PEX5_YEAST
ID PEX5_YEAST Reviewed; 612 AA.
AC P35056; D6VSM4;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Peroxisomal targeting signal receptor;
DE Short=PTS1 receptor;
DE Short=PTS1R;
DE AltName: Full=Peroxin-5;
DE AltName: Full=Peroxisomal protein PAS10;
GN Name=PEX5; Synonyms=PAS10; OrderedLocusNames=YDR244W; ORFNames=YD8419.11;
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=8265627; DOI=10.1073/pnas.90.24.11782;
RA van der Leij I., Franse M.M., Elgersma Y., Distel B., Tabak H.F.;
RT "PAS10 is a tetratricopeptide-repeat protein that is essential for the
RT import of most matrix proteins into peroxisomes of Saccharomyces
RT cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:11782-11786(1993).
RN [2]
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 [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 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 [6]
RP ACETYLATION AT MET-1, UBIQUITINATION AT CYS-6; LYS-18 AND LYS-24,
RP MUTAGENESIS OF CYS-6; LYS-18 AND LYS-24, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=17550898; DOI=10.1074/jbc.m702038200;
RA Williams C., van den Berg M., Sprenger R.R., Distel B.;
RT "A conserved cysteine is essential for Pex4p-dependent ubiquitination of
RT the peroxisomal import receptor Pex5p.";
RL J. Biol. Chem. 282:22534-22543(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Binds to the C-terminal PTS1-type tripeptide peroxisomal
CC targeting signal (SKL-type) and plays an essential role in peroxisomal
CC protein import.
CC -!- INTERACTION:
CC P35056; P80667: PEX13; NbExp=6; IntAct=EBI-13170, EBI-13206;
CC P35056; P53112: PEX14; NbExp=8; IntAct=EBI-13170, EBI-13212;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Peroxisome membrane; Peripheral
CC membrane protein. Note=Its distribution appears to be dynamic. It is
CC probably a cycling receptor found mainly in the cytoplasm and as well
CC associated to the peroxisomal membrane through a docking factor
CC (PEX13).
CC -!- PTM: Ubiquitination at Cys-6 is UBC4-independent but requires the
CC presence of PEX4. Ubiquitination at Lys-18 and Lys-24 are UBC4-
CC dependent. {ECO:0000269|PubMed:17550898}.
CC -!- MISCELLANEOUS: Present with 2070 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peroxisomal targeting signal receptor
CC family. {ECO:0000305}.
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DR EMBL; L23076; AAA64794.1; -; Genomic_DNA.
DR EMBL; Z49701; CAA89730.1; -; Genomic_DNA.
DR EMBL; AY723785; AAU09702.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12084.1; -; Genomic_DNA.
DR PIR; A49403; A49403.
DR RefSeq; NP_010530.1; NM_001180552.1.
DR AlphaFoldDB; P35056; -.
DR SMR; P35056; -.
DR BioGRID; 32295; 234.
DR DIP; DIP-2475N; -.
DR ELM; P35056; -.
DR IntAct; P35056; 15.
DR MINT; P35056; -.
DR STRING; 4932.YDR244W; -.
DR TCDB; 3.A.20.1.5; the peroxisomal protein importer (ppi) family.
DR iPTMnet; P35056; -.
DR MaxQB; P35056; -.
DR PaxDb; P35056; -.
DR PRIDE; P35056; -.
DR EnsemblFungi; YDR244W_mRNA; YDR244W; YDR244W.
DR GeneID; 851831; -.
DR KEGG; sce:YDR244W; -.
DR SGD; S000002652; PEX5.
DR VEuPathDB; FungiDB:YDR244W; -.
DR eggNOG; KOG1125; Eukaryota.
DR GeneTree; ENSGT00940000169247; -.
DR HOGENOM; CLU_013516_3_0_1; -.
DR InParanoid; P35056; -.
DR OMA; SQFTKHV; -.
DR BioCyc; YEAST:G3O-29817-MON; -.
DR Reactome; R-SCE-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-SCE-9033241; Peroxisomal protein import.
DR Reactome; R-SCE-9664873; Pexophagy.
DR PRO; PR:P35056; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P35056; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:1990429; C:peroxisomal importomer complex; 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; IDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:SGD.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IGI:SGD.
DR GO; GO:0016560; P:protein import into peroxisome matrix, docking; IMP:SGD.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR024111; PEX5/PEX5L.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR10130; PTHR10130; 1.
DR Pfam; PF00515; TPR_1; 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 Acetylation; Cytoplasm; Isopeptide bond; Membrane; Peroxisome;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Thioester bond; TPR repeat; Transport; Ubl conjugation.
FT CHAIN 1..612
FT /note="Peroxisomal targeting signal receptor"
FT /id="PRO_0000106316"
FT REPEAT 64..97
FT /note="TPR 1"
FT REPEAT 313..346
FT /note="TPR 2"
FT REPEAT 347..380
FT /note="TPR 3"
FT REPEAT 381..418
FT /note="TPR 4"
FT REPEAT 419..456
FT /note="TPR 5"
FT REPEAT 457..490
FT /note="TPR 6"
FT REPEAT 491..524
FT /note="TPR 7"
FT REPEAT 525..558
FT /note="TPR 8"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:17550898"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 6
FT /note="Glycyl cysteine thioester (Cys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:17550898"
FT CROSSLNK 18
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:17550898"
FT CROSSLNK 24
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:17550898"
FT MUTAGEN 6
FT /note="C->R: Loss of UBE2D2-independent ubiquitination."
FT /evidence="ECO:0000269|PubMed:17550898"
FT MUTAGEN 18
FT /note="K->R: Loss of UBE2D2-dependent ubiquitination. No
FT effect on its function."
FT /evidence="ECO:0000269|PubMed:17550898"
FT MUTAGEN 24
FT /note="K->R: Loss of UBE2D2-dependent ubiquitination. No
FT effect on its function."
FT /evidence="ECO:0000269|PubMed:17550898"
SQ SEQUENCE 612 AA; 69324 MW; 553251971E0BFD8D CRC64;
MDVGSCSVGN NPLAQLHKHT QQNKSLQFNQ KNNGRLNESP LQGTNKPGIS EAFISNVNAI
SQENMANMQR FINGEPLIDD KRRMEIGPSS GRLPPFSNVH SLQTSANPTQ IKGVNDISHW
SQEFQGSNSI QNRNADTGNS EKAWQRGSTT ASSRFQYPNT MMNNYAYASM NSLSGSRLQS
PAFMNQQQSG RSKEGVNEQE QQPWTDQFEK LEKEVSENLD INDEIEKEEN VSEVEQNKPE
TVEKEEGVYG DQYQSDFQEV WDSIHKDAEE VLPSELVNDD LNLGEDYLKY LGGRVNGNIE
YAFQSNNEYF NNPNAYKIGC LLMENGAKLS EAALAFEAAV KEKPDHVDAW LRLGLVQTQN
EKELNGISAL EECLKLDPKN LEAMKTLAIS YINEGYDMSA FTMLDKWAET KYPEIWSRIK
QQDDKFQKEK GFTHIDMNAH ITKQFLQLAN NLSTIDPEIQ LCLGLLFYTK DDFDKTIDCF
ESALRVNPND ELMWNRLGAS LANSNRSEEA IQAYHRALQL KPSFVRARYN LAVSSMNIGC
FKEAAGYLLS VLSMHEVNTN NKKGDVGSLL NTYNDTVIET LKRVFIAMNR DDLLQEVKPG
MDLKRFKGEF SF
