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Membrane-anchored lipid-binding protein YSP2 (Lipid transfer at contact site protein 4) (Lipid transfer protein anchored at membrane contact sites 3) (Yeast suicide protein 2)

 YSP2_YEAST              Reviewed;        1438 AA.
Q06681; D6VSV9;
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-MAY-2018, entry version 117.
RecName: Full=Membrane-anchored lipid-binding protein YSP2 {ECO:0000303|PubMed:26001273};
AltName: Full=Lipid transfer at contact site protein 4 {ECO:0000303|PubMed:25987606};
AltName: Full=Lipid transfer protein anchored at membrane contact sites 3 {ECO:0000303|PubMed:26001273};
AltName: Full=Yeast suicide protein 2 {ECO:0000303|PubMed:16962064};
Name=YSP2 {ECO:0000303|PubMed:16962064};
Synonyms=LAM2 {ECO:0000303|PubMed:26001273},
LTC4 {ECO:0000303|PubMed:25987606};
OrderedLocusNames=YDR326C {ECO:0000312|SGD:S000002734};
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=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(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]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16962064; DOI=10.1016/j.bbabio.2006.07.005;
Sokolov S., Knorre D., Smirnova E., Markova O., Pozniakovsky A.,
Skulachev V., Severin F.;
"Ysp2 mediates death of yeast induced by amiodarone or intracellular
acidification.";
Biochim. Biophys. Acta 1757:1366-1370(2006).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, 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 SER-13, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[6]
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).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411; SER-596 AND
SER-1032, 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).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-1205.
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]
GENE FAMILY.
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 induction of programmed cell death in
response to reactive oxygen species (ROS) (PubMed:16962064). May
be involved in sterol transfer between intracellular membranes
(PubMed:26001273). {ECO:0000269|PubMed:16962064,
ECO:0000269|PubMed:26001273}.
-!- SUBCELLULAR LOCATION: Mitochondrion membrane
{ECO:0000269|PubMed:16962064}; Single-pass membrane protein
{ECO:0000255}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:26001273}; Single-pass membrane protein
{ECO:0000255}. Note=Localizes to puncta in the cell periphery
representing cortical endoplasmic reticulum (cER)-plasma membrane
(PM) membrane contact sites. {ECO:0000269|PubMed:26001273}.
-!- DOMAIN: The VASt domains bind sterols.
{ECO:0000269|PubMed:26001273}.
-!- SIMILARITY: Belongs to the YSP2 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; U32517; AAB64762.1; -; Genomic_DNA.
EMBL; BK006938; DAA12169.1; -; Genomic_DNA.
PIR; S59792; S59792.
RefSeq; NP_010613.1; NM_001180634.1.
PDB; 5YQI; X-ray; 1.60 A; A=851-1016.
PDB; 5YQQ; X-ray; 1.90 A; A/B=1060-1223.
PDB; 5YS0; X-ray; 2.60 A; A/B/C=1060-1223.
PDBsum; 5YQI; -.
PDBsum; 5YQQ; -.
PDBsum; 5YS0; -.
ProteinModelPortal; Q06681; -.
SMR; Q06681; -.
BioGrid; 32384; 76.
DIP; DIP-1840N; -.
IntAct; Q06681; 4.
MINT; Q06681; -.
STRING; 4932.YDR326C; -.
TCDB; 9.B.198.2.1; the membrane-anchored lipid-binding protein (lam) family.
iPTMnet; Q06681; -.
MaxQB; Q06681; -.
PaxDb; Q06681; -.
PRIDE; Q06681; -.
EnsemblFungi; YDR326C; YDR326C; YDR326C.
GeneID; 851926; -.
KEGG; sce:YDR326C; -.
EuPathDB; FungiDB:YDR326C; -.
SGD; S000002734; YSP2.
GeneTree; ENSGT00580000081380; -.
HOGENOM; HOG000001060; -.
InParanoid; Q06681; -.
OMA; NTEIQRE; -.
OrthoDB; EOG092C2YR3; -.
BioCyc; YEAST:G3O-29883-MONOMER; -.
PRO; PR:Q06681; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:SGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:SGD.
GO; GO:0032934; F:sterol binding; IDA:SGD.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0032366; P:intracellular sterol transport; IMP:SGD.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR004182; GRAM.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR031968; VASt.
Pfam; PF16016; DUF4782; 2.
Pfam; PF02893; GRAM; 1.
SMART; SM00568; GRAM; 1.
PROSITE; PS51778; VAST; 2.
1: Evidence at protein level;
3D-structure; Apoptosis; Complete proteome; Endoplasmic reticulum;
Glycoprotein; Membrane; Mitochondrion; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 1438 Membrane-anchored lipid-binding protein
YSP2.
/FTId=PRO_0000253815.
TOPO_DOM 1 1277 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1278 1298 Helical. {ECO:0000255}.
TOPO_DOM 1299 1438 Lumenal. {ECO:0000305}.
DOMAIN 648 716 GRAM. {ECO:0000255}.
DOMAIN 851 1018 VASt 1. {ECO:0000255|PROSITE-
ProRule:PRU01114}.
DOMAIN 1059 1225 VASt 2. {ECO:0000255|PROSITE-
ProRule:PRU01114}.
COMPBIAS 219 232 Asn-rich. {ECO:0000255|PROSITE-
ProRule:PRU00003}.
COMPBIAS 770 815 Asp-rich. {ECO:0000255|PROSITE-
ProRule:PRU00004}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000244|PubMed:17287358,
ECO:0000244|PubMed:17330950}.
MOD_RES 411 411 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 596 596 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 1032 1032 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
CARBOHYD 1306 1306 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1373 1373 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1430 1430 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
MUTAGEN 1205 1205 G->A,T: Reduces the ability to bind
sterol. {ECO:0000305|PubMed:26001273}.
MUTAGEN 1205 1205 G->R: Abolishes the ability to bind
sterol. {ECO:0000305|PubMed:26001273}.
HELIX 851 853 {ECO:0000244|PDB:5YQI}.
STRAND 854 862 {ECO:0000244|PDB:5YQI}.
HELIX 864 872 {ECO:0000244|PDB:5YQI}.
HELIX 877 885 {ECO:0000244|PDB:5YQI}.
HELIX 898 901 {ECO:0000244|PDB:5YQI}.
STRAND 902 911 {ECO:0000244|PDB:5YQI}.
STRAND 919 933 {ECO:0000244|PDB:5YQI}.
TURN 934 936 {ECO:0000244|PDB:5YQI}.
STRAND 937 945 {ECO:0000244|PDB:5YQI}.
TURN 950 953 {ECO:0000244|PDB:5YQI}.
STRAND 954 966 {ECO:0000244|PDB:5YQI}.
TURN 967 969 {ECO:0000244|PDB:5YQI}.
STRAND 970 983 {ECO:0000244|PDB:5YQI}.
HELIX 988 1013 {ECO:0000244|PDB:5YQI}.
STRAND 1061 1071 {ECO:0000244|PDB:5YQQ}.
HELIX 1073 1081 {ECO:0000244|PDB:5YQQ}.
HELIX 1086 1094 {ECO:0000244|PDB:5YQQ}.
STRAND 1097 1099 {ECO:0000244|PDB:5YQQ}.
STRAND 1110 1117 {ECO:0000244|PDB:5YQQ}.
STRAND 1121 1124 {ECO:0000244|PDB:5YS0}.
STRAND 1128 1140 {ECO:0000244|PDB:5YQQ}.
TURN 1141 1143 {ECO:0000244|PDB:5YQQ}.
STRAND 1144 1152 {ECO:0000244|PDB:5YQQ}.
HELIX 1159 1161 {ECO:0000244|PDB:5YQQ}.
STRAND 1162 1173 {ECO:0000244|PDB:5YQQ}.
TURN 1174 1176 {ECO:0000244|PDB:5YQQ}.
STRAND 1177 1188 {ECO:0000244|PDB:5YQQ}.
HELIX 1193 1221 {ECO:0000244|PDB:5YQQ}.
SEQUENCE 1438 AA; 160578 MW; F98E0597C401BCBD CRC64;
MRDEATRKKR SFSDGHFFKK LKLMSRKKQP VMERSKTTRT RKESTNSAAK SSLSLRRANN
GRKTIAKRRV LTDIGSTNEG VAGNSGSNSP AQYSHTPHFS DSIPPLPLEL PDIVSIRSSR
SHISNKSNKN KHGIDLTFIP RRSLQNSKAG LKKPNTSPQG YFNIPVTIDR ASEKVKHTDT
KNTFNSSSSE NERPVLSILQ KDDSQSSSHP AIDSMSAPNN INNNNDIENS SNSLFDTILS
IAHSAISHVP KISALNTEIQ REFSHSGESH TGSTRHPYFH IHHAQQQHPL SQQQGPLPVS
ENANQNPNDT VLIHSPSANT AHRSSSFLRH LDYLLSPTSG PASDKHTQVE EGDDEEELSP
LSKAFLSPST QLVPTNTSTT PLSGSLTPNN RNVNANSNSE TENDNDRDDR SNVGKVKFQP
LKVHEPAIST FGKGNLTLEA VAGSSDIDNT TIDLDENNTN NNPNASSTNL SHISKSNVNN
NLGPKELNTS YRNSTYIDMA RFENSQSNLS SHRARSKTLP ANKALENAVG DEGNSKRNSR
YSSYSNDMAF DDADERKFRS MSKKFLNRRS FSPSNLGNKV IPGINLRNSF NKNRNSSSDF
FSTNQGQQMP RTSTAGSGNI HAIMGLDSGN DDFKLEGIEY ASEKKNSEFH TLFKDCDINP
NEKLIVDHSC ALSRDILLQG RMYISDAHIG FFSNILGWVS TVFIPFKEIV QIEKKTTAGI
FPNGIVIDTL HTKYIFASFM SRDATFDLIT DVWNQIILGK KYRNGFGNND DGTISDSSSA
FFDDSDDNDD DGDLDDDDPD INSTDMTSSD DIDADVFNES NDLGKNQKST NYLLGPNKHS
PTTADFKPSN NDHLVIEANI NAPLGKVVNL LYGEDVSYYE RILKAQKNFE ISPIPNNFLT
KKIRDYAYTK PLSGSIGPSK TKCLITDTLE HYDLEDYVKV LSITKNPDVP SGNIFSVKTV
FLFSWDKNNS TKLTVYNSVD WTGKSWIKSM IEKGTFDGVA DTTKIMISEI KKILSDEDSN
INSKHQASNN ESEEEIINLP TIGPPVHDPT EPDFQKGKDD TVIDEKINIP VPLGTVFSLL
YGDDTSYIKK IIENQNNFNV CDIPKFVNNA REITYTKKLN NSFGPKQTKC IVTETIEHMD
LNSFFMVKQI VRSPDVPYGS SFSVHTRFFY SWGDHNTTNM KVVTNVVWTG KSMLKGTIEK
GSIDGQRSST KQLVDDLKKI ISNASSTKKK SRRRGKTVNK RKSSPSTIKN EKNEENFEDT
STKNSFFSAF SMLQQVNITS VQGIMTIISF FICLIFFFRL LFHSKNTSNI QIITPGTILI
NGNEYNYVPN FKTLYHVYED NIIKDARRKD SNKNNIVTDT EGLIWDWLID RGNGTVQNSV
LSNHIKESNN KKVKLVNGVS DHKIQQLVES IKITELQLQE MKELLAQTDN TSATNQLL


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