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Membrane-anchored lipid-binding protein LAM6 (Lipid transfer at contact site protein 1) (Lipid transfer protein anchored at membrane contact sites 1)

 LAM6_YEAST              Reviewed;         693 AA.
Q08001; D6VY73;
25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 126.
RecName: Full=Membrane-anchored lipid-binding protein LAM6 {ECO:0000303|PubMed:26001273};
AltName: Full=Lipid transfer at contact site protein 1 {ECO:0000303|PubMed:25987606};
AltName: Full=Lipid transfer protein anchored at membrane contact sites 1 {ECO:0000303|PubMed:26001273};
Name=LAM6 {ECO:0000303|PubMed:26001273};
Synonyms=LTC1 {ECO:0000303|PubMed:25987606};
OrderedLocusNames=YLR072W {ECO:0000312|SGD:S000004062};
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594 AND SER-597, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-343 AND SER-591, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-343; SER-591; THR-593;
SER-594 AND SER-597, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=26119743; DOI=10.1016/j.celrep.2015.06.022;
Elbaz-Alon Y., Eisenberg-Bord M., Shinder V., Stiller S.B.,
Shimoni E., Wiedemann N., Geiger T., Schuldiner M.;
"Lam6 regulates the extent of contacts between organelles.";
Cell Rep. 12:7-14(2015).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=26001273; DOI=10.7554/eLife.07253;
Gatta A.T., Wong L.H., Sere Y.Y., Calderon-Norena D.M., Cockcroft S.,
Menon A.K., Levine T.P.;
"A new family of StART domain proteins at membrane contact sites has a
role in ER-PM sterol transport.";
Elife 4:E07253-E07253(2015).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=25987606; DOI=10.1083/jcb.201502033;
Murley A., Sarsam R.D., Toulmay A., Yamada J., Prinz W.A., Nunnari J.;
"Ltc1 is an ER-localized sterol transporter and a component of ER-
mitochondria and ER-vacuole contacts.";
J. Cell Biol. 209:539-548(2015).
-!- FUNCTION: Involved in regulation of various organellar membrane
contact sites (PubMed:26119743). May be involved in sterol
transfer between intracellular membranes (PubMed:26001273).
Selectively transports sterols between membranes in vitro.
Involved in stress-dependent formation of sterol-enriched vacuolar
membrane domains (PubMed:25987606). {ECO:0000269|PubMed:25987606,
ECO:0000269|PubMed:26001273, ECO:0000269|PubMed:26119743}.
-!- SUBUNIT: Interacts with the ERMES complex.
{ECO:0000269|PubMed:26119743}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:26001273}; Single-pass membrane protein
{ECO:0000255}. Note=Localizes to intracellular puncta representing
endoplasmic reticulum-mitochondrion membrane contact sites
(ERMES), nucleus-vacuole junctions (NVJ) and vacuole-mitochondria
patches (vCLAMP) (PubMed:14562095, PubMed:26119743,
PubMed:26001273, PubMed:25987606). Localization to ER-mitochondria
contacts is dependent on TOM70/TOM71, and localisation to ER-
vacuole junctions on VAC8 (PubMed:25987606).
{ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:25987606,
ECO:0000269|PubMed:26001273, ECO:0000269|PubMed:26119743}.
-!- DOMAIN: The VASt domain bind sterols.
{ECO:0000250|UniProtKB:P38800}.
-!- SIMILARITY: Belongs to the YSP2 family. {ECO:0000305}.
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EMBL; Z73244; CAA97629.1; -; Genomic_DNA.
EMBL; BK006945; DAA09389.1; -; Genomic_DNA.
PIR; S64904; S64904.
RefSeq; NP_013173.1; NM_001181959.1.
PDB; 5YQR; X-ray; 2.40 A; A=161-272.
PDBsum; 5YQR; -.
ProteinModelPortal; Q08001; -.
SMR; Q08001; -.
BioGrid; 31346; 90.
DIP; DIP-1861N; -.
IntAct; Q08001; 9.
MINT; Q08001; -.
STRING; 4932.YLR072W; -.
TCDB; 9.B.198.2.4; the membrane-anchored lipid-binding protein (lam) family.
iPTMnet; Q08001; -.
MaxQB; Q08001; -.
PaxDb; Q08001; -.
PRIDE; Q08001; -.
EnsemblFungi; YLR072W; YLR072W; YLR072W.
GeneID; 850761; -.
KEGG; sce:YLR072W; -.
EuPathDB; FungiDB:YLR072W; -.
SGD; S000004062; LAM6.
GeneTree; ENSGT00580000081380; -.
InParanoid; Q08001; -.
OrthoDB; EOG092C2YR3; -.
BioCyc; YEAST:G3O-32224-MONOMER; -.
PRO; PR:Q08001; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0044233; C:ER-mitochondrion membrane contact site; IDA:SGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0071561; C:nucleus-vacuole junction; IDA:SGD.
GO; GO:1990816; C:vacuole-mitochondrion membrane contact site; IDA:SGD.
GO; GO:0015248; F:sterol transporter activity; IDA:SGD.
GO; GO:0032366; P:intracellular sterol transport; IDA:SGD.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR004182; GRAM.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR031968; VASt.
Pfam; PF16016; DUF4782; 1.
Pfam; PF02893; GRAM; 1.
SMART; SM00568; GRAM; 1.
PROSITE; PS51778; VAST; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Endoplasmic reticulum; Membrane;
Phosphoprotein; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 693 Membrane-anchored lipid-binding protein
LAM6.
/FTId=PRO_0000247247.
TOPO_DOM 1 630 Cytoplasmic. {ECO:0000305}.
TRANSMEM 631 651 Helical. {ECO:0000255}.
TOPO_DOM 652 693 Lumenal. {ECO:0000305}.
DOMAIN 164 230 GRAM. {ECO:0000255}.
DOMAIN 403 576 VASt. {ECO:0000255|PROSITE-
ProRule:PRU01114}.
COMPBIAS 347 360 Poly-Ser.
MOD_RES 343 343 Phosphothreonine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 591 591 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 593 593 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 594 594 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 597 597 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
HELIX 161 169 {ECO:0000244|PDB:5YQR}.
STRAND 179 208 {ECO:0000244|PDB:5YQR}.
STRAND 216 220 {ECO:0000244|PDB:5YQR}.
HELIX 221 223 {ECO:0000244|PDB:5YQR}.
STRAND 224 229 {ECO:0000244|PDB:5YQR}.
STRAND 237 243 {ECO:0000244|PDB:5YQR}.
STRAND 245 249 {ECO:0000244|PDB:5YQR}.
HELIX 254 267 {ECO:0000244|PDB:5YQR}.
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


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