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Database: UniProt
Entry: PEX5_DEBHA
LinkDB: PEX5_DEBHA
Original site: PEX5_DEBHA 
ID   PEX5_DEBHA              Reviewed;         603 AA.
AC   Q6BM14;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Peroxisomal targeting signal receptor;
DE            Short=PTS1 receptor;
DE            Short=PTS1R;
DE   AltName: Full=Peroxin-5;
GN   Name=PEX5; OrderedLocusNames=DEHA2F09108g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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: Receptor that mediates peroxisomal import of proteins
CC       containing a C-terminal PTS1-type tripeptide peroxisomal targeting
CC       signal (SKL-type). Binds to cargo proteins containing a PTS1
CC       peroxisomal targeting signal in the cytosol, and translocates them into
CC       the peroxisome matrix by passing through the PEX13-PEX14 docking
CC       complex along with cargo proteins. PEX5 receptor is then
CC       retrotranslocated into the cytosol, leading to release of bound cargo
CC       in the peroxisome matrix, and reset for a subsequent peroxisome import
CC       cycle. {ECO:0000250|UniProtKB:P35056}.
CC   -!- SUBUNIT: Interacts (via WxxxF/Y and LVxEF motifs) with PEX14; promoting
CC       translocation through the PEX13-PEX14 docking complex.
CC       {ECO:0000250|UniProtKB:P35056}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P35056}. Peroxisome matrix
CC       {ECO:0000250|UniProtKB:P35056}. Note=Cycles between the cytosol and the
CC       peroxisome matrix. Following binding to cargo proteins containing a
CC       PTS1 peroxisomal targeting signal in the cytosol, recruited to the
CC       docking complex, composed of PEX13 and PEX14, leading to translocation
CC       into the peroxisome matrix along with cargo proteins. Export and
CC       recycling to the cytosol is initiated by binding to the PEX2-PEX10-
CC       PEX12 ligase complex via its unstructured N-terminus that inserts into
CC       the ligase pore and emerges in the cytosol. Cys-10 of PEX5 is then
CC       monoubiquitinated, promoting its extraction from peroxisomal membrane
CC       by the PEX1-PEX6 AAA ATPase complex (By similarity). Extraction is
CC       accompanied by unfolding of the TPR repeats and release of bound cargo
CC       in the peroxisome matrix (By similarity). The TPR repeats refold in the
CC       cytosol and ubiquitination is removed by deubiquitinating enzyme UBP15,
CC       resetting PEX5 for a subsequent import cycle (By similarity).
CC       {ECO:0000250|UniProtKB:P35056, ECO:0000250|UniProtKB:P50542}.
CC   -!- DOMAIN: The TPR repeats mediate interaction with proteins containing a
CC       C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-
CC       type). {ECO:0000250|UniProtKB:A0A1L8FDW4}.
CC   -!- DOMAIN: The WxxxF/Y motifs mediate interaction with PEX14, promoting
CC       association with the PEX13-PEX14 docking complex.
CC       {ECO:0000250|UniProtKB:A0A1L8FDW4}.
CC   -!- DOMAIN: The amphipathic helix 1 and 2 (AH1 and AH2, respectively) are
CC       required for PEX5 retrotranslocation and recycling. AH2 mediates
CC       interaction with lumenal side of the PEX2-PEX10-PEX12 ligase complex,
CC       while AH1 is required for extraction from peroxisomal membrane by the
CC       PEX1-PEX6 AAA ATPase complex. {ECO:0000250|UniProtKB:A0A1L8FDW4}.
CC   -!- PTM: Monoubiquitinated at Cys-10 by PEX2 during PEX5 passage through
CC       the retrotranslocation channel: monoubiquitination acts as a signal for
CC       PEX5 extraction and is required for proper export from peroxisomes and
CC       recycling. When PEX5 recycling is compromised, polyubiquitinated at
CC       Lys-22 by PEX10 during its passage through the retrotranslocation
CC       channel, leading to its degradation. {ECO:0000250|UniProtKB:P35056}.
CC   -!- SIMILARITY: Belongs to the peroxisomal targeting signal receptor
CC       family. {ECO:0000305}.
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DR   EMBL; CR382138; CAG89098.2; -; Genomic_DNA.
DR   RefSeq; XP_460757.2; XM_460757.1.
DR   AlphaFoldDB; Q6BM14; -.
DR   SMR; Q6BM14; -.
DR   STRING; 284592.Q6BM14; -.
DR   GeneID; 2903774; -.
DR   KEGG; dha:DEHA2F09108g; -.
DR   VEuPathDB; FungiDB:DEHA2F09108g; -.
DR   eggNOG; KOG1125; Eukaryota.
DR   HOGENOM; CLU_013516_3_0_1; -.
DR   InParanoid; Q6BM14; -.
DR   OMA; WEEQFKQ; -.
DR   OrthoDB; 2020042at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 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:SF0; GH08708P; 1.
DR   PANTHER; PTHR10130; PEROXISOMAL TARGETING SIGNAL 1 RECEPTOR PEX5; 1.
DR   Pfam; PF00515; TPR_1; 1.
DR   SMART; SM00028; TPR; 4.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50005; TPR; 4.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isopeptide bond; Peroxisome; Protein transport;
KW   Reference proteome; Repeat; Thioester bond; TPR repeat; Translocation;
KW   Transport; Ubl conjugation.
FT   CHAIN           1..603
FT                   /note="Peroxisomal targeting signal receptor"
FT                   /id="PRO_0000106310"
FT   REPEAT          304..338
FT                   /note="TPR 1"
FT   REPEAT          339..372
FT                   /note="TPR 2"
FT   REPEAT          449..482
FT                   /note="TPR 3"
FT   REPEAT          484..516
FT                   /note="TPR 4"
FT   REPEAT          518..550
FT                   /note="TPR 5"
FT   REGION          11..33
FT                   /note="Amphipathic helix 1 (AH1)"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1L8FDW4"
FT   REGION          23..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          58..76
FT                   /note="Amphipathic helix 2 (AH2)"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1L8FDW4"
FT   REGION          232..248
FT                   /note="Amphipathic helix 4 (AH4)"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1L8FDW4"
FT   MOTIF           99..103
FT                   /note="WxxxF/Y motif 1"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1L8FDW4"
FT   MOTIF           128..132
FT                   /note="WxxxF/Y motif 2"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1L8FDW4"
FT   MOTIF           192..196
FT                   /note="WxxxF/Y motif 3"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1L8FDW4"
FT   MOTIF           271..275
FT                   /note="WxxxF/Y motif 4"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1L8FDW4"
FT   CROSSLNK        10
FT                   /note="Glycyl cysteine thioester (Cys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P35056"
FT   CROSSLNK        22
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P35056"
SQ   SEQUENCE   603 AA;  68734 MW;  F30230B4AAF68147 CRC64;
     MSFVGGGADC SANSNAIAQF NKHTQQDRSL QRQAANQQGI VQNGQGFKKD SMMNERERQN
     MDQFMNNGPS QSNFQFQPMR HELNMIQQNH KQPNVQNNWT NEFQTNSPSP VQRNTPLAKT
     GSPANAQWAT EFQQPMDQTF NQSNQQQFNN MPNMRMGGYR PMMGMSMMGG GMHQQQNQMQ
     HQEQNQDHQV DWDNQFKEIE QLTNETKDAE AEQVKGEEEP EIVIDDKYQA TFQEVWDSLN
     SEEVENDFIN QQYEEFKNTQ RDSMPADMAQ WEKDFAKYAS TRAHFGDYQF EDNQHNQFLD
     LPKESDPYEI GLQLMENGAK LSEAALAFEA AIQRNEGHIN AWLKLGEVQT QNEKEIAGIS
     ALEKCLELHP ENSEALMTLA ISYINEGYDN AAFATLERWI STKYPQVADQ ARQQNPAIDD
     EDRFSLNKRV TELFLNAAQL SPNSANMDPD VQMGLGVLFY ANEDFDKTID CFKAALSIKP
     DDAVLWNRLG ASLANSNRSE EAVDAYFKAL ELKPTFVRAR YNLGVSCINI GCYKEAAEHL
     LSGLSMHQVE GVQTDASSTL NHNQSTSLTE TLKRAFIALD RRDLLEKVKP DMDINQFRGE
     FSF
//
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