LPX1_YEAST
ID LPX1_YEAST Reviewed; 387 AA.
AC Q12405; D6W2E6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Peroxisomal membrane protein LPX1;
DE EC=3.1.1.-;
DE AltName: Full=Lipase of peroxisomes protein 1;
GN Name=LPX1; OrderedLocusNames=YOR084W; ORFNames=YOR3120W;
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 [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=12135984; DOI=10.1083/jcb.200204059;
RA Smith J.J., Marelli M., Christmas R.H., Vizeacoumar F.J., Dilworth D.J.,
RA Ideker T., Galitski T., Dimitrov K., Rachubinski R.A., Aitchison J.D.;
RT "Transcriptome profiling to identify genes involved in peroxisome assembly
RT and function.";
RL J. Cell Biol. 158:259-271(2002).
RN [6]
RP INDUCTION.
RX PubMed=14512416; DOI=10.1074/jbc.m309580200;
RA Lucau-Danila A., Delaveau T., Lelandais G., Devaux F., Jacq C.;
RT "Competitive promoter occupancy by two yeast paralogous transcription
RT factors controlling the multidrug resistance phenomenon.";
RL J. Biol. Chem. 278:52641-52650(2003).
RN [7]
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 [8]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, INDUCTION,
RP DISRUPTION PHENOTYPE, REGION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18199283; DOI=10.1111/j.1742-4658.2007.06217.x;
RA Thoms S., Debelyy M.O., Nau K., Meyer H.E., Erdmann R.;
RT "Lpx1p is a peroxisomal lipase required for normal peroxisome morphology.";
RL FEBS J. 275:504-514(2008).
RN [9]
RP INDUCTION.
RX PubMed=19235764; DOI=10.1002/yea.1655;
RA Roberts G.G. III, Hudson A.P.;
RT "Rsf1p is required for an efficient metabolic shift from fermentative to
RT glycerol-based respiratory growth in S. cerevisiae.";
RL Yeast 26:95-110(2009).
CC -!- FUNCTION: Has acyl esterase, lipase and phospholipase A activity.
CC {ECO:0000269|PubMed:18199283}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.3 uM for p-nitrophenyl butyrate (PNB)
CC {ECO:0000269|PubMed:18199283};
CC Vmax=5.6 pmol/h/ug enzyme toward 1,2-dioleoyl-3-(pyren-1-yl)decanoyl-
CC rac-glycerol (DPG) {ECO:0000269|PubMed:18199283};
CC Vmax=7.9 pmol/h/ug enzyme toward 1,2-bis-(4,4-difluoro-5,7-dimethyl-
CC 4-bora-3a,4a-diaza-sindacene-3-undecanoyl)-sn-glycero-3-
CC phosphocholine (BPC) {ECO:0000269|PubMed:18199283};
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:12135984,
CC ECO:0000269|PubMed:18199283}. Note=Peroxisomal import is dependent on
CC the peroxisomal targeting signal type 1 (PTS1) receptor PEX5 and on
CC self-interaction.
CC -!- INDUCTION: By oleic acid. Transcriptionally up-regulated by YRM1 along
CC with genes involved in multidrug resistance. Expression is also
CC dependent on RSF1 and RSF2 for transcriptional induction during growth
CC on glycerol-based medium. {ECO:0000269|PubMed:12135984,
CC ECO:0000269|PubMed:14512416, ECO:0000269|PubMed:18199283,
CC ECO:0000269|PubMed:19235764}.
CC -!- DISRUPTION PHENOTYPE: Aberrant morphology characterized by
CC intraperoxisomal vesicles or invaginations.
CC {ECO:0000269|PubMed:18199283}.
CC -!- MISCELLANEOUS: Present with 2350 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X94335; CAA64006.1; -; Genomic_DNA.
DR EMBL; Z74992; CAA99279.1; -; Genomic_DNA.
DR EMBL; AY692642; AAT92661.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10862.1; -; Genomic_DNA.
DR PIR; S61645; S61645.
DR RefSeq; NP_014727.1; NM_001183503.1.
DR PDB; 2Y6U; X-ray; 1.90 A; A=1-387.
DR PDB; 2Y6V; X-ray; 2.83 A; A/B/C=1-387.
DR PDBsum; 2Y6U; -.
DR PDBsum; 2Y6V; -.
DR AlphaFoldDB; Q12405; -.
DR SMR; Q12405; -.
DR BioGRID; 34482; 64.
DR DIP; DIP-2772N; -.
DR IntAct; Q12405; 3.
DR MINT; Q12405; -.
DR STRING; 4932.YOR084W; -.
DR ESTHER; yeast-YOR084W; 6_AlphaBeta_hydrolase.
DR MEROPS; S33.022; -.
DR iPTMnet; Q12405; -.
DR PaxDb; Q12405; -.
DR PRIDE; Q12405; -.
DR EnsemblFungi; YOR084W_mRNA; YOR084W; YOR084W.
DR GeneID; 854251; -.
DR KEGG; sce:YOR084W; -.
DR SGD; S000005610; LPX1.
DR VEuPathDB; FungiDB:YOR084W; -.
DR eggNOG; ENOG502QT3R; Eukaryota.
DR HOGENOM; CLU_061432_0_0_1; -.
DR InParanoid; Q12405; -.
DR OMA; DQVTHGD; -.
DR BioCyc; YEAST:G3O-33620-MON; -.
DR PRO; PR:Q12405; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12405; protein.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005782; C:peroxisomal matrix; IDA:SGD.
DR GO; GO:0016298; F:lipase activity; IBA:GO_Central.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:SGD.
DR GO; GO:0019433; P:triglyceride catabolic process; IGI:SGD.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Peroxisome; Reference proteome.
FT CHAIN 1..387
FT /note="Peroxisomal membrane protein LPX1"
FT /id="PRO_0000270570"
FT REGION 385..387
FT /note="Peroxisomal targeting signal type 1"
FT STRAND 5..14
FT /evidence="ECO:0007829|PDB:2Y6U"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:2Y6U"
FT STRAND 32..41
FT /evidence="ECO:0007829|PDB:2Y6U"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:2Y6U"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:2Y6U"
FT HELIX 65..74
FT /evidence="ECO:0007829|PDB:2Y6U"
FT TURN 80..83
FT /evidence="ECO:0007829|PDB:2Y6U"
FT STRAND 84..92
FT /evidence="ECO:0007829|PDB:2Y6U"
FT HELIX 98..103
FT /evidence="ECO:0007829|PDB:2Y6U"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:2Y6U"
FT HELIX 114..128
FT /evidence="ECO:0007829|PDB:2Y6U"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:2Y6V"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:2Y6U"
FT HELIX 146..157
FT /evidence="ECO:0007829|PDB:2Y6U"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:2Y6U"
FT HELIX 194..202
FT /evidence="ECO:0007829|PDB:2Y6U"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:2Y6U"
FT HELIX 211..220
FT /evidence="ECO:0007829|PDB:2Y6U"
FT TURN 223..226
FT /evidence="ECO:0007829|PDB:2Y6U"
FT HELIX 229..239
FT /evidence="ECO:0007829|PDB:2Y6U"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:2Y6U"
FT HELIX 259..264
FT /evidence="ECO:0007829|PDB:2Y6U"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:2Y6U"
FT HELIX 273..279
FT /evidence="ECO:0007829|PDB:2Y6U"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:2Y6U"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:2Y6U"
FT HELIX 300..309
FT /evidence="ECO:0007829|PDB:2Y6U"
FT STRAND 311..318
FT /evidence="ECO:0007829|PDB:2Y6U"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:2Y6U"
FT HELIX 330..347
FT /evidence="ECO:0007829|PDB:2Y6U"
FT HELIX 360..378
FT /evidence="ECO:0007829|PDB:2Y6U"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:2Y6V"
SQ SEQUENCE 387 AA; 43727 MW; D7880389F62E9AC2 CRC64;
MEQNRFKKET KTCSASWPRA PQSTLCATDR LELTYDVYTS AERQRRSRTA TRLNLVFLHG
SGMSKVVWEY YLPRLVAADA EGNYAIDKVL LIDQVNHGDS AVRNRGRLGT NFNWIDGARD
VLKIATCELG SIDSHPALNV VIGHSMGGFQ ALACDVLQPN LFHLLILIEP VVITRKAIGA
GRPGLPPDSP QIPENLYNSL RLKTCDHFAN ESEYVKYMRN GSFFTNAHSQ ILQNIIDFER
TKASGDDEDG GPVRTKMEQA QNLLCYMNMQ TFAPFLISNV KFVRKRTIHI VGARSNWCPP
QNQLFLQKTL QNYHLDVIPG GSHLVNVEAP DLVIERINHH IHEFVLTSPL QSSHIPQLTL
EERAVMFDRA FDSFKNEALV KTTKQKL
