LAM1_YEAST
ID LAM1_YEAST Reviewed; 1228 AA.
AC P38851; D3DLA4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Membrane-anchored lipid-binding protein LAM1 {ECO:0000303|PubMed:26001273};
DE AltName: Full=Lipid transfer protein anchored at membrane contact sites 1 {ECO:0000303|PubMed:26001273};
DE AltName: Full=Yeast suicide protein 1 {ECO:0000303|PubMed:15657396};
GN Name=LAM1 {ECO:0000303|PubMed:26001273};
GN Synonyms=YSP1 {ECO:0000303|PubMed:15657396};
GN OrderedLocusNames=YHR155W {ECO:0000312|SGD:S000001198};
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP DOMAIN.
RX PubMed=15023338; DOI=10.1016/s1097-2765(04)00083-8;
RA Yu J.W., Mendrola J.M., Audhya A., Singh S., Keleti D., DeWald D.B.,
RA Murray D., Emr S.D., Lemmon M.A.;
RT "Genome-wide analysis of membrane targeting by S.cerevisiae pleckstrin
RT homology domains.";
RL Mol. Cell 13:677-688(2004).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15657396; DOI=10.1083/jcb.200408145;
RA Pozniakovsky A.I., Knorre D.A., Markova O.V., Hyman A.A., Skulachev V.P.,
RA Severin F.F.;
RT "Role of mitochondria in the pheromone- and amiodarone-induced programmed
RT death of yeast.";
RL J. Cell Biol. 168:257-269(2005).
RN [7]
RP FUNCTION.
RX PubMed=18800175;
RA Lushchak V., Abrat O., Miedzobrodzki J., Semchyshyn H.;
RT "Pdr12p-dependent and -independent fluorescein extrusion from baker's yeast
RT cells.";
RL Acta Biochim. Pol. 55:595-601(2008).
RN [8]
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).
CC -!- FUNCTION: Involved in mitochondrial fragmentation during programmed
CC cell death in response to high levels of alpha-factor mating pheromone
CC or the drug amiodarone (PubMed:15657396, PubMed:18800175). May be
CC involved in sterol transfer between intracellular membranes
CC (PubMed:26001273). {ECO:0000269|PubMed:15657396,
CC ECO:0000269|PubMed:18800175, ECO:0000269|PubMed:26001273}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15657396}; Single-pass
CC membrane protein {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 domain bind sterols. {ECO:0000250|UniProtKB:P38800}.
CC -!- MISCELLANEOUS: Present with 1170 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SIP3 family. {ECO:0000305}.
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DR EMBL; U10397; AAB68977.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06848.1; -; Genomic_DNA.
DR PIR; S46754; S46754.
DR RefSeq; NP_012025.1; NM_001179286.1.
DR AlphaFoldDB; P38851; -.
DR BioGRID; 36589; 66.
DR IntAct; P38851; 1.
DR MINT; P38851; -.
DR STRING; 4932.YHR155W; -.
DR TCDB; 9.B.198.1.1; the membrane-anchored lipid-binding protein (lam) family.
DR iPTMnet; P38851; -.
DR MaxQB; P38851; -.
DR PaxDb; P38851; -.
DR PRIDE; P38851; -.
DR TopDownProteomics; P38851; -.
DR EnsemblFungi; YHR155W_mRNA; YHR155W; YHR155W.
DR GeneID; 856560; -.
DR KEGG; sce:YHR155W; -.
DR SGD; S000001198; LAM1.
DR VEuPathDB; FungiDB:YHR155W; -.
DR eggNOG; ENOG502QU87; Eukaryota.
DR GeneTree; ENSGT00940000154453; -.
DR HOGENOM; CLU_001720_0_0_1; -.
DR InParanoid; P38851; -.
DR BioCyc; YEAST:G3O-31190-MON; -.
DR PRO; PR:P38851; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38851; protein.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0015248; F:sterol transporter activity; IC:SGD.
DR GO; GO:0032366; P:intracellular sterol transport; IMP:SGD.
DR CDD; cd07609; BAR_SIP3_fungi; 1.
DR CDD; cd13280; PH_SIP3; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR039463; Sip3/Lam1_BAR.
DR InterPro; IPR042067; Sip3_PH.
DR InterPro; IPR031968; VASt.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF16016; VASt; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51778; VAST; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Mitochondrion;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..1228
FT /note="Membrane-anchored lipid-binding protein LAM1"
FT /id="PRO_0000202927"
FT TOPO_DOM 1..1062
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26001273"
FT TRANSMEM 1063..1083
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1084..1228
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P38717"
FT DOMAIN 308..421
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 773..978
FT /note="VASt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01114"
FT CARBOHYD 1205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1228 AA; 143584 MW; C8872EAE8270A4B6 CRC64;
MHEHKAELRL ITVALNEAST DSPSFRASVN YFHTRMESLS SWMHSTVDYV ENTYKPSFQD
FQRIKETLFS QLLPSPILLS NGFVSNQPYT PLLVRDFTRD VSDLSNTVMK IILGDENSQY
TAALSALSSD AINPYFNKRK TFEYYQRKYD SFLTDFLAAT NDGNTLIPQN LQNETFKLVD
IKHKYIEASL DLTEAISLMK VNLDKFLIET IDIVRKNNVI TTKDTKDVID ITPELTETLK
DWTDWIESNL QTLQALSSKL SEAKYAILKL SLARMKPSRL IQDYDLKSIQ NLKFNLPKSI
SNGNNSEEKG LSGWLYMKTT VGHDPKRVVW VRRWCFLQNN VFGVFSLSPS KTYVEETDKF
GILWITVEYL PKEPRNFCFK LRIQNPNCKT EEENTYIDII LQAESIDELK SWINTLTSHK
RIALSIKEEN DPRYQLARKK IEPQFFEFAS SSSTSTDKLL TSFSSKTLTL VEELKKNYMS
EDDIYSIIDN KAYHLRVIST PIATQLTHLA LFSTFLSVSN YYPCATQANT WGTANWNDLS
YLVNPLKGSS VHKPATVSNS SRFSVSYPDY YPYSLKVDDI QFRSIFFSVN HDFLQVPKEL
VLLRYSSVWC PNNKQKFASM AFVTLNHIYV YLNISGFSYL RRIDLLDIDS IEYDKSPKHV
SSRMLHMQRG DGLRFNMSVF FTDRRAVASK LQFLIENKAM HIPKGEKEVL EIFQELDEEI
ENEKKIIKDN LSESEHYSKD YDYLLKSTYD HHFENTNETP MELMSRKLRL EREAWCYFQD
NFKVGSKTLF HVLFGDKSQV FPSSLFLCKK GSNLNNNSYW ERIRRAKEDA SCQFELCRKL
QFQLNRTSNF IKDLLWLKDD NDNFKLVLQQ RVTKIKQGYY FEVEEGPIIV KFPLCHPLLL
RVRFIIAECI TSQGESLKKC DLAILYDFNY VESIDKLNTK VEKLWLFERI HLNWALRYCK
LEHSEINRKT REYLKKFNDR EKMSDVIKLC GFLGVLPKER IENDEKAGDF MQPVYINYDF
LSLSKIFTKL TVFYLSSVII KTMKVLLAMV MVIFKCFSKV NKTLYYCLLI SAVTNLFFVG
KSIHSYFSVK SAETLFQNYA NGDQRGLQIM HRSLTVPDLN LLTRKMMDND QENPVFKRFD
EDKNAYQYKG TRQEIAIKRN QVLTELKILQ NTEKELVQGS YRKFIITERD KCITTQNEIF
DLWINDTKLQ DYCMACFAEY NRLSAIPV
