PEX5_CRIGR
ID PEX5_CRIGR Reviewed; 640 AA.
AC Q920N5; Q7TNJ1; Q920N3;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 104.
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;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND
RP CHARACTERIZATION OF VARIANT ARG-343.
RC TISSUE=Ovary;
RX PubMed=11606046; DOI=10.1006/bbrc.2001.5773;
RA Ito R., Huang Y., Yao C., Shimozawa N., Suzuki Y., Kondo N., Imanaka T.,
RA Usuda N., Ito M.;
RT "Temperature-sensitive phenotype of Chinese hamster ovary cells defective
RT in PEX5 gene.";
RL Biochem. Biophys. Res. Commun. 288:321-327(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Ovary;
RX PubMed=16428307; DOI=10.1093/jb/mvi175;
RA Ito R., Morita M., Takahashi N., Shimozawa N., Usuda N., Imanaka T.,
RA Ito M.;
RT "Identification of Pex5pM, and retarded maturation of 3-ketoacyl-CoA
RT thiolase and acyl-CoA oxidase in CHO cells expressing mutant Pex5p
RT isoforms.";
RL J. Biochem. 138:781-790(2005).
RN [3]
RP FUNCTION, AND INTERACTION WITH PEX7; PEX13 AND PEX14.
RX PubMed=11865044; DOI=10.1128/mcb.22.6.1639-1655.2002;
RA Otera H., Setoguchi K., Hamasaki M., Kumashiro T., Shimizu N., Fujiki Y.;
RT "Peroxisomal targeting signal receptor Pex5p interacts with cargoes and
RT import machinery components in a spatiotemporally differentiated manner:
RT conserved Pex5p WXXXF/Y motifs are critical for matrix protein import.";
RL Mol. Cell. Biol. 22:1639-1655(2002).
RN [4]
RP UBIQUITINATION AT CYS-11, AND MUTAGENESIS OF CYS-11.
RX PubMed=21554508; DOI=10.1111/j.1600-0854.2011.01217.x;
RA Okumoto K., Misono S., Miyata N., Matsumoto Y., Mukai S., Fujiki Y.;
RT "Cysteine ubiquitination of PTS1 receptor Pex5p regulates Pex5p
RT recycling.";
RL Traffic 12:1067-1083(2011).
RN [5]
RP INTERACTION WITH VWA8.
RX PubMed=30204880; DOI=10.1093/jb/mvy073;
RA Niwa H., Miyauchi-Nanri Y., Okumoto K., Mukai S., Noi K., Ogura T.,
RA Fujiki Y.;
RT "A newly isolated Pex7-binding, atypical PTS2 protein P7BP2 is a novel
RT dynein-type AAA+ protein.";
RL J. Biochem. 164:437-447(2018).
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:0000269|PubMed:11606046,
CC ECO:0000269|PubMed:11865044, ECO:0000269|PubMed:16428307}.
CC -!- SUBUNIT: Interacts with PEX12 (By similarity). Interacts with PEX7,
CC PEX13 and PEX14 (PubMed:11865044). Interacts (Cys-linked ubiquitinated)
CC with ZFAND6 (By similarity). Isoform 1 but not isoform 3 interacts with
CC isoform 2 of VWA8 in a PEX7-dependent manner (PubMed:30204880).
CC {ECO:0000250|UniProtKB:P50542, ECO:0000269|PubMed:11865044,
CC ECO:0000269|PubMed:30204880}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16428307}.
CC Peroxisome membrane {ECO:0000269|PubMed:16428307}; Peripheral membrane
CC protein {ECO:0000269|PubMed:16428307}. Note=Its distribution appears to
CC 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).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Pex5pL, PTS1RL;
CC IsoId=Q920N5-1; Sequence=Displayed;
CC Name=2; Synonyms=Pex5pM, PTS1RM;
CC IsoId=Q920N5-2; Sequence=VSP_024717;
CC Name=3; Synonyms=Pex5pS, PTS1RS;
CC IsoId=Q920N5-3; Sequence=VSP_024716;
CC -!- PTM: Monoubiquitination at Cys-11 is required for proper export from
CC peroxisomes and recycling. {ECO:0000269|PubMed:21554508}.
CC -!- SIMILARITY: Belongs to the peroxisomal targeting signal receptor
CC family. {ECO:0000305}.
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DR EMBL; AB065000; BAB69071.1; -; mRNA.
DR EMBL; AB063320; BAB69070.1; -; mRNA.
DR EMBL; AB098709; BAC81427.1; -; mRNA.
DR RefSeq; NP_001230930.1; NM_001244001.1. [Q920N5-1]
DR RefSeq; XP_007644336.1; XM_007646146.2. [Q920N5-2]
DR AlphaFoldDB; Q920N5; -.
DR SMR; Q920N5; -.
DR IntAct; Q920N5; 26.
DR STRING; 10029.NP_001230930.1; -.
DR Ensembl; ENSCGRT00001026058; ENSCGRP00001021814; ENSCGRG00001020537. [Q920N5-1]
DR Ensembl; ENSCGRT00001026072; ENSCGRP00001021828; ENSCGRG00001020537. [Q920N5-2]
DR GeneID; 100689015; -.
DR KEGG; cge:100689015; -.
DR CTD; 5830; -.
DR eggNOG; KOG1125; Eukaryota.
DR GeneTree; ENSGT00940000156605; -.
DR OMA; NYRMKGP; -.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0005782; C:peroxisomal matrix; ISS:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0005052; F:peroxisome matrix targeting signal-1 binding; ISS:UniProtKB.
DR GO; GO:0033328; F:peroxisome membrane targeting sequence binding; IEA:Ensembl.
DR GO; GO:0008022; F:protein C-terminus binding; ISS:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR GO; GO:0140311; F:protein sequestering activity; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0048468; P:cell development; IEA:Ensembl.
DR GO; GO:0021795; P:cerebral cortex cell migration; IEA:Ensembl.
DR GO; GO:0021895; P:cerebral cortex neuron differentiation; IEA:Ensembl.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IEA:Ensembl.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:Ensembl.
DR GO; GO:0007006; P:mitochondrial membrane organization; IEA:Ensembl.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0050905; P:neuromuscular process; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:0016560; P:protein import into peroxisome matrix, docking; IEA:Ensembl.
DR GO; GO:0016561; P:protein import into peroxisome matrix, translocation; ISS:UniProtKB.
DR GO; GO:0045046; P:protein import into peroxisome membrane; IEA:Ensembl.
DR GO; GO:0006625; P:protein targeting to peroxisome; ISS:UniProtKB.
DR GO; GO:0051262; P:protein tetramerization; ISS:UniProtKB.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IEA:Ensembl.
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 Alternative splicing; Cytoplasm; Membrane; Peroxisome; Phosphoprotein;
KW Protein transport; Repeat; Thioester bond; TPR repeat; Transport;
KW Ubl conjugation.
FT CHAIN 1..640
FT /note="Peroxisomal targeting signal 1 receptor"
FT /id="PRO_0000285543"
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 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50542"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50542"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50542"
FT MOD_RES 167
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:21554508"
FT VAR_SEQ 216..252
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11606046"
FT /id="VSP_024717"
FT VAR_SEQ 216..222
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16428307"
FT /id="VSP_024716"
FT VARIANT 343
FT /note="G -> R (loss of peroxisomal import at 37C for
FT proteins with type-1 targeting sequences)"
FT /evidence="ECO:0000269|PubMed:11606046"
FT MUTAGEN 11
FT /note="C->A: Acumulates in peroxisomes and abrogates
FT peroxisomal import of PTS1- and PTS2-containing proteins."
FT /evidence="ECO:0000269|PubMed:21554508"
SQ SEQUENCE 640 AA; 70834 MW; 473432F41BA4880F CRC64;
MAMRELVEGE CGGANPLMKL ATHFTQDKAL RQEGLRPGPW PPGASAAETV SKPLGVGSED
ELVAEFLQDQ NAPLVSRAPQ TFKMDDLLAE MQEIEQSNFR QAPQRAPGVA DLALSENWAQ
EFLAAGDAVD VAQDYNETDW SQEFIAEVTD PLSVSPARWA EEYLEQSEEK LWLGEPEGSS
TTDRWYDDYH PEEDLQHTAS DFVSKVDDPK LANSEFLKFV RQIGEGQVSL ESAAGSGRAQ
AEQWAAEFIQ QQGTSEAWVD QFTRSGNTSA LDVEFERAKS AIESDVDFWD KLQAELEEMA
KRDAEAHPWL SDYDDLTSAS YDKGYQFEEE NPLRDHPQAF EEGLRRLEEG DLPNAVLLFE
AAVQQDPKHM EAWQYLGTTQ AENEQELLAI SALRRCLELK PDNRTALMAL AVSFTNESLQ
RQACETLRDW LRYSPAYAHL VTPGEEGASG AGLGPSKRVL GSLLSDSLFL EVKELFLAAV
RLDPTSIDPD VQCGLGVLFN LSGEYDKAVD CFTAALSVRP NDYLLWNKLG ATLANGNQSE
EAVAAYRRAL ELQPGYIRSR YNLGISCINL GAHREAVEHF LEALNMQRKS RGPRGEGGAM
SENIWSTLRL ALSMLGQSDA YGAADARDLS ALLAMFGLPQ
