PEX6_ARATH
ID PEX6_ARATH Reviewed; 941 AA.
AC Q8RY16; Q9SA70;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Peroxisome biogenesis protein 6 {ECO:0000303|PubMed:14745029};
DE AltName: Full=Peroxin-6 {ECO:0000303|PubMed:14745029};
DE Short=AtPEX6 {ECO:0000303|PubMed:14745029};
GN Name=PEX6 {ECO:0000303|PubMed:14745029};
GN OrderedLocusNames=At1g03000 {ECO:0000312|Araport:AT1G03000};
GN ORFNames=F10O3.18 {ECO:0000312|EMBL:AAD25809.1};
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], FUNCTION, AND MUTAGENESIS OF ARG-766.
RX PubMed=14745029; DOI=10.1073/pnas.0304368101;
RA Zolman B.K., Bartel B.;
RT "An Arabidopsis indole-3-butyric acid-response mutant defective in
RT PEROXIN6, an apparent ATPase implicated in peroxisomal function.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:1786-1791(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
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 [5]
RP FUNCTION.
RX PubMed=17544464; DOI=10.1016/j.phytochem.2007.04.024;
RA Delker C., Zolman B.K., Miersch O., Wasternack C.;
RT "Jasmonate biosynthesis in Arabidopsis thaliana requires peroxisomal beta-
RT oxidation enzymes--additional proof by properties of pex6 and aim1.";
RL Phytochemistry 68:1642-1650(2007).
RN [6]
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 [7]
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 [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PEX1 AND APME9.
RX PubMed=21487094; DOI=10.1105/tpc.110.080770;
RA Goto S., Mano S., Nakamori C., Nishimura M.;
RT "Arabidopsis ABERRANT PEROXISOME MORPHOLOGY9 is a peroxin that recruits the
RT PEX1-PEX6 complex to peroxisomes.";
RL Plant Cell 23:1573-1587(2011).
RN [9]
RP FUNCTION.
RX PubMed=20969679; DOI=10.1111/j.1600-0854.2010.01136.x;
RA Ratzel S.E., Lingard M.J., Woodward A.W., Bartel B.;
RT "Reducing PEX13 expression ameliorates physiological defects of late-acting
RT peroxin mutants.";
RL Traffic 12:121-134(2011).
CC -!- FUNCTION: Involved in peroxisomal-targeting signal one (PTS1) and
CC peroxisomal-targeting signal two (PTS2) protein import. Required for
CC jasmonate biosynthesis. Necessary for the developmental elimination of
CC obsolete peroxisome matix proteins. May form heteromeric AAA ATPase
CC complexes required for the import of proteins. May be involved in PEX5
CC recycling. {ECO:0000269|PubMed:14745029, ECO:0000269|PubMed:17478547,
CC ECO:0000269|PubMed:17544464, ECO:0000269|PubMed:19246395,
CC ECO:0000269|PubMed:20969679}.
CC -!- SUBUNIT: Forms a AAA ATPase complex in the cytoplasm with PEX1
CC (PubMed:21487094). Interacts with APME9 (PubMed:21487094).
CC {ECO:0000269|PubMed:21487094}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21487094}.
CC Note=Localizes to the peroxisome when interacting with APEM9.
CC {ECO:0000269|PubMed:21487094}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD25809.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY333116; AAQ90161.1; -; mRNA.
DR EMBL; AC006550; AAD25809.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27513.1; -; Genomic_DNA.
DR EMBL; AY078962; AAL84960.1; -; mRNA.
DR EMBL; BT001151; AAN64542.1; -; mRNA.
DR PIR; F86160; F86160.
DR RefSeq; NP_171799.2; NM_100181.5.
DR AlphaFoldDB; Q8RY16; -.
DR SMR; Q8RY16; -.
DR BioGRID; 24550; 2.
DR STRING; 3702.AT1G03000.1; -.
DR TCDB; 3.A.20.1.2; the peroxisomal protein importer (ppi) family.
DR PaxDb; Q8RY16; -.
DR PRIDE; Q8RY16; -.
DR ProteomicsDB; 236404; -.
DR EnsemblPlants; AT1G03000.1; AT1G03000.1; AT1G03000.
DR GeneID; 839315; -.
DR Gramene; AT1G03000.1; AT1G03000.1; AT1G03000.
DR KEGG; ath:AT1G03000; -.
DR Araport; AT1G03000; -.
DR TAIR; locus:2007574; AT1G03000.
DR eggNOG; KOG0736; Eukaryota.
DR HOGENOM; CLU_000688_0_8_1; -.
DR InParanoid; Q8RY16; -.
DR OMA; VEYSCHN; -.
DR OrthoDB; 233419at2759; -.
DR PhylomeDB; Q8RY16; -.
DR BRENDA; 3.6.4.7; 399.
DR PRO; PR:Q8RY16; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8RY16; baseline and differential.
DR Genevisible; Q8RY16; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP:TAIR.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IMP:TAIR.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Peroxisome biogenesis;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..941
FT /note="Peroxisome biogenesis protein 6"
FT /id="PRO_0000404529"
FT BINDING 384..391
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 698..705
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MUTAGEN 766
FT /note="R->Q: In pex6-1; Loss of sensitivity to exogenous
FT indole-3-butyric acid (IBA)and decreased number of
FT peroxisomes. Larger size of the peroxisomes."
FT /evidence="ECO:0000269|PubMed:14745029"
SQ SEQUENCE 941 AA; 103045 MW; 376F78C8996BD64E CRC64;
MVERRNPLVL SSTRSTLRSV LNSSQPSSAD GDRVLNKDGD LLRGNARLSA GILRWRKDGE
NVSDAKLDSL DDSALVGLST QLLKRLSINS GSLVVVKNIE IGIQRVAQVV VLDPPKTTLE
DASLTQVPVS DSLHTMLVFP TYDLMGQQLL DQEVAYLSPM LAFNLSLHIS CLKSLVHRGN
GVLEKYFEAK CDEEFIGKSA EDGSKIGLDL EPVSQVPGYA SHLRVSFVKI PECGTIPSLK
VNSSFEAEER QGLIDSALQK YFGTDRQLSR GDIFRIYIDW NCGSSICNPC SQRLCSESDD
YIYFKVIAME PSNERFLRVN HSQTALVLGG TVSSGLPPDL LVYRSKVPMP LQEETVNILA
SVLSPPLCPS ALASKLRVAV LLHGIPGCGK RTVVKYVARR LGLHVVEFSC HSLLASSERK
TSTALAQTFN MARRYSPTIL LLRHFDVFKN LGSQDGSLGD RVGVSFEIAS VIRELTEPVS
NGDSSMEEKS NSNFSENEVG KFRGHQVLLI ASAESTEGIS PTIRRCFSHE IRMGSLNDEQ
RSEMLSQSLQ GVSQFLNISS DEFMKGLVGQ TSGFLPRDLQ ALVADAGANL YISQESETKK
INSLSDDLHG VDIHQASQID NSTEKLTAKE DFTKALDRSK KRNASALGAP KVPNVKWDDV
GGLEDVKTSI LDTVQLPLLH KDLFSSGLRK RSGVLLYGPP GTGKTLLAKA VATECSLNFL
SVKGPELINM YIGESEKNVR DIFEKARSAR PCVIFFDELD SLAPARGASG DSGGVMDRVV
SQMLAEIDGL SDSSQDLFII GASNRPDLID PALLRPGRFD KLLYVGVNAD ASYRERVLKA
LTRKFKLSED VSLYSVAKKC PSTFTGADMY ALCADAWFQA AKRKVSKSDS GDMPTEEDDP
DSVVVEYVDF IKAMDQLSPS LSITELKKYE MLRDQFQGRS S
