PEX9_YEAST
ID PEX9_YEAST Reviewed; 514 AA.
AC Q04364; D6VZJ2; Q6B2L0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Peroxisomal targeting signal receptor 9 {ECO:0000303|PubMed:27678487};
DE Short=PTS1 receptor 9 {ECO:0000303|PubMed:27678487};
DE Short=PTS1R 9 {ECO:0000303|PubMed:27678487};
DE AltName: Full=Peroxin-9 {ECO:0000303|PubMed:27678487};
GN Name=PEX9 {ECO:0000303|PubMed:27678487}; OrderedLocusNames=YMR018W;
GN ORFNames=YM9711.06;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
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 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 [4]
RP LACK OF INVOLVEMENT IN PTS1 IMPORT.
RX PubMed=11463335; DOI=10.1042/0264-6021:3570635;
RA Amery L., Sano H., Mannaerts G.P., Snider J., Van Looy J., Fransen M.,
RA Van Veldhoven P.P.;
RT "Identification of PEX5p-related novel peroxisome-targeting signal 1
RT (PTS1)-binding proteins in mammals.";
RL Biochem. J. 357:635-646(2001).
RN [5]
RP INTERACTION WITH TLG1.
RX PubMed=11283351; DOI=10.1073/pnas.061034498;
RA Ito T., Chiba T., Ozawa R., Yoshida M., Hattori M., Sakaki Y.;
RT "A comprehensive two-hybrid analysis to explore the yeast protein
RT interactome.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4569-4574(2001).
RN [6]
RP FUNCTION, INTERACTION WITH PEX14; MLS1 AND MLS2, DOMAIN, INDUCTION,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=27678487; DOI=10.1242/jcs.195271;
RA Effelsberg D., Cruz-Zaragoza L.D., Schliebs W., Erdmann R.;
RT "Pex9p is a new yeast peroxisomal import receptor for PTS1-containing
RT proteins.";
RL J. Cell Sci. 129:4057-4066(2016).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27663510; DOI=10.1242/jcs.195255;
RA Yifrach E., Chuartzman S.G., Dahan N., Maskit S., Zada L., Weill U.,
RA Yofe I., Olender T., Schuldiner M., Zalckvar E.;
RT "Characterization of proteome dynamics during growth in oleate reveals a
RT new peroxisome-targeting receptor.";
RL J. Cell Sci. 129:4067-4075(2016).
CC -!- FUNCTION: Peroxisomal import receptor that mediates the peroxisomal
CC import of both malate synthases MLS1 and MLS2 in oleate-grown cells
CC (PubMed:27678487, PubMed:27663510). Recognizes the C-terminal
CC peroxisomal targeting signal PTS1 sequence SKL of MLS1 and MLS2,
CC probably via its TPR domains (PubMed:27678487). Interacts with the
CC PTS1-receptor docking protein PEX14 but not with peroxins PEX1, PEX3
CC through to PEX8, PEX10, PEX11, PEX12, PEX13, PEX15, PEX17, PEX18, PEX19
CC and PEX21 (PubMed:27678487). {ECO:0000269|PubMed:27663510,
CC ECO:0000269|PubMed:27678487}.
CC -!- SUBUNIT: Interacts the PTS1-receptor docking protein PEX14
CC (PubMed:27678487). Interacts with malate synthases MLSL1 and MLS2
CC (PubMed:27678487). Interacts with TLG1 (PubMed:11283351).
CC {ECO:0000269|PubMed:11283351, ECO:0000269|PubMed:27678487}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27678487}.
CC Peroxisome membrane {ECO:0000269|PubMed:27663510,
CC ECO:0000269|PubMed:27678487}; Peripheral membrane protein
CC {ECO:0000269|PubMed:27663510, ECO:0000269|PubMed:27678487}.
CC -!- INDUCTION: Expression is induced by oleate.
CC {ECO:0000269|PubMed:27678487}.
CC -!- DOMAIN: The WxxxF motif is involved in the interaction with the PTS1-
CC receptor docking protein PEX14. {ECO:0000269|PubMed:27678487}.
CC -!- DOMAIN: The TPR repeats are involved in the interaction with the C-
CC terminal peroxisomal targeting signal PTS1 of MLS1 and MLS2.
CC {ECO:0000269|PubMed:27678487}.
CC -!- DISRUPTION PHENOTYPE: Leads to a clear mislocalization of both MLS1 and
CC MLS2 to the cytosol. {ECO:0000269|PubMed:27678487}.
CC -!- SIMILARITY: Belongs to the peroxisomal targeting signal receptor
CC family. {ECO:0000305}.
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DR EMBL; Z49211; CAA89120.1; -; Genomic_DNA.
DR EMBL; AY692720; AAT92739.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09916.1; -; Genomic_DNA.
DR PIR; S54019; S54019.
DR RefSeq; NP_013731.1; NM_001182514.1.
DR AlphaFoldDB; Q04364; -.
DR SMR; Q04364; -.
DR BioGRID; 35189; 119.
DR DIP; DIP-4510N; -.
DR IntAct; Q04364; 2.
DR MINT; Q04364; -.
DR STRING; 4932.YMR018W; -.
DR PaxDb; Q04364; -.
DR PRIDE; Q04364; -.
DR EnsemblFungi; YMR018W_mRNA; YMR018W; YMR018W.
DR GeneID; 855032; -.
DR KEGG; sce:YMR018W; -.
DR SGD; S000004620; PEX9.
DR VEuPathDB; FungiDB:YMR018W; -.
DR eggNOG; KOG1125; Eukaryota.
DR GeneTree; ENSGT00940000169247; -.
DR HOGENOM; CLU_560444_0_0_1; -.
DR InParanoid; Q04364; -.
DR OMA; PSHINAW; -.
DR BioCyc; YEAST:G3O-32724-MON; -.
DR PRO; PR:Q04364; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04364; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:SGD.
DR GO; GO:0005777; C:peroxisome; IDA:SGD.
DR GO; GO:0005052; F:peroxisome matrix targeting signal-1 binding; ISS:SGD.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IMP:SGD.
DR GO; GO:0016560; P:protein import into peroxisome matrix, docking; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR024111; PEX5/PEX5L.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR10130; PTHR10130; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 4.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Membrane; Peroxisome; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..514
FT /note="Peroxisomal targeting signal receptor 9"
FT /id="PRO_0000106320"
FT REPEAT 174..207
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 218..252
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 254..286
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REPEAT 288..320
FT /note="TPR 4"
FT /evidence="ECO:0000255"
FT REPEAT 326..359
FT /note="TPR 5"
FT /evidence="ECO:0000255"
FT REPEAT 360..393
FT /note="TPR 6"
FT /evidence="ECO:0000255"
FT REPEAT 394..427
FT /note="TPR 7"
FT /evidence="ECO:0000255"
FT REPEAT 429..461
FT /note="TPR 8"
FT /evidence="ECO:0000255"
FT MOTIF 91..95
FT /note="WxxxF motif"
FT /evidence="ECO:0000305|PubMed:27678487"
FT CONFLICT 9
FT /note="T -> P (in Ref. 3; AAT92739)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 514 AA; 59065 MW; 8A1302220602B64A CRC64;
MNEVTCSITG DNPIHKINNG LGLKWNNLGK FSDFQTNDSA ARDARTIDYI FTNCQTGSSI
GKIDFRAALP ADKSQHSGVS EKEFSRLENQ WSKEFSCFPK NKNADVTKPS RNKHEKRSAN
LHNRYFAQYY STAYQQNRIY PCRISYNEHS SVSNGWEFQF KSIENQLLNE LKIENNVEEK
TVGYEYVAEY EETIDFMHML SSVPQTYQFL KSNIYITERD PYKIGCVLMD NGSNLNEVVM
AFEAAISQDP SHINAWLKLG IVNFENESES NGELALRNCL NLDPNNTIAL ENLAIHHINQ
QNESESLKLF HKWILSKFSK VFQPSAGENK DSINKIPKKA HLAHILESLL NMGIEKKDQY
DIYSVLSILY YSDQKIKQSQ KCLEFLLLEK PNNGTIWNRY GAILANTKSY HSAINAYNKC
KQLRPNFTRV RYNLAIAYMN KGDYVKASKM LIEVILLRSK GYEHNKAKMQ NKFMQNLKNA
LIASKNFDSL DLINGSHNTE SLISTLKAIY NKMD
