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Q8LGF7 (PEX4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein PEROXIN-4

Short name=AtPEX4
Alternative name(s):
Probable ubiquitin-conjugating enzyme E2 21
EC=6.3.2.19
Ubiquitin carrier protein 21
Gene names
Name:PEX4
Synonyms:UBC21
Ordered Locus Names:At5g25760
ORF Names:F18A17.10
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length157 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for peroxisome biogenesis. Necessary for the developmental elimination of obsolete peroxisome matrix proteins. May be involved in the ubiquitination of PEX5, targeting it for recycling. Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins By similarity. Ref.7 Ref.8

Catalytic activity

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with PEX22. Ref.6

Subcellular location

Peroxisome membrane; Peripheral membrane protein By similarity.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 157157Protein PEROXIN-4
PRO_0000345187

Sites

Active site901Glycyl thioester intermediate By similarity

Experimental info

Mutagenesis1231P → L in pex4-1; reduced peroxisomal function and loss of response to indole-3-butyric acid. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q8LGF7 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 36FB1E11684F48B4

FASTA15717,708
        10         20         30         40         50         60 
MQASRARLFK EYKEVQREKV ADPDIQLICD DTNIFKWTAL IKGPSETPYE GGVFQLAFSV 

        70         80         90        100        110        120 
PEPYPLQPPQ VRFLTKIFHP NVHFKTGEIC LDILKNAWSP AWTLQSVCRA IIALMAHPEP 

       130        140        150 
DSPLNCDSGN LLRSGDVRGF NSMAQMYTRL AAMPKKG 

« Hide

References

« Hide 'large scale' references
[1]"Genome analysis and functional characterization of the E2 and RING-type E3 ligase ubiquitination enzymes of Arabidopsis."
Kraft E., Stone S.L., Ma L., Su N., Gao Y., Lau O.-S., Deng X.-W., Callis J.
Plant Physiol. 139:1597-1611(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, NOMENCLATURE.
[2]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Arabidopsis ORF clones."
Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[6]"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: IDENTIFICATION, MUTAGENESIS OF PRO-123, INTERACTION WITH PEX22.
[7]"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.
[8]"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.
+Additional computationally mapped references.

Web resources

PlantsUBQ

A functional genomics database for the ubiquitin/26S proteasome proteolytic pathway in plants

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ027035 mRNA. Translation: AAY44861.1.
AC005405 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED93482.1.
CP002688 Genomic DNA. Translation: AED93483.1.
AY084297 mRNA. Translation: AAM60888.1.
BT025616 mRNA. Translation: ABF59034.1.
RefSeqNP_001031939.1. NM_001036862.1.
NP_568476.1. NM_122477.2.
UniGeneAt.20548.
At.30893.

3D structure databases

ProteinModelPortalQ8LGF7.
SMRQ8LGF7. Positions 7-127.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid17920. 1 interaction.
IntActQ8LGF7. 1 interaction.
STRING3702.AT5G25760.1-P.

Proteomic databases

PaxDbQ8LGF7.
PRIDEQ8LGF7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G25760.1; AT5G25760.1; AT5G25760.
AT5G25760.2; AT5G25760.2; AT5G25760.
GeneID832645.
KEGGath:AT5G25760.

Organism-specific databases

TAIRAT5G25760.

Phylogenomic databases

eggNOGCOG5078.
HOGENOMHOG000233455.
InParanoidQ8LGF7.
KOK10689.
OMAHPNIHFK.
PhylomeDBQ8LGF7.

Enzyme and pathway databases

BioCycARA:AT5G25760-MONOMER.
ARA:GQT-755-MONOMER.
UniPathwayUPA00143.

Gene expression databases

GenevestigatorQ8LGF7.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePEX4_ARATH
AccessionPrimary (citable) accession number: Q8LGF7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: October 1, 2002
Last modified: June 11, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names