LAM5_YEAST
ID LAM5_YEAST Reviewed; 674 AA.
AC P43560; D6VTI7; P43559;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Membrane-anchored lipid-binding protein LAM5 {ECO:0000303|PubMed:26001273};
DE AltName: Full=Lipid transfer at contact site protein 2 {ECO:0000303|PubMed:25987606};
DE AltName: Full=Lipid transfer protein anchored at membrane contact sites 1 {ECO:0000303|PubMed:26001273};
GN Name=LAM5 {ECO:0000303|PubMed:26001273};
GN Synonyms=LTC2 {ECO:0000303|PubMed:25987606};
GN OrderedLocusNames=YFL042C {ECO:0000312|SGD:S000001852};
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=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [2]
RP SEQUENCE REVISION.
RA Murakami Y.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-110; SER-113; THR-143 AND
RP SER-149, AND 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 SER-140, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND THR-143, AND
RP 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 [7]
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 [8]
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 intracellular puncta representing
CC endoplasmic reticulum (ER)-mitochondrion membrane contact sites,
CC nucleus-vacuole junctions (NVJ) and other non-NVJ ER-vacuole contact
CC sites. {ECO:0000269|PubMed:26001273}.
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; D50617; BAA24424.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12397.1; -; Genomic_DNA.
DR PIR; S78570; S78570.
DR RefSeq; NP_116611.1; NM_001179924.1.
DR AlphaFoldDB; P43560; -.
DR SMR; P43560; -.
DR BioGRID; 31104; 44.
DR DIP; DIP-1182N; -.
DR IntAct; P43560; 5.
DR MINT; P43560; -.
DR STRING; 4932.YFL042C; -.
DR TCDB; 9.B.198.2.3; the membrane-anchored lipid-binding protein (lam) family.
DR iPTMnet; P43560; -.
DR MaxQB; P43560; -.
DR PaxDb; P43560; -.
DR PRIDE; P43560; -.
DR EnsemblFungi; YFL042C_mRNA; YFL042C; YFL042C.
DR GeneID; 850501; -.
DR KEGG; sce:YFL042C; -.
DR SGD; S000001852; LAM5.
DR VEuPathDB; FungiDB:YFL042C; -.
DR eggNOG; KOG1032; Eukaryota.
DR GeneTree; ENSGT00940000176474; -.
DR HOGENOM; CLU_015638_1_1_1; -.
DR InParanoid; P43560; -.
DR OMA; DNWEPVS; -.
DR BioCyc; YEAST:G3O-30421-MON; -.
DR PRO; PR:P43560; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43560; protein.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; 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; IBA:GO_Central.
DR GO; GO:0071561; C:nucleus-vacuole junction; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032934; F:sterol binding; IBA:GO_Central.
DR GO; GO:0120015; F:sterol transfer activity; ISS:SGD.
DR GO; GO:0032366; P:intracellular sterol transport; ISS: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 Endoplasmic reticulum; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..674
FT /note="Membrane-anchored lipid-binding protein LAM5"
FT /id="PRO_0000202673"
FT TOPO_DOM 1..633
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 634..654
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 655..674
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 198..264
FT /note="GRAM"
FT /evidence="ECO:0000255"
FT DOMAIN 409..582
FT /note="VASt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01114"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..356
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 110
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 143
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
SQ SEQUENCE 674 AA; 76347 MW; 161F12303E1102C4 CRC64;
MSDVDNWEPV SDNEDSTDSV KQLGPPFEHA SNNDNAGDTE AESLQEVPLN TETNDVRKNL
VVITNQSAAD EHPTEIKHDQ SRTSSTSSFF SGMISSFKSN VPSPVSRSTT PTSPVSQPSI
ISHRREPSMG SKRRSSRRIS NATIAEIGSP LQQVEKPDEV KTRLTPSQMK EDNYDHRRFV
EERYMDTPYH YASEQRNKDF HETFKSVPKD DRLLDDFNCG LNRELLYQGK LYITETHLCF
NSNVLGWIAK VLIAFEDVTF MEKTSAAGLF PSAISIETKM GKTLFNGFIS RDAAFGLMKE
VWSRTLLQKD MASENINTKA EKSGNGKEID DAINSIDEEN NDKDANDNDT NENDDENIST
NETTPNSTSS SPDKEKEKAY KLRADSSYQY DGPIYHHSTS FPAEPMANNE FVLKELPFDC
APGILFEIMF NSEQNEFLLD FLRGQEGSQI TTIPNFTSID GSSMTLKREY SYEKALHFPA
GPKSTTCYVA EVIKRKDPDT YYEVISSIRT PNVPSGGSFS TKTRYLIRWN DEITCLLRVS
FWVEWTGSSW IKGMVENGCK NGQLEAAQLM ERILSKFIKN NVEECQITIS KEEEEQDDKE
VKNKLKEVDL EQPREAVVTA PAIAEQQGLK VTMETWLFLY LIVVVLLLFN LFYIRSIAVS
LHQLVKLQLV ELKL
