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 25-MAY-2022, entry version 101.
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: 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-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; CR382138; CAG89098.2; -; Genomic_DNA.
DR RefSeq; XP_460757.2; XM_460757.1.
DR AlphaFoldDB; Q6BM14; -.
DR SMR; Q6BM14; -.
DR STRING; 4959.XP_460757.2; -.
DR EnsemblFungi; CAG89098; CAG89098; DEHA2F09108g.
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; SQFTKHV; -.
DR OrthoDB; 588648at2759; -.
DR Proteomes; UP000000599; Chromosome F.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Isopeptide bond; Membrane; Peroxisome;
KW Protein transport; Reference proteome; Repeat; Thioester bond; TPR repeat;
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 23..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 192..259
FT /evidence="ECO:0000255"
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 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
