinder V., Stiller S.B., Shimoni E.,
RA Wiedemann N., Geiger T., Schuldiner M.;
RT "Lam6 regulates the extent of contacts between organelles.";
RL Cell Rep. 12:7-14(2015).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26001273; DOI=10.7554/elife.07253;
RA Gatta A.T., Wong L.H., Sere Y.Y., Calderon-Norena D.M., Cockcroft S.,
RA Menon A.K., Levine T.P.;
RT "A new family of StART domain proteins at membrane contact sites has a role
RT in ER-PM sterol transport.";
RL Elife 4:E07253-E07253(2015).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25987606; DOI=10.1083/jcb.201502033;
RA Murley A., Sarsam R.D., Toulmay A., Yamada J., Prinz W.A., Nunnari J.;
RT "Ltc1 is an ER-localized sterol transporter and a component of ER-
RT mitochondria and ER-vacuole contacts.";
RL J. Cell Biol. 209:539-548(2015).
CC -!- FUNCTION: Involved in regulation of various organellar membrane contact
CC sites (PubMed:26119743). May be involved in sterol transfer between
CC intracellular membranes (PubMed:26001273). Selectively transports
CC sterols between membranes in vitro. Involved in stress-dependent
CC formation of sterol-enriched vacuolar membrane domains
CC (PubMed:25987606). {ECO:0000269|PubMed:25987606,
CC ECO:0000269|PubMed:26001273, ECO:0000269|PubMed:26119743}.
CC -!- SUBUNIT: Interacts with the ERMES complex.
CC {ECO:0000269|PubMed:26119743}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:26001273}; Single-pass membrane protein
CC {ECO:0000255}. Note=Localizes to intracellular puncta representing
CC endoplasmic reticulum-mitochondrion membrane contact sites (ERMES),
CC nucleus-vacuole junctions (NVJ) and vacuole-mitochondria patches
CC (vCLAMP) (PubMed:14562095, PubMed:26119743, PubMed:26001273,
CC PubMed:25987606). Localization to ER-mitochondria contacts is dependent
CC on TOM70/TOM71, and localization to ER-vacuole junctions on VAC8
CC (PubMed:25987606). {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:25987606, ECO:0000269|PubMed:26001273,
CC ECO:0000269|PubMed:26119743}.
CC -!- DOMAIN: The VASt domain bind sterols. {ECO:0000250|UniProtKB:P38800}.
CC -!- SIMILARITY: Belongs to the YSP2 family. {ECO:0000305}.
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DR EMBL; Z73244; CAA97629.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09389.1; -; Genomic_DNA.
DR PIR; S64904; S64904.
DR RefSeq; NP_013173.1; NM_001181959.1.
DR PDB; 5YQR; X-ray; 2.40 A; A=161-272.
DR PDBsum; 5YQR; -.
DR AlphaFoldDB; Q08001; -.
DR SMR; Q08001; -.
DR BioGRID; 31346; 94.
DR DIP; DIP-1861N; -.
DR IntAct; Q08001; 9.
DR MINT; Q08001; -.
DR STRING; 4932.YLR072W; -.
DR TCDB; 9.B.198.2.4; the membrane-anchored lipid-binding protein (lam) family.
DR iPTMnet; Q08001; -.
DR MaxQB; Q08001; -.
DR PaxDb; Q08001; -.
DR PRIDE; Q08001; -.
DR EnsemblFungi; YLR072W_mRNA; YLR072W; YLR072W.
DR GeneID; 850761; -.
DR KEGG; sce:YLR072W; -.
DR SGD; S000004062; LAM6.
DR VEuPathDB; FungiDB:YLR072W; -.
DR eggNOG; KOG1032; Eukaryota.
DR GeneTree; ENSGT00940000176474; -.
DR HOGENOM; CLU_015638_1_0_1; -.
DR InParanoid; Q08001; -.
DR OMA; RISYWIT; -.
DR BioCyc; YEAST:G3O-32224-MON; -.
DR PRO; PR:Q08001; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q08001; protein.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0140268; C:endoplasmic reticulum-plasma membrane contact site; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0071561; C:nucleus-vacuole junction; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:1990816; C:vacuole-mitochondrion membrane contact site; IDA:SGD.
DR GO; GO:0032934; F:sterol binding; IBA:GO_Central.
DR GO; GO:0120015; F:sterol transfer activity; IDA:SGD.
DR GO; GO:0032366; P:intracellular sterol transport; IDA:SGD.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR031968; VASt.
DR Pfam; PF02893; GRAM; 1.
DR Pfam; PF16016; VASt; 1.
DR SMART; SM00568; GRAM; 1.
DR PROSITE; PS51778; VAST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..693
FT /note="Membrane-anchored lipid-binding protein LAM6"
FT /id="PRO_0000247247"
FT TOPO_DOM 1..630
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 631..651
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 652..693
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 164..230
FT /note="GRAM"
FT /evidence="ECO:0000255"
FT DOMAIN 403..576
FT /note="VASt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01114"
FT REGION 340..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 343
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 593
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT HELIX 161..169
FT /evidence="ECO:0007829|PDB:5YQR"
FT STRAND 179..208
FT /evidence="ECO:0007829|PDB:5YQR"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:5YQR"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:5YQR"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:5YQR"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:5YQR"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:5YQR"
FT HELIX 254..267
FT /evidence="ECO:0007829|PDB:5YQR"
SQ SEQUENCE 693 AA; 78212 MW; FACE2F16326B36F6 CRC64;
MWGDSMRELG DAMDNELNAV KPVVEEGGMD GARKFIKGKS FQKSSTEHML ISPGRDGSVP
LNGLKSSPAD PHLSDVNSIL DNHRGGGETA LTSVNNIIMA TSTNGDSDGV DGDAKRPSIS
NCSSRSSFFD TVLSTFSLKS NSQDTVTNEV KNIEVQFASE EANKKFRQMF KPLAPNTRLI
TDYFCYFHRE FPYQGRIYLS NTHLCFNSTV LNWMAKLQIP LNEIKYLDKV TTNSSAISVE
TVTNRYTFSG FIARDEVFQL ITRVWSKENL TNINDVLEVD ERVSKKKGIS STPSSIFNNV
STNAYNDFIS TTTTEPTSRA SYMSENDMLI EEAIRSVDDY MGTPRASPSS SSSSSSSSSS
LGSSTTYYCR PVYRLKPNAP FQYEGPFHVQ ETMDFPYKPE ANNEYVLLER QFSVPPGLLF
IMMFNEDNPV FELSFLKTQD SSNISHIGTF EKVNKDGQHY REFQYTKQLH FPVGPKSTNC
EVAEILLHCD WERYINVLSI TRTPNVPSGT SFSTRTRYMF RWDDQGQGCI LKISFWVDWN
ASSWIKPMVE SNCKNGQISA TKDLVKLVEE FVEKYVELSK EKADTLKPLP SVTSFGSPRK
VAAPELTMVQ PESKPEAEAE ISEIGSDRWR FNWVNIIILV LLVLNLLYLM KLNKKMDKLT
NLMTHKDEVV AHATLLDIPA KVQWSRPRRG DVL
