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   02-SEP-2026, entry version 164.
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; 50.
DR   DIP; DIP-1182N; -.
DR   FunCoup; P43560; 194.
DR   IntAct; P43560; 7.
DR   MINT; P43560; -.
DR   STRING; 4932.YFL042C; -.
DR   TCDB; 9.B.198.2.3; the membrane-anchored lipid-binding protein (lam) family.
DR   GlyGen; P43560; 22 sites, 1 O-linked glycan (22 sites).
DR   iPTMnet; P43560; -.
DR   PaxDb; 4932-YFL042C; -.
DR   PeptideAtlas; P43560; -.
DR   EnsemblFungi; YFL042C_mRNA; YFL042C; YFL042C.
DR   GeneID; 850501; -.
DR   KEGG; sce:YFL042C; -.
DR   AGR; SGD:S000001852; -.
DR   SGD; S000001852; LAM5.
DR   VEuPathDB; FungiDB:YFL042C; -.
DR   eggNOG; KOG1032; Eukaryota.
DR   HOGENOM; CLU_015638_1_1_1; -.
DR   InParanoid; P43560; -.
DR   OMA; DNWEPVS; -.
DR   OrthoDB; 2162691at2759; -.
DR   BioCyc; YEAST:G3O-30421-MONOMER; -.
DR   BioGRID-ORCS; 850501; 3 hits in 10 CRISPR screens.
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; EXP:UniProtKB.
DR   GO; GO:0140268; C:endoplasmic reticulum-plasma membrane contact site; IBA:GO_Central.
DR   GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane contact site; 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   CDD; cd13220; PH-GRAM_GRAMDC; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR051482; Cholesterol_transport.
DR   InterPro; IPR004182; GRAM.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR031968; VASt.
DR   PANTHER; PTHR23319; GRAM DOMAIN CONTAINING 1B, ISOFORM E; 1.
DR   PANTHER; PTHR23319:SF4; GRAM DOMAIN CONTAINING 1B, ISOFORM E; 1.
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        69..81
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..119
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..357
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..371
FT                   /note="Low complexity"
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
//