ID   PEX5_ASHGO              Reviewed;         569 AA.
AC   Q752X0;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 5.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Peroxisomal targeting signal receptor;
DE            Short=PTS1 receptor;
DE            Short=PTS1R;
DE   AltName: Full=Peroxin-5;
GN   Name=PEX5; OrderedLocusNames=AFR453W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 281 AND 301.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Peroxisome membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Its
CC       distribution appears to be dynamic. It is probably a cycling receptor
CC       found mainly in the cytoplasm and as well associated to the peroxisomal
CC       membrane (By similarity). {ECO:0000250}.
CC   -!- PTM: Ubiquitination at Cys-5 is UBC4-independent but requires the
CC       presence of PEX4. Ubiquitination at Lys-17 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; AE016819; AAS53824.3; -; Genomic_DNA.
DR   RefSeq; NP_986000.3; NM_212136.3.
DR   AlphaFoldDB; Q752X0; -.
DR   SMR; Q752X0; -.
DR   STRING; 33169.AAS53824; -.
DR   EnsemblFungi; AAS53824; AAS53824; AGOS_AFR453W.
DR   GeneID; 4622277; -.
DR   KEGG; ago:AGOS_AFR453W; -.
DR   eggNOG; KOG1125; Eukaryota.
DR   HOGENOM; CLU_013516_3_0_1; -.
DR   InParanoid; Q752X0; -.
DR   OMA; SQFTKHV; -.
DR   Proteomes; UP000000591; Chromosome VI.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:1990429; C:peroxisomal importomer complex; IEA:EnsemblFungi.
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:0030674; F:protein-macromolecule adaptor activity; IEA:EnsemblFungi.
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   SMART; SM00028; TPR; 4.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   PROSITE; PS50005; TPR; 5.
DR   PROSITE; PS50293; TPR_REGION; 2.
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..569
FT                   /note="Peroxisomal targeting signal receptor"
FT                   /id="PRO_0000106307"
FT   REPEAT          281..315
FT                   /note="TPR 1"
FT   REPEAT          316..349
FT                   /note="TPR 2"
FT   REPEAT          417..450
FT                   /note="TPR 3"
FT   REPEAT          452..484
FT                   /note="TPR 4"
FT   REPEAT          486..518
FT                   /note="TPR 5"
FT   CROSSLNK        5
FT                   /note="Glycyl cysteine thioester (Cys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        17
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   569 AA;  62416 MW;  096B2CD66A8B736F CRC64;
     MSADCSVGAN PLAQLNKRVQ QDRTLQHGSH VNIHQGAEAQ AFKSGPQVSE SNKFQMEQFM
     AGKASSGGNM FMGAGMSSGP LALGGSSGLR MSPGPAKELG ARLGGAPMTG SWSQEFNQQV
     GSPVQSSSAV SSVSMSSASS SVARAGAYRP MNMMRPVMGL QGARAVGVER HAGPAINDAA
     WEQQFQELEK QVEKTLNISD PVEQQQVLEE LSAEAREADY AGGDYEKRFQ QIWNDIHDQT
     DDLDSRTELG GGSGDYQRVF STRPAQTAQY AFETDNQYLH NTDAYKIGCI LMENGAKLSE
     AALAFEAAVQ QDPGHVDAWL RLGLVQTQNE KELSGINALE QCLKADPHNL MALMTVAISY
     INEGYDVSAF TMLGRWLETK YPAFVEEPLD RVDRYNLSRL IIEQYLRVAN ALPEVDPDVQ
     LGLGILFYAN EDFDKTIDCF RAALAVRPDD ECMWNRLGAS LANSNRSEEA IQAYHRAIQL
     KPTFVRARYN LAVSSMNIGC YREAAEHLLT ALSMHEVEGV AMAPGSGNVP SSNILETLKR
     AFIAMDRRDL LERVVPNMDL QQFRGEFNF