ID PEX7_YEAST Reviewed; 375 AA. AC P39108; D6VSC5; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 27-MAR-2024, entry version 188. DE RecName: Full=Peroxisomal targeting signal 2 receptor {ECO:0000305}; DE Short=PTS2 receptor; DE AltName: Full=Peroxin-7 {ECO:0000305}; GN Name=PEX7 {ECO:0000312|SGD:S000002549}; GN Synonyms=PAS7 {ECO:0000303|PubMed:7957058}, PEB1 GN {ECO:0000303|PubMed:7535304}; OrderedLocusNames=YDR142C; GN ORFNames=YD2943.01C, YD9302.18C; 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], FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=7957058; DOI=10.1002/j.1460-2075.1994.tb06818.x; RA Marzioch M., Erdmann R., Veenhuis M., Kunau W.-H.; RT "PAS7 encodes a novel yeast member of the WD-40 protein family essential RT for import of 3-oxoacyl-CoA thiolase, a PTS2-containing protein, into RT peroxisomes."; RL EMBO J. 13:4908-4918(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION. RC STRAIN=S288c / GRF88; RX PubMed=7535304; DOI=10.1083/jcb.129.1.65; RA Zhang J.W., Lazarow P.B.; RT "PEB1 (PAS7) in Saccharomyces cerevisiae encodes a hydrophilic, intra- RT peroxisomal protein that is a member of the WD repeat family and is RT essential for the import of thiolase into peroxisomes."; RL J. Cell Biol. 129:65-80(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169867; RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., RA Mewes H.-W., Zollner A., Zaccaria P.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."; RL Nature 387:75-78(1997). RN [4] 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 [5] 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 [6] RP FUNCTION. RX PubMed=9094717; DOI=10.1016/s0092-8674(00)80185-3; RA Albertini M., Rehling P., Erdmann R., Girzalsky W., Kiel J.A.K.W., RA Veenhuis M., Kunau W.-H.; RT "Pex14p, a peroxisomal membrane protein binding both receptors of the two RT PTS-dependent import pathways."; RL Cell 89:83-92(1997). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3; RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M., RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E., RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.; RT "Assigning function to yeast proteins by integration of technologies."; RL Mol. Cell 12:1353-1365(2003). RN [8] 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 [9] {ECO:0007744|PDB:3W15} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH PEX21 AND PTS2-TYPE RP PEROXISOMAL TARGETING SIGNAL, FUNCTION, INTERACTION WITH PEX21, AND RP MUTAGENESIS OF 32-PHE--LEU-34; LEU-34; ASP-61; GLU-106; PHE-344 AND RP TRP-364. RX PubMed=23812376; DOI=10.1038/nsmb.2618; RA Pan D., Nakatsu T., Kato H.; RT "Crystal structure of peroxisomal targeting signal-2 bound to its receptor RT complex Pex7p-Pex21p."; RL Nat. Struct. Mol. Biol. 20:987-993(2013). CC -!- FUNCTION: Receptor required for the peroxisomal import of proteins CC containing a C-terminal PTS2-type peroxisomal targeting signal, such as CC 3-oxoacyl-CoA thiolase (PubMed:7957058, PubMed:7535304, CC PubMed:23812376). Specifically binds to cargo proteins containing a CC PTS2 peroxisomal targeting signal in the cytosol (PubMed:23812376). CC Cargo protein-binding triggers interaction with PEX21 and formation of CC a ternary complex composed of PEX21 and PEX7 along with PTS2-containing CC cargo proteins, which is tranlocated into peroxisomes by passing CC through the PEX13-PEX14 docking complex (PubMed:9094717, CC PubMed:23812376). {ECO:0000269|PubMed:23812376, CC ECO:0000269|PubMed:7535304, ECO:0000269|PubMed:7957058, CC ECO:0000269|PubMed:9094717}. CC -!- SUBUNIT: Interacts with PEX21. {ECO:0000269|PubMed:23812376}. CC -!- INTERACTION: CC P39108; P38855: PEX18; NbExp=6; IntAct=EBI-13183, EBI-24803; CC P39108; P50091: PEX21; NbExp=13; IntAct=EBI-13183, EBI-23549; CC P39108; P27796: POT1; NbExp=5; IntAct=EBI-13183, EBI-19236; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:7957058}. CC Peroxisome matrix {ECO:0000269|PubMed:7535304, CC ECO:0000269|PubMed:7957058}. CC -!- MISCELLANEOUS: Present with 589 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the WD repeat peroxin-7 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X81424; CAA57183.1; -; Genomic_DNA. DR EMBL; X83704; CAA58677.1; -; Genomic_DNA. DR EMBL; Z54139; CAA90811.1; -; Genomic_DNA. DR EMBL; Z48179; CAA88224.1; -; Genomic_DNA. DR EMBL; AY557700; AAS56026.1; -; Genomic_DNA. DR EMBL; BK006938; DAA11985.1; -; Genomic_DNA. DR PIR; S50228; S50228. DR RefSeq; NP_010426.1; NM_001180449.1. DR PDB; 3W15; X-ray; 1.80 A; A=1-375. DR PDBsum; 3W15; -. DR AlphaFoldDB; P39108; -. DR SMR; P39108; -. DR BioGRID; 32196; 80. DR ComplexPortal; CPX-1905; Peroxisomal PEX7-PEX18 receptor complex. DR ComplexPortal; CPX-1906; Peroxisomal PEX7-PEX21 receptor complex. DR DIP; DIP-1501N; -. DR IntAct; P39108; 56. DR MINT; P39108; -. DR STRING; 4932.YDR142C; -. DR TCDB; 3.A.20.1.5; the peroxisomal protein importer (ppi) family. DR iPTMnet; P39108; -. DR MaxQB; P39108; -. DR PaxDb; 4932-YDR142C; -. DR PeptideAtlas; P39108; -. DR EnsemblFungi; YDR142C_mRNA; YDR142C; YDR142C. DR GeneID; 851720; -. DR KEGG; sce:YDR142C; -. DR AGR; SGD:S000002549; -. DR SGD; S000002549; PEX7. DR VEuPathDB; FungiDB:YDR142C; -. DR eggNOG; KOG0277; Eukaryota. DR HOGENOM; CLU_046581_1_0_1; -. DR InParanoid; P39108; -. DR OMA; FAVHWNL; -. DR OrthoDB; 5474268at2759; -. DR BioCyc; YEAST:G3O-29739-MONOMER; -. DR Reactome; R-SCE-9033241; Peroxisomal protein import. DR BioGRID-ORCS; 851720; 0 hits in 10 CRISPR screens. DR PRO; PR:P39108; -. DR Proteomes; UP000002311; Chromosome IV. DR RNAct; P39108; Protein. DR GO; GO:0062137; C:cargo receptor complex; IPI:ComplexPortal. DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal. DR GO; GO:0005829; C:cytosol; IDA:SGD. DR GO; GO:0005782; C:peroxisomal matrix; IBA:GO_Central. DR GO; GO:0005778; C:peroxisomal membrane; IDA:ComplexPortal. DR GO; GO:0005777; C:peroxisome; IDA:SGD. DR GO; GO:0005053; F:peroxisome matrix targeting signal-2 binding; IDA:UniProtKB. DR GO; GO:0016558; P:protein import into peroxisome matrix; IBA:GO_Central. DR GO; GO:0016560; P:protein import into peroxisome matrix, docking; IPI:SGD. DR GO; GO:0006625; P:protein targeting to peroxisome; IEA:UniProt. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR020472; G-protein_beta_WD-40_rep. DR InterPro; IPR044536; PEX7. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR46027; PEROXISOMAL TARGETING SIGNAL 2 RECEPTOR; 1. DR PANTHER; PTHR46027:SF1; PEROXISOMAL TARGETING SIGNAL 2 RECEPTOR; 1. DR Pfam; PF00400; WD40; 3. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00320; WD40; 6. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS00678; WD_REPEATS_1; 2. DR PROSITE; PS50082; WD_REPEATS_2; 3. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Peroxisome; Protein transport; Reference proteome; KW Repeat; Transport; WD repeat. FT CHAIN 1..375 FT /note="Peroxisomal targeting signal 2 receptor" FT /id="PRO_0000051120" FT REPEAT 58..89 FT /note="WD 1" FT REPEAT 102..133 FT /note="WD 2" FT REPEAT 172..203 FT /note="WD 3" FT REPEAT 218..249 FT /note="WD 4" FT REPEAT 281..312 FT /note="WD 5" FT REPEAT 340..372 FT /note="WD 6" FT MUTAGEN 32..34 FT /note="FGL->AGA: Decreased formation of a ternary complex FT composed of PEX21 and PEX7 along with PTS2-containing cargo FT proteins." FT /evidence="ECO:0000269|PubMed:23812376" FT MUTAGEN 34 FT /note="L->A: Does not prevent peroxisomal import of FT proteins containing a C-terminal PTS2-type peroxisomal FT targeting signal, such as 3-oxoacyl-CoA thiolase." FT /evidence="ECO:0000269|PubMed:23812376" FT MUTAGEN 34 FT /note="L->D: Decreased formation of a ternary complex FT composed of PEX21 and PEX7 along with PTS2-containing cargo FT proteins." FT /evidence="ECO:0000269|PubMed:23812376" FT MUTAGEN 61 FT /note="D->R: Abolished ability to mediate peroxisomal FT import of proteins containing a C-terminal PTS2-type FT peroxisomal targeting signal; when associated with H-106." FT /evidence="ECO:0000269|PubMed:23812376" FT MUTAGEN 106 FT /note="E->H: Abolished ability to mediate peroxisomal FT import of proteins containing a C-terminal PTS2-type FT peroxisomal targeting signal; when associated with R-61." FT /evidence="ECO:0000269|PubMed:23812376" FT MUTAGEN 344 FT /note="F->A: Does not prevent peroxisomal import of FT proteins containing a C-terminal PTS2-type peroxisomal FT targeting signal, such as 3-oxoacyl-CoA thiolase. Decreased FT formation of a ternary complex composed of PEX21 and PEX7 FT along with PTS2-containing cargo proteins; when associated FT with A-364." FT /evidence="ECO:0000269|PubMed:23812376" FT MUTAGEN 364 FT /note="W->A: Decreased formation of a ternary complex FT composed of PEX21 and PEX7 along with PTS2-containing cargo FT proteins; when associated with A-344." FT /evidence="ECO:0000269|PubMed:23812376" FT STRAND 2..5 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 9..16 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 23..30 FT /evidence="ECO:0007829|PDB:3W15" FT HELIX 31..33 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 38..45 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 51..61 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 63..68 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 75..80 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 83..89 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 97..101 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 107..112 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 114..118 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 120..124 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 129..132 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 140..143 FT /evidence="ECO:0007829|PDB:3W15" FT HELIX 148..153 FT /evidence="ECO:0007829|PDB:3W15" FT HELIX 158..160 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 177..182 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 189..194 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 197..203 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 210..216 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 223..228 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 235..240 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 245..249 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 274..278 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 281..284 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 286..291 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 298..303 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 308..312 FT /evidence="ECO:0007829|PDB:3W15" FT TURN 326..328 FT /evidence="ECO:0007829|PDB:3W15" FT TURN 330..333 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 334..338 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 345..350 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 352..355 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 358..363 FT /evidence="ECO:0007829|PDB:3W15" FT STRAND 366..372 FT /evidence="ECO:0007829|PDB:3W15" SQ SEQUENCE 375 AA; 42323 MW; 7D53A42A8ACF23F9 CRC64; MLRYHMQGFS GYGVQYSPFF DNRLAVAAGS NFGLVGNGKL FILEIDRSGR IVEVNSFLTQ DCLFDLAWNE SHENQVLVAQ GDGTLRLFDT TFKEFPIAIF KEHEREVFSC NWNLVNRQNF LSSSWDGSIK IWSPLRKQSL MTLTPRPLEI TKMVDPLNAI ILKKKSFTGI SKNRNCVYQA QFSPHDQNLV LSCSGNSYAS LFDIRLPSGK NQNNFLVHSG LEALTCDFNK YRPYVVATGG VDNAIRIWDI RMLNKNESAT IKRTVPGQLH NSSCINEIPN AHGLAIRKVT WSPHHSNILM SASYDMTCRI WRDLSNDGAK ETYKTNSTDA TKGSIFNFTQ HSEFVFGADW SLWGKPGYVA STAWDGNLFV WNGLG //