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Protein

Peroxisome biogenesis protein 5

Gene

PEX5

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Import receptor for peroxisomal-targeting signal one (PTS1). A receptor-cargo complex composed of PEX5, PEX7, a PTS1-containing protein and a PTS2-containing protein is targeted to peroxisomes during import. Necessary for the developmental elimination of obsolete peroxisome matrix proteins.7 Publications

GO - Molecular functioni

GO - Biological processi

  • protein import into peroxisome matrix, docking Source: GO_Central
  • protein targeting to peroxisome Source: TAIR
  • response to auxin Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Peroxisome biogenesis, Protein transport, Translocation, Transport

Protein family/group databases

TCDBi3.A.20.1.2. the peroxisomal protein importer (ppi) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisome biogenesis protein 5
Alternative name(s):
Peroxin-5
Short name:
AtPEX5
Peroxisomal targeting signal type 1 receptor
Pex5p
Gene namesi
Name:PEX5
Ordered Locus Names:At5g56290
ORF Names:MXK23.3
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G56290.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Peroxisome

Pathology & Biotechi

Disruption phenotypei

Peroxisome-defective phenotype including an absolute requirement for sucrose during early development, high seedling lethality, and delayed development.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi128 – 19164Missing in pex5-10; loss of import of both PTS1- and PTS2-containing proteins. 1 PublicationAdd
BLAST
Mutagenesisi318 – 3181S → L in pex5-1; reduced sensitivity to exogenous indole-3-butyric acid (IBA), loss of PTS2-containing proteins import, but no effect on PTS1-containing proteins import. 1 Publication
Mutagenesisi658 – 72871Missing : Loss of interaction with PTS1-containing proteins, reduced interaction with PEX14 and no effect on interaction with PEX7. 1 PublicationAdd
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 728728Peroxisome biogenesis protein 5PRO_0000403357Add
BLAST

Post-translational modificationi

May be monoubiquitinated by PEX4 and PEX12 for recycling from the peroxisome.By similarity

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiQ9FMA3.
PRIDEiQ9FMA3.

PTM databases

iPTMnetiQ9FMA3.

Expressioni

Tissue specificityi

Expressed in flowers, siliques, leaves and roots.1 Publication

Developmental stagei

Expressed at the early stage of germination and during the conversion of glyoxysomes to peroxisomes. Accumulates at high levels in seedlings and at lower levels as plants mature.3 Publications

Inductioni

Up-regulated by hydrogen peroxide, the absence of sucrose and by dark versus light conditions.2 Publications

Gene expression databases

GenevisibleiQ9FMA3. AT.

Interactioni

Subunit structurei

Interacts (via N-terminus) with PEX7 (via C-terminus), (via WXXXF/Y repeats) with PEX14 and (via TPR repeats) with PTS1-containing proteins. Interacts with LACS7.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LACS7Q8LKS54EBI-993861,EBI-993851
PEX14Q9FXT63EBI-993861,EBI-9536455

Protein-protein interaction databases

BioGridi20972. 15 interactions.
IntActiQ9FMA3. 16 interactions.
STRINGi3702.AT5G56290.1.

Structurei

3D structure databases

ProteinModelPortaliQ9FMA3.
SMRiQ9FMA3. Positions 446-728.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati240 – 24451
Repeati257 – 26152
Repeati270 – 27453
Repeati348 – 35254
Repeati362 – 36655
Repeati378 – 38256
Repeati396 – 40057
Repeati408 – 41258
Repeati425 – 42959
Repeati491 – 52434TPR 1Add
BLAST
Repeati590 – 62334TPR 2Add
BLAST
Repeati625 – 65733TPR 3Add
BLAST
Repeati658 – 69134TPR 4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni240 – 4291909 X 5 AA repeats of WXXXF/YAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi18 – 225Poly-Ser

Sequence similaritiesi

Contains 4 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG1125. Eukaryota.
ENOG410XQ6Q. LUCA.
HOGENOMiHOG000264895.
InParanoidiQ9FMA3.
KOiK13342.
OMAiQPTDSPY.
PhylomeDBiQ9FMA3.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR024111. PTS1R_family.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR10130. PTHR10130. 2 hits.
PfamiPF00515. TPR_1. 1 hit.
PF13181. TPR_8. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 4 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
PROSITEiPS50005. TPR. 4 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9FMA3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMRDLVNGG AACAVPGSSS SSNPLGALTN ALLGSSSKTQ ERLKEIPNAN
60 70 80 90 100
RSGPRPQFYS EDQQIRSLPG SELDQPLLQP GAQGSEFFRG FRSVDQNGLG
110 120 130 140 150
AAWDEVQQGG PMPPMGPMFE PVQPTFEGPP QRVLSNFLHS FVESSRGGIP
160 170 180 190 200
FRPAPVPVLG LSQSDKQCIR DRSSIMARHF FADRGEEFIN SQVNALLSSL
210 220 230 240 250
DIDDGIQARG HVPGRFRELD DYWNESQAVV KPNLHPADNW AAEFNQHGMD
260 270 280 290 300
HGGPDSWVQS FEQQHGVNGW ATEFEQGQSQ LMSSQMRSMD MQNIAAMEQT
310 320 330 340 350
RKLAHTLSQD GNPKFQNSRF LQFVSKMSRG ELIIDENQVK QASAPGEWAT
360 370 380 390 400
EYEQQYLGPP SWADQFANEK LSHGPEQWAD EFASGRGQQE TAEDQWVNEF
410 420 430 440 450
SKLNVDDWID EFAEGPVGDS SADAWANAYD EFLNEKNAGK QTSGVYVFSD
460 470 480 490 500
MNPYVGHPEP MKEGQELFRK GLLSEAALAL EAEVMKNPEN AEGWRLLGVT
510 520 530 540 550
HAENDDDQQA IAAMMRAQEA DPTNLEVLLA LGVSHTNELE QATALKYLYG
560 570 580 590 600
WLRNHPKYGA IAPPELADSL YHADIARLFN EASQLNPEDA DVHIVLGVLY
610 620 630 640 650
NLSREFDRAI TSFQTALQLK PNDYSLWNKL GATQANSVQS ADAISAYQQA
660 670 680 690 700
LDLKPNYVRA WANMGISYAN QGMYKESIPY YVRALAMNPK ADNAWQYLRL
710 720
SLSCASRQDM IEACESRNLD LLQKEFPL
Length:728
Mass (Da):80,912
Last modified:March 1, 2001 - v1
Checksum:i12EF434E8C06DDFB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti571 – 5744YHAD → FHAE in AAC62012 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF074843 mRNA. Translation: AAC62012.1.
AB009049, AB026656 Genomic DNA. Translation: BAB11256.1.
CP002688 Genomic DNA. Translation: AED96745.1.
AY056299 mRNA. Translation: AAL07148.1.
AY096679 mRNA. Translation: AAM20313.1.
PIRiT51817.
RefSeqiNP_200440.1. NM_125012.4.
UniGeneiAt.10824.

Genome annotation databases

EnsemblPlantsiAT5G56290.1; AT5G56290.1; AT5G56290.
GeneIDi835728.
GrameneiAT5G56290.1; AT5G56290.1; AT5G56290.
KEGGiath:AT5G56290.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF074843 mRNA. Translation: AAC62012.1.
AB009049, AB026656 Genomic DNA. Translation: BAB11256.1.
CP002688 Genomic DNA. Translation: AED96745.1.
AY056299 mRNA. Translation: AAL07148.1.
AY096679 mRNA. Translation: AAM20313.1.
PIRiT51817.
RefSeqiNP_200440.1. NM_125012.4.
UniGeneiAt.10824.

3D structure databases

ProteinModelPortaliQ9FMA3.
SMRiQ9FMA3. Positions 446-728.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi20972. 15 interactions.
IntActiQ9FMA3. 16 interactions.
STRINGi3702.AT5G56290.1.

Protein family/group databases

TCDBi3.A.20.1.2. the peroxisomal protein importer (ppi) family.

PTM databases

iPTMnetiQ9FMA3.

Proteomic databases

PaxDbiQ9FMA3.
PRIDEiQ9FMA3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G56290.1; AT5G56290.1; AT5G56290.
GeneIDi835728.
GrameneiAT5G56290.1; AT5G56290.1; AT5G56290.
KEGGiath:AT5G56290.

Organism-specific databases

TAIRiAT5G56290.

Phylogenomic databases

eggNOGiKOG1125. Eukaryota.
ENOG410XQ6Q. LUCA.
HOGENOMiHOG000264895.
InParanoidiQ9FMA3.
KOiK13342.
OMAiQPTDSPY.
PhylomeDBiQ9FMA3.

Miscellaneous databases

PROiQ9FMA3.

Gene expression databases

GenevisibleiQ9FMA3. AT.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR024111. PTS1R_family.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR10130. PTHR10130. 2 hits.
PfamiPF00515. TPR_1. 1 hit.
PF13181. TPR_8. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 4 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
PROSITEiPS50005. TPR. 4 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of a cDNA encoding Pex5p, a peroxisomal targeting signal type 1 receptor from Arabidopsis (Accession No. AF074843) (PGR98-154)."
    Brickner D.G., Brickner J.H., Olsen L.J.
    Plant Physiol. 118:330-330(1998)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence features of the regions of 1,456,315 bp covered by nineteen physically assigned P1 and TAC clones."
    Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N., Tabata S.
    DNA Res. 5:41-54(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. "Structural analysis of Arabidopsis thaliana chromosome 5. XI."
    Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., Tabata S.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. Cited for: INDUCTION BY HYDROGEN PEROXIDE, DEVELOPMENTAL STAGE.
    Strain: cv. Columbia.
  7. "Genetic analysis of indole-3-butyric acid responses in Arabidopsis thaliana reveals four mutant classes."
    Zolman B.K., Yoder A., Bartel B.
    Genetics 156:1323-1337(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-318.
  8. "Direct interaction and determination of binding domains among peroxisomal import factors in Arabidopsis thaliana."
    Nito K., Hayashi M., Nishimura M.
    Plant Cell Physiol. 43:355-366(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PEX7 AND PEX14, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  9. "AtLACS7 interacts with the TPR domains of the PTS1 receptor PEX5."
    Bonsegna S., Slocombe S.P., De Bellis L., Baker A.
    Arch. Biochem. Biophys. 443:74-81(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LACS7.
  10. "Differential contribution of two peroxisomal protein receptors to the maintenance of peroxisomal functions in Arabidopsis."
    Hayashi M., Yagi M., Nito K., Kamada T., Nishimura M.
    J. Biol. Chem. 280:14829-14835(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PEX7; PEX14 AND PTS1-CONTAINING PROTEINS, MUTAGENESIS OF 658-VAL--LEU-728.
  11. "The Arabidopsis peroxisomal targeting signal type 2 receptor PEX7 is necessary for peroxisome function and dependent on PEX5."
    Woodward A.W., Bartel B.
    Mol. Biol. Cell 16:573-583(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Identification and functional characterization of Arabidopsis PEROXIN4 and the interacting protein PEROXIN22."
    Zolman B.K., Monroe-Augustus M., Silva I.D., Bartel B.
    Plant Cell 17:3422-3435(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  13. "The Arabidopsis pex12 and pex13 mutants are defective in both PTS1- and PTS2-dependent protein transport to peroxisomes."
    Mano S., Nakamori C., Nito K., Kondo M., Nishimura M.
    Plant J. 47:604-618(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  14. "Functional classification of Arabidopsis peroxisome biogenesis factors proposed from analyses of knockdown mutants."
    Nito K., Kamigaki A., Kondo M., Hayashi M., Nishimura M.
    Plant Cell Physiol. 48:763-774(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "Peroxisome-associated matrix protein degradation in Arabidopsis."
    Lingard M.J., Monroe-Augustus M., Bartel B.
    Proc. Natl. Acad. Sci. U.S.A. 106:4561-4566(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "Interdependence of the peroxisome-targeting receptors in Arabidopsis thaliana: PEX7 facilitates PEX5 accumulation and import of PTS1 cargo into peroxisomes."
    Ramon N.M., Bartel B.
    Mol. Biol. Cell 21:1263-1271(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PEX7.
  17. "pex5 mutants that differentially disrupt PTS1 and PTS2 peroxisomal matrix protein import in Arabidopsis."
    Khan B.R., Zolman B.K.
    Plant Physiol. 154:1602-1615(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE, INDUCTION BY LIGHT AND SUCROSE, MUTAGENESIS OF 128-GLY--SER-191.

Entry informationi

Entry nameiPEX5_ARATH
AccessioniPrimary (citable) accession number: Q9FMA3
Secondary accession number(s): O82467
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: March 1, 2001
Last modified: May 11, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

PEX5 stability in light-grown seedlings depends on PEX7.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.