YSP2_YEAST
ID YSP2_YEAST Reviewed; 1438 AA.
AC Q06681; D6VSV9;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Membrane-anchored lipid-binding protein YSP2 {ECO:0000303|PubMed:26001273};
DE AltName: Full=Lipid transfer at contact site protein 4 {ECO:0000303|PubMed:25987606};
DE AltName: Full=Lipid transfer protein anchored at membrane contact sites 3 {ECO:0000303|PubMed:26001273};
DE AltName: Full=Yeast suicide protein 2 {ECO:0000303|PubMed:16962064};
GN Name=YSP2 {ECO:0000303|PubMed:16962064};
GN Synonyms=LAM2 {ECO:0000303|PubMed:26001273},
GN LTC4 {ECO:0000303|PubMed:25987606};
GN OrderedLocusNames=YDR326C {ECO:0000312|SGD:S000002734};
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16962064; DOI=10.1016/j.bbabio.2006.07.005;
RA Sokolov S., Knorre D., Smirnova E., Markova O., Pozniakovsky A.,
RA Skulachev V., Severin F.;
RT "Ysp2 mediates death of yeast induced by amiodarone or intracellular
RT acidification.";
RL Biochim. Biophys. Acta 1757:1366-1370(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411; SER-596 AND SER-1032,
RP AND IDENTIFICATION BY 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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-1205.
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 GENE FAMILY.
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 induction of programmed cell death in response to
CC reactive oxygen species (ROS) (PubMed:16962064). May be involved in
CC sterol transfer between intracellular membranes (PubMed:26001273).
CC {ECO:0000269|PubMed:16962064, ECO:0000269|PubMed:26001273}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:16962064}; Single-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:26001273}; Single-pass membrane protein
CC {ECO:0000255}. Note=Localizes to puncta in the cell periphery
CC representing cortical endoplasmic reticulum (cER)-plasma membrane (PM)
CC membrane contact sites. {ECO:0000269|PubMed:26001273}.
CC -!- DOMAIN: The VASt domains bind sterols. {ECO:0000269|PubMed:26001273}.
CC -!- SIMILARITY: Belongs to the YSP2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U32517; AAB64762.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12169.1; -; Genomic_DNA.
DR PIR; S59792; S59792.
DR RefSeq; NP_010613.1; NM_001180634.1.
DR PDB; 5YQI; X-ray; 1.60 A; A=851-1016.
DR PDB; 5YQQ; X-ray; 1.90 A; A/B=1060-1223.
DR PDB; 5YS0; X-ray; 2.60 A; A/B/C=1060-1223.
DR PDB; 6CAY; X-ray; 2.00 A; A/B/C/D=851-1017.
DR PDBsum; 5YQI; -.
DR PDBsum; 5YQQ; -.
DR PDBsum; 5YS0; -.
DR PDBsum; 6CAY; -.
DR AlphaFoldDB; Q06681; -.
DR SMR; Q06681; -.
DR BioGRID; 32384; 89.
DR DIP; DIP-1840N; -.
DR IntAct; Q06681; 4.
DR MINT; Q06681; -.
DR STRING; 4932.YDR326C; -.
DR TCDB; 9.B.198.2.1; the membrane-anchored lipid-binding protein (lam) family.
DR iPTMnet; Q06681; -.
DR MaxQB; Q06681; -.
DR PaxDb; Q06681; -.
DR PRIDE; Q06681; -.
DR EnsemblFungi; YDR326C_mRNA; YDR326C; YDR326C.
DR GeneID; 851926; -.
DR KEGG; sce:YDR326C; -.
DR SGD; S000002734; YSP2.
DR VEuPathDB; FungiDB:YDR326C; -.
DR eggNOG; KOG1032; Eukaryota.
DR GeneTree; ENSGT00940000172082; -.
DR HOGENOM; CLU_002908_0_0_1; -.
DR InParanoid; Q06681; -.
DR OMA; YIMVRQI; -.
DR BioCyc; YEAST:G3O-29883-MON; -.
DR PRO; PR:Q06681; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q06681; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:SGD.
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:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032934; F:sterol binding; IDA:SGD.
DR GO; GO:0120015; F:sterol transfer activity; IDA:SGD.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0032366; P:intracellular sterol transport; IMP:SGD.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR031968; VASt.
DR InterPro; IPR040147; Ysp2/Lam4-like.
DR PANTHER; PTHR23319:SF4; PTHR23319:SF4; 2.
DR Pfam; PF02893; GRAM; 1.
DR Pfam; PF16016; VASt; 2.
DR SMART; SM00568; GRAM; 1.
DR PROSITE; PS51778; VAST; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Mitochondrion; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1438
FT /note="Membrane-anchored lipid-binding protein YSP2"
FT /id="PRO_0000253815"
FT TOPO_DOM 1..1277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1278..1298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1299..1438
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 648..716
FT /note="GRAM"
FT /evidence="ECO:0000255"
FT DOMAIN 851..1018
FT /note="VASt 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01114"
FT DOMAIN 1059..1225
FT /note="VASt 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01114"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1225..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..804
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1240
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1032
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CARBOHYD 1306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 1205
FT /note="G->A,T: Reduces the ability to bind sterol."
FT /evidence="ECO:0000305|PubMed:26001273"
FT MUTAGEN 1205
FT /note="G->R: Abolishes the ability to bind sterol."
FT /evidence="ECO:0000305|PubMed:26001273"
FT HELIX 851..853
FT /evidence="ECO:0007829|PDB:5YQI"
FT STRAND 854..862
FT /evidence="ECO:0007829|PDB:5YQI"
FT HELIX 864..872
FT /evidence="ECO:0007829|PDB:5YQI"
FT HELIX 877..885
FT /evidence="ECO:0007829|PDB:5YQI"
FT HELIX 898..901
FT /evidence="ECO:0007829|PDB:5YQI"
FT STRAND 902..911
FT /evidence="ECO:0007829|PDB:5YQI"
FT STRAND 914..917
FT /evidence="ECO:0007829|PDB:6CAY"
FT STRAND 919..933
FT /evidence="ECO:0007829|PDB:5YQI"
FT TURN 934..936
FT /evidence="ECO:0007829|PDB:5YQI"
FT STRAND 937..945
FT /evidence="ECO:0007829|PDB:5YQI"
FT TURN 950..953
FT /evidence="ECO:0007829|PDB:5YQI"
FT STRAND 954..966
FT /evidence="ECO:0007829|PDB:5YQI"
FT TURN 967..969
FT /evidence="ECO:0007829|PDB:5YQI"
FT STRAND 970..983
FT /evidence="ECO:0007829|PDB:5YQI"
FT HELIX 988..1013
FT /evidence="ECO:0007829|PDB:5YQI"
FT STRAND 1061..1071
FT /evidence="ECO:0007829|PDB:5YQQ"
FT HELIX 1073..1081
FT /evidence="ECO:0007829|PDB:5YQQ"
FT HELIX 1086..1094
FT /evidence="ECO:0007829|PDB:5YQQ"
FT STRAND 1097..1099
FT /evidence="ECO:0007829|PDB:5YQQ"
FT STRAND 1110..1117
FT /evidence="ECO:0007829|PDB:5YQQ"
FT STRAND 1121..1124
FT /evidence="ECO:0007829|PDB:5YS0"
FT STRAND 1128..1140
FT /evidence="ECO:0007829|PDB:5YQQ"
FT TURN 1141..1143
FT /evidence="ECO:0007829|PDB:5YQQ"
FT STRAND 1144..1152
FT /evidence="ECO:0007829|PDB:5YQQ"
FT HELIX 1159..1161
FT /evidence="ECO:0007829|PDB:5YQQ"
FT STRAND 1162..1173
FT /evidence="ECO:0007829|PDB:5YQQ"
FT TURN 1174..1176
FT /evidence="ECO:0007829|PDB:5YQQ"
FT STRAND 1177..1188
FT /evidence="ECO:0007829|PDB:5YQQ"
FT HELIX 1193..1221
FT /evidence="ECO:0007829|PDB:5YQQ"
SQ 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
