PEX5_YARLI
ID PEX5_YARLI Reviewed; 598 AA.
AC Q99144;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Peroxisomal targeting signal receptor;
DE Short=PTS1 receptor;
DE Short=PTS1R;
DE AltName: Full=Peroxin-5;
DE AltName: Full=Peroxisomal protein PAY32;
GN Name=PAY32; Synonyms=PEX5; OrderedLocusNames=YALI0F28457g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=E 122;
RX PubMed=8522603; DOI=10.1083/jcb.131.6.1453;
RA Szilard R.K., Titorenko V.I., Veenhuis M., Rachubinski R.A.;
RT "Pay32p of the yeast Yarrowia lipolytica is an intraperoxisomal component
RT of the matrix protein translocation machinery.";
RL J. Cell Biol. 131:1453-1469(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 -!- 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-10 is UBC4-independent but requires the
CC presence of PEX4. Ubiquitination at Lys-22 is UBC4-dependent (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peroxisomal targeting signal receptor
CC family. {ECO:0000305}.
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DR EMBL; U28155; AAA85166.1; -; Genomic_DNA.
DR EMBL; CR382132; CAG78803.1; -; Genomic_DNA.
DR RefSeq; XP_505991.1; XM_505991.1.
DR AlphaFoldDB; Q99144; -.
DR SMR; Q99144; -.
DR STRING; 4952.CAG78803; -.
DR EnsemblFungi; CAG78803; CAG78803; YALI0_F28457g.
DR GeneID; 2908530; -.
DR KEGG; yli:YALI0F28457g; -.
DR VEuPathDB; FungiDB:YALI0_F28457g; -.
DR HOGENOM; CLU_013516_3_0_1; -.
DR InParanoid; Q99144; -.
DR OMA; SQFTKHV; -.
DR Proteomes; UP000001300; Chromosome F.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0005052; F:peroxisome matrix targeting signal-1 binding; IBA:GO_Central.
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; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR10130; PTHR10130; 1.
DR Pfam; PF00515; TPR_1; 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 3: Inferred from homology;
KW Cytoplasm; Isopeptide bond; Membrane; Peroxisome; Protein transport;
KW Reference proteome; Repeat; Thioester bond; TPR repeat; Transport;
KW Ubl conjugation.
FT CHAIN 1..598
FT /note="Peroxisomal targeting signal receptor"
FT /id="PRO_0000106315"
FT REPEAT 304..337
FT /note="TPR 1"
FT REPEAT 338..371
FT /note="TPR 2"
FT REPEAT 372..409
FT /note="TPR 3"
FT REPEAT 410..447
FT /note="TPR 4"
FT REPEAT 448..481
FT /note="TPR 5"
FT REPEAT 482..515
FT /note="TPR 6"
FT REPEAT 516..549
FT /note="TPR 7"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 10
FT /note="Glycyl cysteine thioester (Cys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 598 AA; 66601 MW; 6E47CB9EEB97BFC5 CRC64;
MSFMRGGSEC STGRNPLSQF TKHTAEDRSL QHDRVAGPSG GRVGGMRSNT GEMSQQDREM
MARFGAAGPE QSSFNYEQMR HELHNMGAQG GQIPQVPSQQ GAANGGQWAR DFGGQQTAPG
AAPQDAKNWN AEFQRGGSPA EAMQQQGPGP MQGGMGMGGM PMYGMARPMY SGMSANMAPQ
FQPQQANARV VELDEQNWEE QFKQMDSAVG KGKEVEEQTA ETATATETVT ETETTTEDKP
MDIKNMDFEN IWKNLQVNVL DNMDEWLEET NSPAWERDFH EYTHNRPEFA DYQFEENNQF
MEHPDPFKIG VELMETGGRL SEAALAFEAA VQKNTEHAEA WGRLGACQAQ NEKEDPAIRA
LERCIKLEPG NLSALMNLSV SYTNEGYENA AYATLERWLA TKYPEVVDQA RNQEPRLGNE
DKFQLHSRVT ELFIRAAQLS PDGANIDADV QVGLGVLFYG NEEYDKAIDC FNAAIAVRPD
DALLWNRLGA TLANSHRSEE AIDAYYKALE LRPSFVRARY NLGVSCINIG CYKEAAQYLL
GALSMHKVEG VQDDVLANQS TNLYDTLKRV FLGMDRRDLV AKVGNGMDVN QFRNEFEF
