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PEX5_RAT
ID   PEX5_RAT                Reviewed;         640 AA.
AC   Q2M2R8;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Peroxisomal targeting signal 1 receptor;
DE            Short=PTS1 receptor;
DE            Short=PTS1R;
DE   AltName: Full=PTS1-BP;
DE   AltName: Full=Peroxin-5;
DE   AltName: Full=Peroxisomal C-terminal targeting signal import receptor;
DE   AltName: Full=Peroxisome receptor 1;
GN   Name=Pex5; Synonyms=Pex5_predicted;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 408-604.
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   UBIQUITINATION AT CYS-11.
RX   PubMed=18359941; DOI=10.1074/jbc.m800402200;
RA   Grou C.P., Carvalho A.F., Pinto M.P., Wiese S., Piechura H., Meyer H.E.,
RA   Warscheid B., Sa-Miranda C., Azevedo J.E.;
RT   "Members of the E2D (UbcH5) family mediate the ubiquitination of the
RT   conserved cysteine of Pex5p, the peroxisomal import receptor.";
RL   J. Biol. Chem. 283:14190-14197(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|UniProtKB:Q920N5}.
CC   -!- SUBUNIT: Interacts with PEX7, PEX12, PEX13 and PEX14. Interacts (Cys-
CC       linked ubiquitinated) with ZFAND6. Interacts with VWA8 in a PEX7-
CC       dependent manner. {ECO:0000250|UniProtKB:P50542,
CC       ECO:0000250|UniProtKB:Q920N5}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q920N5}.
CC       Peroxisome membrane {ECO:0000250|UniProtKB:Q920N5}; Peripheral membrane
CC       protein {ECO:0000250|UniProtKB:Q920N5}. Note=Its distribution appears
CC       to be dynamic. It is probably a cycling receptor found mainly in the
CC       cytoplasm and as well associated to the peroxisomal membrane through a
CC       docking factor (PEX13) (By similarity). {ECO:0000250}.
CC   -!- PTM: Monoubiquitination at Cys-11 is required for proper export from
CC       peroxisomes and recycling. {ECO:0000250|UniProtKB:Q920N5}.
CC   -!- SIMILARITY: Belongs to the peroxisomal targeting signal receptor
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDM01958.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH473964; EDM01958.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC111709; AAI11710.1; -; mRNA.
DR   RefSeq; NP_001164055.1; NM_001170584.1.
DR   RefSeq; XP_006237446.1; XM_006237384.2.
DR   RefSeq; XP_006237447.1; XM_006237385.3.
DR   RefSeq; XP_008761499.1; XM_008763277.2.
DR   AlphaFoldDB; Q2M2R8; -.
DR   SMR; Q2M2R8; -.
DR   BioGRID; 260235; 4.
DR   STRING; 10116.ENSRNOP00000014028; -.
DR   iPTMnet; Q2M2R8; -.
DR   PhosphoSitePlus; Q2M2R8; -.
DR   PaxDb; Q2M2R8; -.
DR   PRIDE; Q2M2R8; -.
DR   GeneID; 312703; -.
DR   KEGG; rno:312703; -.
DR   UCSC; RGD:1307612; rat.
DR   CTD; 5830; -.
DR   RGD; 1307612; Pex5.
DR   eggNOG; KOG1125; Eukaryota.
DR   HOGENOM; CLU_013516_4_0_1; -.
DR   InParanoid; Q2M2R8; -.
DR   OMA; QAENEMD; -.
DR   OrthoDB; 588648at2759; -.
DR   PhylomeDB; Q2M2R8; -.
DR   TreeFam; TF315044; -.
DR   Reactome; R-RNO-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR   Reactome; R-RNO-9033241; Peroxisomal protein import.
DR   Reactome; R-RNO-9664873; Pexophagy.
DR   PRO; PR:Q2M2R8; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Proteomes; UP000234681; Chromosome 4.
DR   Bgee; ENSRNOG00000010407; Expressed in liver and 19 other tissues.
DR   Genevisible; Q2M2R8; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; IDA:RGD.
DR   GO; GO:0016020; C:membrane; IDA:RGD.
DR   GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR   GO; GO:0005778; C:peroxisomal membrane; IDA:HGNC-UCL.
DR   GO; GO:0005777; C:peroxisome; IDA:RGD.
DR   GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR   GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR   GO; GO:0005052; F:peroxisome matrix targeting signal-1 binding; ISO:RGD.
DR   GO; GO:0033328; F:peroxisome membrane targeting sequence binding; ISO:RGD.
DR   GO; GO:0000268; F:peroxisome targeting sequence binding; ISO:RGD.
DR   GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR   GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
DR   GO; GO:0140311; F:protein sequestering activity; ISO:RGD.
DR   GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR   GO; GO:0048468; P:cell development; ISO:RGD.
DR   GO; GO:0044255; P:cellular lipid metabolic process; ISO:RGD.
DR   GO; GO:0021795; P:cerebral cortex cell migration; ISO:RGD.
DR   GO; GO:0021895; P:cerebral cortex neuron differentiation; ISO:RGD.
DR   GO; GO:0007029; P:endoplasmic reticulum organization; ISO:RGD.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; ISO:RGD.
DR   GO; GO:0007006; P:mitochondrial membrane organization; ISO:RGD.
DR   GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR   GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:RGD.
DR   GO; GO:0050905; P:neuromuscular process; ISO:RGD.
DR   GO; GO:0001764; P:neuron migration; ISO:RGD.
DR   GO; GO:0007031; P:peroxisome organization; ISO:RGD.
DR   GO; GO:0040018; P:positive regulation of multicellular organism growth; ISO:RGD.
DR   GO; GO:0016558; P:protein import into peroxisome matrix; ISO:RGD.
DR   GO; GO:0016560; P:protein import into peroxisome matrix, docking; ISO:RGD.
DR   GO; GO:0045046; P:protein import into peroxisome membrane; ISO:RGD.
DR   GO; GO:0006625; P:protein targeting to peroxisome; ISO:RGD.
DR   GO; GO:0000038; P:very long-chain fatty acid metabolic process; ISO:RGD.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR024111; PEX5/PEX5L.
DR   InterPro; IPR024113; PEX5_animals.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR10130; PTHR10130; 1.
DR   PANTHER; PTHR10130:SF2; PTHR10130:SF2; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00028; TPR; 4.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   PROSITE; PS50005; TPR; 5.
DR   PROSITE; PS50293; TPR_REGION; 1.
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..640
FT                   /note="Peroxisomal targeting signal 1 receptor"
FT                   /id="PRO_0000396503"
FT   REPEAT          336..369
FT                   /note="TPR 1"
FT   REPEAT          371..403
FT                   /note="TPR 2"
FT   REPEAT          404..437
FT                   /note="TPR 3"
FT   REPEAT          454..486
FT                   /note="TPR 4"
FT   REPEAT          489..522
FT                   /note="TPR 5"
FT   REPEAT          524..556
FT                   /note="TPR 6"
FT   REPEAT          558..590
FT                   /note="TPR 7"
FT   MOD_RES         114
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P50542"
FT   MOD_RES         152
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P50542"
FT   MOD_RES         154
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P50542"
FT   MOD_RES         166
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P50542"
FT   MOD_RES         280
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P50542"
FT   CROSSLNK        11
FT                   /note="Glycyl cysteine thioester (Cys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:18359941"
SQ   SEQUENCE   640 AA;  71022 MW;  57B65CDA460A5BD6 CRC64;
     MAMRELVESE CGGANPLMKL ATHFTQDKAL RQEGLRPPWP PGASAAETVS KPLGVGTEDE
     LVAEFLQDQN ATLVSRAPQT FKMDDLLAEM QEIEQSNFRQ APQRAPGVAD LALSENWAQE
     FLAAGDAVDV AQDYNETDWS QEFIAEVTDP LSVSPARWAE EYLEQSEEKL WLGDPEGTST
     TDRWYDEYHP EEDLQHTASD FVSKVDDPKL ANSEFLKFVR QIGEGQVSLE SAAGSGRAQA
     EQWAAEFIQQ QGTSEAWVDQ FTRPGNKLAA LQVEFERAKS AIESDVDFWD KLQAELEEMA
     KRDAEAHPWL SDYDDLTSAS YDKGYQFEEE NPLRDHPQPF EEGLRRLEEG DLPNAVLLFE
     AAVQQDPKHM EAWQYLGTTQ AENEQELLAI SALRRCLELK PDNRTALMAL AVSFTNESLQ
     RQACETLRDW LRYSPAYAHL VAPGEEGASG AGLGPSKRVL GSLLSDSLFL EVKELFLAAV
     RLDPTSIDPD VQCGLGVLFN LSGEYDKAVD CFTAALSVRP NDYLLWNKLG ATLANGNQSE
     EAVAAYRRAL ELQPGYIRSR YNLGISCINL GAHREAVEHF LEALNMQRKS RGPRGEGGAM
     SENIWSTLRL ALSMLGQSDA YGAADARDLP ALLTMFGLPQ
 
 
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