LAM4_YEAST
ID LAM4_YEAST Reviewed; 1345 AA.
AC P38800; D3DL31;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Membrane-anchored lipid-binding protein LAM4 {ECO:0000303|PubMed:26001273};
DE AltName: Full=Lipid transfer at contact site protein 3 {ECO:0000303|PubMed:25987606};
DE AltName: Full=Lipid transfer protein anchored at membrane contact sites 1 {ECO:0000303|PubMed:26001273};
GN Name=LAM4 {ECO:0000303|PubMed:26001273};
GN Synonyms=LTC3 {ECO:0000303|PubMed:25987606};
GN OrderedLocusNames=YHR080C {ECO:0000312|SGD:S000001122};
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-747, 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-747, AND IDENTIFICATION BY
RP 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-66, AND IDENTIFICATION BY
RP 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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-1119.
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 [7]
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: May be involved in sterol transfer between intracellular
CC membranes. {ECO:0000269|PubMed:26001273}.
CC -!- SUBCELLULAR LOCATION: 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}.
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DR EMBL; U10556; AAB68895.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06775.1; -; Genomic_DNA.
DR PIR; S46817; S46817.
DR RefSeq; NP_011948.1; NM_001179210.1.
DR PDB; 5YQJ; X-ray; 1.50 A; A/B/C=749-929.
DR PDB; 5YQP; X-ray; 1.70 A; A/B=953-1137.
DR PDB; 6BYD; X-ray; 2.19 A; A=946-1145.
DR PDB; 6BYM; X-ray; 2.20 A; A/B=946-1145.
DR PDBsum; 5YQJ; -.
DR PDBsum; 5YQP; -.
DR PDBsum; 6BYD; -.
DR PDBsum; 6BYM; -.
DR AlphaFoldDB; P38800; -.
DR SMR; P38800; -.
DR BioGRID; 36515; 72.
DR DIP; DIP-5282N; -.
DR IntAct; P38800; 3.
DR MINT; P38800; -.
DR STRING; 4932.YHR080C; -.
DR TCDB; 9.B.198.2.2; the membrane-anchored lipid-binding protein (lam) family.
DR iPTMnet; P38800; -.
DR MaxQB; P38800; -.
DR PaxDb; P38800; -.
DR PRIDE; P38800; -.
DR EnsemblFungi; YHR080C_mRNA; YHR080C; YHR080C.
DR GeneID; 856480; -.
DR KEGG; sce:YHR080C; -.
DR SGD; S000001122; LAM4.
DR VEuPathDB; FungiDB:YHR080C; -.
DR eggNOG; KOG1032; Eukaryota.
DR GeneTree; ENSGT00940000172082; -.
DR HOGENOM; CLU_002908_0_0_1; -.
DR InParanoid; P38800; -.
DR OMA; VNNEREY; -.
DR BioCyc; YEAST:G3O-31127-MON; -.
DR PRO; PR:P38800; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38800; protein.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA: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:0005739; C:mitochondrion; HDA: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:0032366; P:intracellular sterol transport; IBA:GO_Central.
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; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..1345
FT /note="Membrane-anchored lipid-binding protein LAM4"
FT /id="PRO_0000202901"
FT TOPO_DOM 1..1197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1198..1218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1219..1345
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 549..616
FT /note="GRAM"
FT /evidence="ECO:0000255"
FT DOMAIN 758..930
FT /note="VASt 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01114"
FT DOMAIN 967..1139
FT /note="VASt 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01114"
FT REGION 51..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..702
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 66
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MUTAGEN 1119
FT /note="G->R: Abolishes the ability to bind sterol."
FT /evidence="ECO:0000269|PubMed:26001273"
FT STRAND 760..769
FT /evidence="ECO:0007829|PDB:5YQJ"
FT HELIX 771..779
FT /evidence="ECO:0007829|PDB:5YQJ"
FT HELIX 784..792
FT /evidence="ECO:0007829|PDB:5YQJ"
FT STRAND 815..826
FT /evidence="ECO:0007829|PDB:5YQJ"
FT STRAND 829..845
FT /evidence="ECO:0007829|PDB:5YQJ"
FT TURN 846..848
FT /evidence="ECO:0007829|PDB:5YQJ"
FT STRAND 849..857
FT /evidence="ECO:0007829|PDB:5YQJ"
FT TURN 862..865
FT /evidence="ECO:0007829|PDB:5YQJ"
FT STRAND 866..881
FT /evidence="ECO:0007829|PDB:5YQJ"
FT STRAND 883..893
FT /evidence="ECO:0007829|PDB:5YQJ"
FT HELIX 900..926
FT /evidence="ECO:0007829|PDB:5YQJ"
FT STRAND 969..979
FT /evidence="ECO:0007829|PDB:5YQP"
FT HELIX 981..989
FT /evidence="ECO:0007829|PDB:5YQP"
FT HELIX 994..1001
FT /evidence="ECO:0007829|PDB:5YQP"
FT STRAND 1006..1008
FT /evidence="ECO:0007829|PDB:5YQP"
FT STRAND 1024..1032
FT /evidence="ECO:0007829|PDB:5YQP"
FT STRAND 1035..1038
FT /evidence="ECO:0007829|PDB:5YQP"
FT STRAND 1040..1053
FT /evidence="ECO:0007829|PDB:5YQP"
FT STRAND 1057..1066
FT /evidence="ECO:0007829|PDB:5YQP"
FT HELIX 1073..1075
FT /evidence="ECO:0007829|PDB:5YQP"
FT STRAND 1076..1086
FT /evidence="ECO:0007829|PDB:5YQP"
FT STRAND 1088..1090
FT /evidence="ECO:0007829|PDB:5YQP"
FT STRAND 1092..1104
FT /evidence="ECO:0007829|PDB:5YQP"
FT HELIX 1109..1136
FT /evidence="ECO:0007829|PDB:5YQP"
SQ SEQUENCE 1345 AA; 149680 MW; 2FDAB94A686564C2 CRC64;
MTRDSKKKHH WGTAFLRTIG VKRKHKKDRN FLNNTTGENV STTASAERFR RVGGNPDIPS
LLKPETFTES PAKGSQKAAA SSLAHSQGVF NIPIVIDPME TNRLEKTNTN LTAGSLKGRF
QDGNSNSNSV PSLSVQALEK EKLQSGKREG SSNQAEEKTP DGHDEHTAFE TFLSFAHNAV
SHIPKINVQD ADNGTISRNE PKDRKKNSSN ISGALSENST NNKNTSSTKE SDGPFLKNLD
NILAASKSST PSNQQLNTTE AGSKSKPSSL SRLAFGNLKG HIHSNSHSSS NAISGDDTSL
DDTRKMTDDM ARKVVFEPIR HSHDKPTPGV GNLKLEHFDD SQATLEGLEA MSAESLPEAD
HLDSRGPVQQ SNLERKTVPS KWSVVSSSTT DGVKPRRRAK SMISAMADKQ NTSSDVLQDC
KKRLSFNSSN GLTNNDPEYE DREPREMSKK FLNRRSFSPG SISMGMKVLP STALKYSLNK
VKNSTDIAST IIPRPSMSNG RPSSGLRRSS SKSFSSTPVN IIEPSEENGR QSSIRIKGVE
YASEKKDAEF HAIFKDSGVS PNERLILDHS CALSRDILLQ GRMYISDQHI GFYSNILGWV
STVFIPFKTI VQIEKRATAG IFPNGIVIDT LHTKYTFASF TSRDATYDLI TEVWNQIILG
KRFRSNSNNT NSSSNSISDD ENDDYDDDYD DYGDDDDDLY DNSNNISDST DMTSSVSIGK
PEDLPMPLQT DTPYGTGIPP LGPKIHSPTE TVYKPAPNEK LVNESTIHAS LGRVVNILFG
KDVSYIMAIL KAQKNSDISP IPVLVDSPTV SEGKKRDYSY VKTTPGAIGP GKTKCMITET
IQHFNLEEYV QVLQTTKTPD VPSGNSFYVR TVYLLSWANN NETKLKLYVS VEWTGKSLIK
SPIEKGTFDG VTDATKILVE ELGNILTRSA TKRKRSSKEN TVTVSTLPKM EPSSHAPTEP
DIQKDKDDSI IRENENIPAP LGTVVQLLFG SNTEYMQKVI TRDKNNVNVE TIPKFTPSLV
EGGSRHYEYT KKLNNSIGPK QTKCLLTESI EHMDINNYVL VTQTTKTPDV PSGSNFAVES
KIFLFWGQHD TTNMTVITKI NWTSKSFLKG AIEKGSVEGQ KVSVDYMLSE LRDIISRAKS
KKPVKKVMKS HDKHRPFHSK VEQKSSESRK SDDNKDILTH ILDFVQNNFS SEIFMNKLLS
PQKLFLILGL TIMLFWSPRL HVFQEKNNLQ IIKPGRLLID GQEYNYVPSF GTLYNSYENA
ISSKKKRENV NYARDKSPIV GRESDIWDWI SNRGSAISPR GRAMLRNDDE HKLQQLSESI
KITEMQLNHM KTMLDNIERD ANDLS
