PEX5_KLULA
ID PEX5_KLULA Reviewed; 566 AA.
AC Q6CT48;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Peroxisomal targeting signal receptor;
DE Short=PTS1 receptor;
DE Short=PTS1R;
DE AltName: Full=Peroxin-5;
GN Name=PEX5; OrderedLocusNames=KLLA0C15455g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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-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; CR382123; CAH01742.1; -; Genomic_DNA.
DR RefSeq; XP_452891.1; XM_452891.1.
DR AlphaFoldDB; Q6CT48; -.
DR SMR; Q6CT48; -.
DR STRING; 28985.XP_452891.1; -.
DR EnsemblFungi; CAH01742; CAH01742; KLLA0_C15455g.
DR GeneID; 2892605; -.
DR KEGG; kla:KLLA0_C15455g; -.
DR eggNOG; KOG1125; Eukaryota.
DR HOGENOM; CLU_013516_3_0_1; -.
DR InParanoid; Q6CT48; -.
DR OMA; SQFTKHV; -.
DR Proteomes; UP000000598; Chromosome C.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:1990429; C:peroxisomal importomer complex; IEA:EnsemblFungi.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005052; F:peroxisome matrix targeting signal-1 binding; IEA:EnsemblFungi.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:EnsemblFungi.
DR GO; GO:0016560; P:protein import into peroxisome matrix, docking; IEA:EnsemblFungi.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR024111; PEX5/PEX5L.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR10130; PTHR10130; 1.
DR Pfam; PF07719; TPR_2; 1.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 5.
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..566
FT /note="Peroxisomal targeting signal receptor"
FT /id="PRO_0000106311"
FT REPEAT 277..311
FT /note="TPR 1"
FT REPEAT 312..345
FT /note="TPR 2"
FT REPEAT 416..449
FT /note="TPR 3"
FT REPEAT 451..483
FT /note="TPR 4"
FT REPEAT 485..517
FT /note="TPR 5"
FT REGION 88..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 566 AA; 63386 MW; 53D4E9F19EABA5E3 CRC64;
MSADCSVGSN PLAQLNKHAQ QNPALRQVGY QNPASNVAQN FKTHVNEVSN ANRFQMDQFM
NRSPGFSDGQ LGMAPVPSAI LSHGPRFGLK KQDSGSSNMS AGDTAQHSRS WGNEFNSRSP
QQGLASRVNN VERISNTNSM SSYRPGMSRI GRPMMHTGIS SLHNYSHMSQ QTPQMSSDDG
VLADKQWNEQ FEALEKAVAE NLTMEDNKEE TKEEIVVEDG YQADFQEVWD KLQAETADNN
LETSDSQWEK DYARYMTGKA THIPPYRFDN DNQYMHNPNA YEIGCILMEN GAKLSEAALA
FEAAVQEDPA HVDAWLKLGL VQTQNEKEMN GISALEQCLS LDPTNQQALM TISISYINEG
YDLTAFSMLN RWLDSKYPEL TRSPTIDEAN IDRFNLSKQV ITKYLQVANA LPQVDPEVQL
GLGTLFYANE EFGKTIDCFR TALEVNPNDE LMWNRLGASL ANSNRSEEAI QAYHKALALK
PSFVRARYNL AISSMNIGCY KEAAESLLSA LSMHEVENVP ITGSVVQSNN ILETLKRSFV
AMDRRDLLEK VMPGMDLQQF RNEFNF
