GENTAUR Molecular Products.

 LAM1_YEAST              Reviewed;        1228 AA.
 P38851; D3DLA4;
 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
 01-FEB-1995, sequence version 1.
 05-DEC-2018, entry version 124.
 RecName: Full=Membrane-anchored lipid-binding protein LAM1 {ECO:0000303|PubMed:26001273};
 AltName: Full=Lipid transfer protein anchored at membrane contact sites 1 {ECO:0000303|PubMed:26001273};
 AltName: Full=Yeast suicide protein 1 {ECO:0000303|PubMed:15657396};
 Name=LAM1 {ECO:0000303|PubMed:26001273};
 Synonyms=YSP1 {ECO:0000303|PubMed:15657396};
 OrderedLocusNames=YHR155W {ECO:0000312|SGD:S000001198};
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
 Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
 Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
 NCBI_TaxID=559292;
 [1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=ATCC 204508 / S288c;
 PubMed=8091229; DOI=10.1126/science.8091229;
 Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J.,
 Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J.,
 Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y.,
 Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L.,
 Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K.,
 Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R.,
 Vaudin M.;
 "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
 VIII.";
 Science 265:2077-2082(1994).
 [2]
 GENOME REANNOTATION.
 STRAIN=ATCC 204508 / S288c;
 PubMed=24374639; DOI=10.1534/g3.113.008995;
 Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
 Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
 Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
 Cherry J.M.;
 "The reference genome sequence of Saccharomyces cerevisiae: Then and
 now.";
 G3 (Bethesda) 4:389-398(2014).
 [3]
 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
 PubMed=14562095; DOI=10.1038/nature02026;
 Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
 Weissman J.S., O'Shea E.K.;
 "Global analysis of protein localization in budding yeast.";
 Nature 425:686-691(2003).
 [4]
 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
 PubMed=14562106; DOI=10.1038/nature02046;
 Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
 Dephoure N., O'Shea E.K., Weissman J.S.;
 "Global analysis of protein expression in yeast.";
 Nature 425:737-741(2003).
 [5]
 DOMAIN.
 PubMed=15023338; DOI=10.1016/S1097-2765(04)00083-8;
 Yu J.W., Mendrola J.M., Audhya A., Singh S., Keleti D., DeWald D.B.,
 Murray D., Emr S.D., Lemmon M.A.;
 "Genome-wide analysis of membrane targeting by S.cerevisiae pleckstrin
 homology domains.";
 Mol. Cell 13:677-688(2004).
 [6]
 FUNCTION, AND SUBCELLULAR LOCATION.
 PubMed=15657396; DOI=10.1083/jcb.200408145;
 Pozniakovsky A.I., Knorre D.A., Markova O.V., Hyman A.A.,
 Skulachev V.P., Severin F.F.;
 "Role of mitochondria in the pheromone- and amiodarone-induced
 programmed death of yeast.";
 J. Cell Biol. 168:257-269(2005).
 [7]
 FUNCTION.
 PubMed=18800175;
 Lushchak V., Abrat O., Miedzobrodzki J., Semchyshyn H.;
 "Pdr12p-dependent and -independent fluorescein extrusion from baker's
 yeast cells.";
 Acta Biochim. Pol. 55:595-601(2008).
 [8]
 FUNCTION, AND SUBCELLULAR LOCATION.
 PubMed=26001273; DOI=10.7554/eLife.07253;
 Gatta A.T., Wong L.H., Sere Y.Y., Calderon-Norena D.M., Cockcroft S.,
 Menon A.K., Levine T.P.;
 "A new family of StART domain proteins at membrane contact sites has a
 role in ER-PM sterol transport.";
 Elife 4:E07253-E07253(2015).
 -!- FUNCTION: Involved in mitochondrial fragmentation during
     programmed cell death in response to high levels of alpha-factor
     mating pheromone or the drug amiodarone (PubMed:15657396,
     PubMed:18800175). May be involved in sterol transfer between
     intracellular membranes (PubMed:26001273).
     {ECO:0000269|PubMed:15657396, ECO:0000269|PubMed:18800175,
     ECO:0000269|PubMed:26001273}.
 -!- SUBCELLULAR LOCATION: Mitochondrion membrane
     {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15657396};
     Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
     membrane {ECO:0000269|PubMed:26001273}; Single-pass membrane
     protein {ECO:0000255}. Note=Localizes to puncta in the cell
     periphery representing cortical endoplasmic reticulum (cER)-plasma
     membrane (PM) membrane contact sites.
     {ECO:0000269|PubMed:26001273}.
 -!- DOMAIN: The VASt domain bind sterols.
     {ECO:0000250|UniProtKB:P38800}.
 -!- MISCELLANEOUS: Present with 1170 molecules/cell in log phase SD
     medium. {ECO:0000269|PubMed:14562106}.
 -!- SIMILARITY: Belongs to the SIP3 family. {ECO:0000305}.
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 EMBL; U10397; AAB68977.1; -; Genomic_DNA.
 EMBL; BK006934; DAA06848.1; -; Genomic_DNA.
 PIR; S46754; S46754.
 RefSeq; NP_012025.1; NM_001179286.1.
 ProteinModelPortal; P38851; -.
 SMR; P38851; -.
 BioGrid; 36589; 66.
 IntAct; P38851; 1.
 MINT; P38851; -.
 STRING; 4932.YHR155W; -.
 TCDB; 9.B.198.1.1; the membrane-anchored lipid-binding protein (lam) family.
 MaxQB; P38851; -.
 PaxDb; P38851; -.
 PRIDE; P38851; -.
 TopDownProteomics; P38851; -.
 EnsemblFungi; YHR155W_mRNA; YHR155W_mRNA; YHR155W.
 GeneID; 856560; -.
 KEGG; sce:YHR155W; -.
 SGD; S000001198; LAM1.
 GeneTree; ENSGT00940000154887; -.
 HOGENOM; HOG000057112; -.
 InParanoid; P38851; -.
 OrthoDB; EOG092C0B9T; -.
 BioCyc; YEAST:G3O-31190-MONOMER; -.
 PRO; PR:P38851; -.
 Proteomes; UP000002311; Chromosome VIII.
 GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:SGD.
 GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
 GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
 GO; GO:0005739; C:mitochondrion; IDA:SGD.
 GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
 GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
 GO; GO:0015248; F:sterol transporter activity; IC:SGD.
 GO; GO:0032366; P:intracellular sterol transport; IMP:SGD.
 GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
 CDD; cd07609; BAR_SIP3_fungi; 1.
 Gene3D; 1.20.1270.60; -; 1.
 Gene3D; 2.30.29.30; -; 1.
 InterPro; IPR027267; AH/BAR_dom_sf.
 InterPro; IPR011993; PH-like_dom_sf.
 InterPro; IPR001849; PH_domain.
 InterPro; IPR039463; Sip3/Lam1_BAR.
 InterPro; IPR031968; VASt.
 Pfam; PF00169; PH; 1.
 Pfam; PF16016; VASt; 1.
 SMART; SM00233; PH; 1.
 SUPFAM; SSF103657; SSF103657; 1.
 PROSITE; PS50003; PH_DOMAIN; 1.
 PROSITE; PS51778; VAST; 1.
 1: Evidence at protein level;
 Complete proteome; Endoplasmic reticulum; Glycoprotein; Membrane;
 Mitochondrion; Reference proteome; Transmembrane; Transmembrane helix.
 CHAIN         1   1228       Membrane-anchored lipid-binding protein
                              LAM1.
                              /FTId=PRO_0000202927.
 TOPO_DOM      1   1062       Cytoplasmic.
                              {ECO:0000305|PubMed:26001273}.
 TRANSMEM   1063   1083       Helical. {ECO:0000255}.
 TOPO_DOM   1084   1228       Lumenal. {ECO:0000250|UniProtKB:P38717}.
 DOMAIN      308    421       PH. {ECO:0000255|PROSITE-
                              ProRule:PRU00145}.
 DOMAIN      773    978       VASt. {ECO:0000255|PROSITE-
                              ProRule:PRU01114}.
 CARBOHYD   1205   1205       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255|PROSITE-ProRule:PRU00498}.
 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

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