PEX5_SCHPO
ID PEX5_SCHPO Reviewed; 598 AA.
AC O94325;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Peroxisomal targeting signal receptor;
DE Short=PTS1 receptor;
DE Short=PTS1R;
DE AltName: Full=Peroxin-5;
GN Name=pex5; ORFNames=SPBC725.07;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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-7 is UBC4-independent but requires the
CC presence of PEX4.
CC -!- SIMILARITY: Belongs to the peroxisomal targeting signal receptor
CC family. {ECO:0000305}.
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DR EMBL; CU329671; CAA22179.1; -; Genomic_DNA.
DR PIR; T40659; T40659.
DR RefSeq; NP_595487.1; NM_001021398.2.
DR AlphaFoldDB; O94325; -.
DR SMR; O94325; -.
DR BioGRID; 277627; 24.
DR IntAct; O94325; 2.
DR STRING; 4896.SPBC725.07.1; -.
DR iPTMnet; O94325; -.
DR MaxQB; O94325; -.
DR PaxDb; O94325; -.
DR PRIDE; O94325; -.
DR EnsemblFungi; SPBC725.07.1; SPBC725.07.1:pep; SPBC725.07.
DR GeneID; 2541112; -.
DR KEGG; spo:SPBC725.07; -.
DR PomBase; SPBC725.07; pex5.
DR VEuPathDB; FungiDB:SPBC725.07; -.
DR eggNOG; KOG1125; Eukaryota.
DR HOGENOM; CLU_455728_0_0_1; -.
DR InParanoid; O94325; -.
DR OMA; SIACINM; -.
DR PhylomeDB; O94325; -.
DR Reactome; R-SPO-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-SPO-9033241; Peroxisomal protein import.
DR Reactome; R-SPO-9664873; Pexophagy.
DR PRO; PR:O94325; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IDA:PomBase.
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; IPR019734; TPR_repeat.
DR PANTHER; PTHR10130; PTHR10130; 1.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 4.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Membrane; Peroxisome; Phosphoprotein; 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_0000106314"
FT REPEAT 328..361
FT /note="TPR 1"
FT REPEAT 438..471
FT /note="TPR 2"
FT REPEAT 472..505
FT /note="TPR 3"
FT REPEAT 507..539
FT /note="TPR 4"
FT REGION 62..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CROSSLNK 7
FT /note="Glycyl cysteine thioester (Cys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 598 AA; 67104 MW; 4F80CAD9976B659F CRC64;
MSVEAGCSTL SNPLKKLTST AVVNNSTPSA QYRKHLTKSQ SRTYAPLQTL SEDQFTSFKN
LQGNNSPLGN VVKNPVSLKT GNHTGTTTRG GSKENWVHSF SSLQQQNSKS AWTSEFSEVF
LNSSENDRFR NLNQPLKQSF FGSAGLNLSS NTEIPLQSSL AIDETELAKK FEEASQISNK
LEKEKDATGS KSIEELWEEH QKQLKNAGLE PASLEEYQKQ WEDFLKSNNI SDDPYTSSVN
SFANDNLAHN KNIDPQIFQH SDTDNVVENS LQTEDVYSQN QDESSEVVKE LNGIDPFVEA
MNLIKNGGSI SKAAVLLEQS VKENPQHFEA WKWLGRIHTL LGNESRVVEA LLEAVKLDST
NLDLMMDLAV SYVNQSLNVQ ALVCLEDWIV NSFPQYRNRF AKINERFEEK DSANDLLKMQ
MYFLDVAYEL SLAKKRSSKV QAGLGIIMYM LKEYERSADC FRQALQDEPS NEILWNKLGA
ALTNAEKNTE AVSSYNRAVS LQPQYVRVRS NMAVSNINLG YFEDAAKHLL AAIDIIQNSS
TSMESCESNE ELWEMLRKVF LIGFQSTDLA SQSYPGANTS YIRAQLSDLQ GWPGVELE
