PEX5_ARATH
ID PEX5_ARATH Reviewed; 728 AA.
AC Q9FMA3; O82467;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Peroxisome biogenesis protein 5;
DE AltName: Full=Peroxin-5;
DE Short=AtPEX5;
DE AltName: Full=Peroxisomal targeting signal type 1 receptor;
DE AltName: Full=Pex5p;
GN Name=PEX5; OrderedLocusNames=At5g56290; ORFNames=MXK23.3;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Brickner D.G., Brickner J.H., Olsen L.J.;
RT "Sequence analysis of a cDNA encoding Pex5p, a peroxisomal targeting signal
RT type 1 receptor from Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR98-154(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP INDUCTION BY HYDROGEN PEROXIDE, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=11118212; DOI=10.1093/emboj/19.24.6770;
RA Lopez-Huertas E., Charlton W.L., Johnson B., Graham I.A., Baker A.;
RT "Stress induces peroxisome biogenesis genes.";
RL EMBO J. 19:6770-6777(2000).
RN [7]
RP MUTAGENESIS OF SER-318.
RX PubMed=11063705; DOI=10.1093/genetics/156.3.1323;
RA Zolman B.K., Yoder A., Bartel B.;
RT "Genetic analysis of indole-3-butyric acid responses in Arabidopsis
RT thaliana reveals four mutant classes.";
RL Genetics 156:1323-1337(2000).
RN [8]
RP FUNCTION, INTERACTION WITH PEX7 AND PEX14, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=11978862; DOI=10.1093/pcp/pcf057;
RA Nito K., Hayashi M., Nishimura M.;
RT "Direct interaction and determination of binding domains among peroxisomal
RT import factors in Arabidopsis thaliana.";
RL Plant Cell Physiol. 43:355-366(2002).
RN [9]
RP INTERACTION WITH LACS7.
RX PubMed=16256065; DOI=10.1016/j.abb.2005.09.003;
RA Bonsegna S., Slocombe S.P., De Bellis L., Baker A.;
RT "AtLACS7 interacts with the TPR domains of the PTS1 receptor PEX5.";
RL Arch. Biochem. Biophys. 443:74-81(2005).
RN [10]
RP FUNCTION, INTERACTION WITH PEX7; PEX14 AND PTS1-CONTAINING PROTEINS, AND
RP MUTAGENESIS OF 658-VAL--LEU-728.
RX PubMed=15637057; DOI=10.1074/jbc.m411005200;
RA Hayashi M., Yagi M., Nito K., Kamada T., Nishimura M.;
RT "Differential contribution of two peroxisomal protein receptors to the
RT maintenance of peroxisomal functions in Arabidopsis.";
RL J. Biol. Chem. 280:14829-14835(2005).
RN [11]
RP FUNCTION.
RX PubMed=15548601; DOI=10.1091/mbc.e04-05-0422;
RA Woodward A.W., Bartel B.;
RT "The Arabidopsis peroxisomal targeting signal type 2 receptor PEX7 is
RT necessary for peroxisome function and dependent on PEX5.";
RL Mol. Biol. Cell 16:573-583(2005).
RN [12]
RP DISRUPTION PHENOTYPE.
RX PubMed=16272432; DOI=10.1105/tpc.105.035691;
RA Zolman B.K., Monroe-Augustus M., Silva I.D., Bartel B.;
RT "Identification and functional characterization of Arabidopsis PEROXIN4 and
RT the interacting protein PEROXIN22.";
RL Plant Cell 17:3422-3435(2005).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=16813573; DOI=10.1111/j.1365-313x.2006.02809.x;
RA Mano S., Nakamori C., Nito K., Kondo M., Nishimura M.;
RT "The Arabidopsis pex12 and pex13 mutants are defective in both PTS1- and
RT PTS2-dependent protein transport to peroxisomes.";
RL Plant J. 47:604-618(2006).
RN [14]
RP FUNCTION.
RX PubMed=17478547; DOI=10.1093/pcp/pcm053;
RA Nito K., Kamigaki A., Kondo M., Hayashi M., Nishimura M.;
RT "Functional classification of Arabidopsis peroxisome biogenesis factors
RT proposed from analyses of knockdown mutants.";
RL Plant Cell Physiol. 48:763-774(2007).
RN [15]
RP FUNCTION.
RX PubMed=19246395; DOI=10.1073/pnas.0811329106;
RA Lingard M.J., Monroe-Augustus M., Bartel B.;
RT "Peroxisome-associated matrix protein degradation in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:4561-4566(2009).
RN [16]
RP FUNCTION, AND INTERACTION WITH PEX7.
RX PubMed=20130089; DOI=10.1091/mbc.e09-08-0672;
RA Ramon N.M., Bartel B.;
RT "Interdependence of the peroxisome-targeting receptors in Arabidopsis
RT thaliana: PEX7 facilitates PEX5 accumulation and import of PTS1 cargo into
RT peroxisomes.";
RL Mol. Biol. Cell 21:1263-1271(2010).
RN [17]
RP FUNCTION, DEVELOPMENTAL STAGE, INDUCTION BY LIGHT AND SUCROSE, AND
RP MUTAGENESIS OF 128-GLY--SER-191.
RX PubMed=20974890; DOI=10.1104/pp.110.162479;
RA Khan B.R., Zolman B.K.;
RT "pex5 mutants that differentially disrupt PTS1 and PTS2 peroxisomal matrix
RT protein import in Arabidopsis.";
RL Plant Physiol. 154:1602-1615(2010).
CC -!- FUNCTION: Import receptor for peroxisomal-targeting signal one (PTS1).
CC A receptor-cargo complex composed of PEX5, PEX7, a PTS1-containing
CC protein and a PTS2-containing protein is targeted to peroxisomes during
CC import. Necessary for the developmental elimination of obsolete
CC peroxisome matrix proteins. {ECO:0000269|PubMed:11978862,
CC ECO:0000269|PubMed:15548601, ECO:0000269|PubMed:15637057,
CC ECO:0000269|PubMed:17478547, ECO:0000269|PubMed:19246395,
CC ECO:0000269|PubMed:20130089, ECO:0000269|PubMed:20974890}.
CC -!- SUBUNIT: Interacts (via N-terminus) with PEX7 (via C-terminus), (via
CC WXXXF/Y repeats) with PEX14 and (via TPR repeats) with PTS1-containing
CC proteins. Interacts with LACS7. {ECO:0000269|PubMed:11978862,
CC ECO:0000269|PubMed:15637057, ECO:0000269|PubMed:16256065,
CC ECO:0000269|PubMed:20130089}.
CC -!- INTERACTION:
CC Q9FMA3; Q8LKS5: LACS7; NbExp=4; IntAct=EBI-993861, EBI-993851;
CC Q9FMA3; Q9FXT6: PEX14; NbExp=3; IntAct=EBI-993861, EBI-9536455;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16813573}.
CC Peroxisome membrane {ECO:0000269|PubMed:16813573}; Peripheral membrane
CC protein {ECO:0000269|PubMed:16813573}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers, siliques, leaves and roots.
CC {ECO:0000269|PubMed:11978862}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the early stage of germination and
CC during the conversion of glyoxysomes to peroxisomes. Accumulates at
CC high levels in seedlings and at lower levels as plants mature.
CC {ECO:0000269|PubMed:11118212, ECO:0000269|PubMed:11978862,
CC ECO:0000269|PubMed:20974890}.
CC -!- INDUCTION: Up-regulated by hydrogen peroxide, the absence of sucrose
CC and by dark versus light conditions. {ECO:0000269|PubMed:11118212,
CC ECO:0000269|PubMed:20974890}.
CC -!- PTM: May be monoubiquitinated by PEX4 and PEX12 for recycling from the
CC peroxisome. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Peroxisome-defective phenotype including an
CC absolute requirement for sucrose during early development, high
CC seedling lethality, and delayed development.
CC {ECO:0000269|PubMed:16272432}.
CC -!- MISCELLANEOUS: PEX5 stability in light-grown seedlings depends on PEX7.
CC -!- SIMILARITY: Belongs to the peroxisomal targeting signal receptor
CC family. {ECO:0000305}.
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DR EMBL; AF074843; AAC62012.1; -; mRNA.
DR EMBL; AB009049; BAB11256.1; -; Genomic_DNA.
DR EMBL; AB026656; BAB11256.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED96745.1; -; Genomic_DNA.
DR EMBL; AY056299; AAL07148.1; -; mRNA.
DR EMBL; AY096679; AAM20313.1; -; mRNA.
DR PIR; T51817; T51817.
DR RefSeq; NP_200440.1; NM_125012.5.
DR AlphaFoldDB; Q9FMA3; -.
DR SMR; Q9FMA3; -.
DR BioGRID; 20972; 16.
DR ELM; Q9FMA3; -.
DR IntAct; Q9FMA3; 16.
DR MINT; Q9FMA3; -.
DR STRING; 3702.AT5G56290.1; -.
DR TCDB; 3.A.20.1.2; the peroxisomal protein importer (ppi) family.
DR iPTMnet; Q9FMA3; -.
DR PaxDb; Q9FMA3; -.
DR PRIDE; Q9FMA3; -.
DR ProteomicsDB; 251018; -.
DR EnsemblPlants; AT5G56290.1; AT5G56290.1; AT5G56290.
DR GeneID; 835728; -.
DR Gramene; AT5G56290.1; AT5G56290.1; AT5G56290.
DR KEGG; ath:AT5G56290; -.
DR Araport; AT5G56290; -.
DR TAIR; locus:2177606; AT5G56290.
DR eggNOG; KOG1125; Eukaryota.
DR HOGENOM; CLU_021069_0_0_1; -.
DR InParanoid; Q9FMA3; -.
DR OMA; NYRMKGP; -.
DR OrthoDB; 588648at2759; -.
DR PhylomeDB; Q9FMA3; -.
DR PRO; PR:Q9FMA3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMA3; baseline and differential.
DR Genevisible; Q9FMA3; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
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 GO; GO:0006625; P:protein targeting to peroxisome; IGI:TAIR.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
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 Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 4.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Membrane; Peroxisome; Peroxisome biogenesis; Protein transport;
KW Receptor; Reference proteome; Repeat; TPR repeat; Translocation; Transport;
KW Ubl conjugation.
FT CHAIN 1..728
FT /note="Peroxisome biogenesis protein 5"
FT /id="PRO_0000403357"
FT REPEAT 240..244
FT /note="1"
FT REPEAT 257..261
FT /note="2"
FT REPEAT 270..274
FT /note="3"
FT REPEAT 348..352
FT /note="4"
FT REPEAT 362..366
FT /note="5"
FT REPEAT 378..382
FT /note="6"
FT REPEAT 396..400
FT /note="7"
FT REPEAT 408..412
FT /note="8"
FT REPEAT 425..429
FT /note="9"
FT REPEAT 491..524
FT /note="TPR 1"
FT REPEAT 590..623
FT /note="TPR 2"
FT REPEAT 625..657
FT /note="TPR 3"
FT REPEAT 658..691
FT /note="TPR 4"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..429
FT /note="9 X 5 AA repeats of WXXXF/Y"
FT COMPBIAS 14..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 128..191
FT /note="Missing: In pex5-10; loss of import of both
FT PTS1- and PTS2-containing proteins."
FT /evidence="ECO:0000269|PubMed:20974890"
FT MUTAGEN 318
FT /note="S->L: In pex5-1; reduced sensitivity to exogenous
FT indole-3-butyric acid (IBA), loss of PTS2-containing
FT proteins import, but no effect on PTS1-containing proteins
FT import."
FT /evidence="ECO:0000269|PubMed:11063705"
FT MUTAGEN 658..728
FT /note="Missing: Loss of interaction with PTS1-containing
FT proteins, reduced interaction with PEX14 and no effect on
FT interaction with PEX7."
FT /evidence="ECO:0000269|PubMed:15637057"
FT CONFLICT 571..574
FT /note="YHAD -> FHAE (in Ref. 1; AAC62012)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 728 AA; 80912 MW; 12EF434E8C06DDFB CRC64;
MAMRDLVNGG AACAVPGSSS SSNPLGALTN ALLGSSSKTQ ERLKEIPNAN RSGPRPQFYS
EDQQIRSLPG SELDQPLLQP GAQGSEFFRG FRSVDQNGLG AAWDEVQQGG PMPPMGPMFE
PVQPTFEGPP QRVLSNFLHS FVESSRGGIP FRPAPVPVLG LSQSDKQCIR DRSSIMARHF
FADRGEEFIN SQVNALLSSL DIDDGIQARG HVPGRFRELD DYWNESQAVV KPNLHPADNW
AAEFNQHGMD HGGPDSWVQS FEQQHGVNGW ATEFEQGQSQ LMSSQMRSMD MQNIAAMEQT
RKLAHTLSQD GNPKFQNSRF LQFVSKMSRG ELIIDENQVK QASAPGEWAT EYEQQYLGPP
SWADQFANEK LSHGPEQWAD EFASGRGQQE TAEDQWVNEF SKLNVDDWID EFAEGPVGDS
SADAWANAYD EFLNEKNAGK QTSGVYVFSD MNPYVGHPEP MKEGQELFRK GLLSEAALAL
EAEVMKNPEN AEGWRLLGVT HAENDDDQQA IAAMMRAQEA DPTNLEVLLA LGVSHTNELE
QATALKYLYG WLRNHPKYGA IAPPELADSL YHADIARLFN EASQLNPEDA DVHIVLGVLY
NLSREFDRAI TSFQTALQLK PNDYSLWNKL GATQANSVQS ADAISAYQQA LDLKPNYVRA
WANMGISYAN QGMYKESIPY YVRALAMNPK ADNAWQYLRL SLSCASRQDM IEACESRNLD
LLQKEFPL
